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Conserved domains on  [gi|294459965|ref|NP_001170899|]
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transient receptor potential cation channel subfamily V member 4 isoform e [Homo sapiens]

Protein Classification

transient-receptor-potential channel family protein( domain architecture ID 1750128)

transient-receptor-potential ion channel protein conducts cations such as calcium into cells; belongs to the Transient Receptor Family (TC. 1.A.4)

Gene Ontology:  GO:0070588|GO:0005262|GO:0070679
SCOP:  4000366
TCDB:  1.A.4

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TRPV super family cl40437
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
103-787 0e+00

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


The actual alignment was detected with superfamily member cd22195:

Pssm-ID: 454755 [Multi-domain]  Cd Length: 733  Bit Score: 1410.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 103 PMDSLFDYGTYRHHSSDNKRWRKKIIEKQPQSPKAPAPQPP-PILKVFNRPILFDIVSRGSTADLDGLLPFLLTHKKRLT 181
Cdd:cd22195    1 PMDSLFDYGTYRQHPTENKRRRKKIIEKKPNINSKAPAPDPpPVLKVFNRPILFDIVSRGSTAELDGLLSFLLSHKKRLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 182 DEEFREPSTGKTCLPKALLNLSNGRNDTIPVLLDIAERTGNMREFINSPFRDIYYRG----------------------- 238
Cdd:cd22195   81 DEEFREPSTGKTCLPKALLNLNNGKNDTIPILLDIAEKTGNLREFINSPFRDVYYRGqtalhiaierrckhyvellvekg 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 239 ------------------------ELPLSLAACTNQPHIVNYLTENPHKKADMRRQDSRGNTVLHALVAIADNTRENTKF 294
Cdd:cd22195  161 advhaqargrffqpkdeggyfyfgELPLSLAACTNQPDIVHYLTENAHKKADLRRQDSRGNTVLHALVAIADNTRENTKF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 295 VTKMYDLLLLKCARLFPDSNLEAVLNNDGLSPLMMAAKTGKIGIFQHIIRREVTDEDTRHLSRKFKDWAYGPVYSSLYDL 374
Cdd:cd22195  241 VTKMYDLLLIKCAKLYPDCNLEAILNNDGMSPLMMAAKLGKIGIFQHIIRREIKDEEARHLSRKFKDWAYGPVYSSLYDL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 375 SSLDTCGEEASVLEILVYNSKIENRHEMLAVEPINELLRDKWRKFGAVSFYINVVSYLCAMVIFTLTAYYQPLEGTPPYP 454
Cdd:cd22195  321 SSLDTCGEEVSVLEILVYNSKIENRHEMLAVEPINELLRDKWRKFGAVSFYISVVSYLVAMIIFTLIAYYRPMEGTPPYP 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 455 YRTTVDYLRLAGEVITLFTGVLFFFTNIKDLFMKKCPGVNSLFIDGSFQLLYFIYSVLVIVSAALYLAGIEAYLAVMVFA 534
Cdd:cd22195  401 YRTTVDYLRLAGEIITLLTGIFFFFTNIKDLFMKKCPGVNSLFIDGSFQLLYFIYSVLVIVTAALYLAGIEAYLAVMVFA 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 535 LVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLLFMIGYASALVSLLNPCANMKVCNEDQTNCTVPTYPSCR 614
Cdd:cd22195  481 LVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLLFMIGYASALVSLLNPCPTKETCKEDSTNCTVPTYPSCR 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 615 DSETFSTFLLDLFKLTIGMGDLEMLSSTKYPVVFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKHIWKLQWATTI 694
Cdd:cd22195  561 DSNTFSKFLLDLFKLTIGMGDLEMLNSAKYPAVFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKQIWKLQWATTI 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 695 LDIERSFPVFLRKAFRSGEMVTVGKSSDGTPDRRWCFRVDEVNWSHWNQNLGIINEDPGKNETYQYYGFSHTVGRLRRDR 774
Cdd:cd22195  641 LDIERSFPVFLRKAFRSGEMVTVGKNLDGTPDRRWCFRVDEVNWSHWNQNLGIINEDPGKNDTYQYYGFSQTVGRLRRDR 720
                        730
                 ....*....|...
gi 294459965 775 WSSVVPRVVELNK 787
Cdd:cd22195  721 WSTVVPRVVELNK 733
 
Name Accession Description Interval E-value
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
103-787 0e+00

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 1410.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 103 PMDSLFDYGTYRHHSSDNKRWRKKIIEKQPQSPKAPAPQPP-PILKVFNRPILFDIVSRGSTADLDGLLPFLLTHKKRLT 181
Cdd:cd22195    1 PMDSLFDYGTYRQHPTENKRRRKKIIEKKPNINSKAPAPDPpPVLKVFNRPILFDIVSRGSTAELDGLLSFLLSHKKRLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 182 DEEFREPSTGKTCLPKALLNLSNGRNDTIPVLLDIAERTGNMREFINSPFRDIYYRG----------------------- 238
Cdd:cd22195   81 DEEFREPSTGKTCLPKALLNLNNGKNDTIPILLDIAEKTGNLREFINSPFRDVYYRGqtalhiaierrckhyvellvekg 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 239 ------------------------ELPLSLAACTNQPHIVNYLTENPHKKADMRRQDSRGNTVLHALVAIADNTRENTKF 294
Cdd:cd22195  161 advhaqargrffqpkdeggyfyfgELPLSLAACTNQPDIVHYLTENAHKKADLRRQDSRGNTVLHALVAIADNTRENTKF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 295 VTKMYDLLLLKCARLFPDSNLEAVLNNDGLSPLMMAAKTGKIGIFQHIIRREVTDEDTRHLSRKFKDWAYGPVYSSLYDL 374
Cdd:cd22195  241 VTKMYDLLLIKCAKLYPDCNLEAILNNDGMSPLMMAAKLGKIGIFQHIIRREIKDEEARHLSRKFKDWAYGPVYSSLYDL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 375 SSLDTCGEEASVLEILVYNSKIENRHEMLAVEPINELLRDKWRKFGAVSFYINVVSYLCAMVIFTLTAYYQPLEGTPPYP 454
Cdd:cd22195  321 SSLDTCGEEVSVLEILVYNSKIENRHEMLAVEPINELLRDKWRKFGAVSFYISVVSYLVAMIIFTLIAYYRPMEGTPPYP 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 455 YRTTVDYLRLAGEVITLFTGVLFFFTNIKDLFMKKCPGVNSLFIDGSFQLLYFIYSVLVIVSAALYLAGIEAYLAVMVFA 534
Cdd:cd22195  401 YRTTVDYLRLAGEIITLLTGIFFFFTNIKDLFMKKCPGVNSLFIDGSFQLLYFIYSVLVIVTAALYLAGIEAYLAVMVFA 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 535 LVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLLFMIGYASALVSLLNPCANMKVCNEDQTNCTVPTYPSCR 614
Cdd:cd22195  481 LVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLLFMIGYASALVSLLNPCPTKETCKEDSTNCTVPTYPSCR 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 615 DSETFSTFLLDLFKLTIGMGDLEMLSSTKYPVVFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKHIWKLQWATTI 694
Cdd:cd22195  561 DSNTFSKFLLDLFKLTIGMGDLEMLNSAKYPAVFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKQIWKLQWATTI 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 695 LDIERSFPVFLRKAFRSGEMVTVGKSSDGTPDRRWCFRVDEVNWSHWNQNLGIINEDPGKNETYQYYGFSHTVGRLRRDR 774
Cdd:cd22195  641 LDIERSFPVFLRKAFRSGEMVTVGKNLDGTPDRRWCFRVDEVNWSHWNQNLGIINEDPGKNDTYQYYGFSQTVGRLRRDR 720
                        730
                 ....*....|...
gi 294459965 775 WSSVVPRVVELNK 787
Cdd:cd22195  721 WSTVVPRVVELNK 733
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
149-752 1.94e-144

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 443.37  E-value: 1.94e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965  149 FNRPILFDIVSRGSTADLDGLLPFLLthkkrltdeefREPSTGKTCLPKALLNLSNGRNDTIPVLLDIAERTGNM----- 223
Cdd:TIGR00870  51 LGRSALFVAAIENENLELTELLLNLS-----------CRGAVGDTLLHAISLEYVDAVEAILLHLLAAFRKSGPLeland 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965  224 -----------------------------------------REFINSPFRDIYYRGELPLSLAACTNQPHIVNYLTENPH 262
Cdd:TIGR00870 120 qytseftpgitalhlaahrqnyeivklllergasvparacgDFFVKSQGVDSFYHGESPLNAAACLGSPSIVALLSEDPA 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965  263 kkaDMRRQDSRGNTVLHALVAIADNTRENTKFVTKMYDLLLLKCARLFPDSNLEAVLNNDGLSPLMMAAKTGKIGIFQHI 342
Cdd:TIGR00870 200 ---DILTADSLGNTLLHLLVMENEFKAEYEELSCQMYNFALSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRLK 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965  343 IRREVTdedtrhlSRKFKDWAYGPVYSSLYDLSSLDTCGEEASVLEILVY---NSKIENRHEMLAVEPINELLRDKWRKF 419
Cdd:TIGR00870 277 LAIKYK-------QKKFVAWPNGQQLLSLYWLEELDGWRRKQSVLELIVVfviGLKFPELSDMYLIAPLSRLGQFKWKPF 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965  420 GAVSFYINVVSYLCAMVIFTLTAYYQP---------LEGTPPY-PYRTTVDYLRLAGEVITLFTGVLFFFTNIKDLFMKk 489
Cdd:TIGR00870 350 IKFIFHSASYLYFLYLIIFTSVAYYRPtrtdlrvtgLQQTPLEmLIVTWVDGLRLGEEKLIWLGGIFEYIHQLWNILDF- 428
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965  490 cpGVNSL----FIDGSFQLLYFIYSVLVIVSAALYLAGIEAYLAVMVFALVLGWMNALYFTRGLKLTGTYSIMIQKILFK 565
Cdd:TIGR00870 429 --GMNSFylatFLDRPFAILFVTQAFLVLREHWLRFDPTLIEEALFAFALVLSWLNLLYIFRGNQHLGPLQIMIGRMILG 506
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965  566 DLFRFLLVYLLFMIGYASALVSLLNPCANMKVcNEDqTNCTVPTypSCRDSETFSTFL---LDLFKLTIGMGDLEMLSST 642
Cdd:TIGR00870 507 DILRFLFIYAVVLFGFACGLNQLYQYYDELKL-NEC-SNPHARS--CEKQGNAYSTLFetsQELFWAIIGLGDLLANEHK 582
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965  643 KYPVVFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKHIWKLQWATTILDIERSFPVFLR-KAFRSGEMVTVG--- 718
Cdd:TIGR00870 583 FTEFVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKLWMSYEREGGTCPPpFNIIPGPKSFVGlfk 662
                         650       660       670
                  ....*....|....*....|....*....|....*.
gi 294459965  719 --KSSDGTPDRRWCFRVDEVNWSHWNQNLGIINEDP 752
Cdd:TIGR00870 663 riEKHDGKKRQRWCRRVEEVNWTTWERKAETLIEDG 698
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
511-683 1.20e-13

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 71.14  E-value: 1.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965  511 VLVIVSAALYLAGIEAYLAVMVFALVLGWMNALYFTRGLKLTGTYSIMIQKILfKDLFRFLLVYLLFMIGYASALVSLLN 590
Cdd:pfam00520  74 VVVLPSLISLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSL-KSLGNLLLLLLLFLFIFAIIGYQLFG 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965  591 PCANMKV-CNEDQTNCTvpTYPSCrdsetfstfLLDLFKL--TIGMGD-LEMLSSTKYPVVFIILLVTYIILTFVLLLNM 666
Cdd:pfam00520 153 GKLKTWEnPDNGRTNFD--NFPNA---------FLWLFQTmtTEGWGDiMYDTIDGKGEFWAYIYFVSFIILGGFLLLNL 221
                         170
                  ....*....|....*..
gi 294459965  667 LIALMGETVGQVSKESK 683
Cdd:pfam00520 222 FIAVIIDNFQELTERTE 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
198-345 8.33e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.57  E-value: 8.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 198 ALLNLSNGRNDTIPVLLDIAERTGN---MREFINSPFrDIYYR---GELPLSLAACTNQPHIVNYLTEnphKKADMRRQD 271
Cdd:COG0666   75 AAGADINAKDDGGNTLLHAAARNGDleiVKLLLEAGA-DVNARdkdGETPLHLAAYNGNLEIVKLLLE---AGADVNAQD 150
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 294459965 272 SRGNTVLHAlvAIADNtreNTKFVtkmyDLLLLKCArlfpdsNLEAVlNNDGLSPLMMAAKTGKIGIFQHIIRR 345
Cdd:COG0666  151 NDGNTPLHL--AAANG---NLEIV----KLLLEAGA------DVNAR-DNDGETPLHLAAENGHLEIVKLLLEA 208
 
Name Accession Description Interval E-value
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
103-787 0e+00

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 1410.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 103 PMDSLFDYGTYRHHSSDNKRWRKKIIEKQPQSPKAPAPQPP-PILKVFNRPILFDIVSRGSTADLDGLLPFLLTHKKRLT 181
Cdd:cd22195    1 PMDSLFDYGTYRQHPTENKRRRKKIIEKKPNINSKAPAPDPpPVLKVFNRPILFDIVSRGSTAELDGLLSFLLSHKKRLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 182 DEEFREPSTGKTCLPKALLNLSNGRNDTIPVLLDIAERTGNMREFINSPFRDIYYRG----------------------- 238
Cdd:cd22195   81 DEEFREPSTGKTCLPKALLNLNNGKNDTIPILLDIAEKTGNLREFINSPFRDVYYRGqtalhiaierrckhyvellvekg 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 239 ------------------------ELPLSLAACTNQPHIVNYLTENPHKKADMRRQDSRGNTVLHALVAIADNTRENTKF 294
Cdd:cd22195  161 advhaqargrffqpkdeggyfyfgELPLSLAACTNQPDIVHYLTENAHKKADLRRQDSRGNTVLHALVAIADNTRENTKF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 295 VTKMYDLLLLKCARLFPDSNLEAVLNNDGLSPLMMAAKTGKIGIFQHIIRREVTDEDTRHLSRKFKDWAYGPVYSSLYDL 374
Cdd:cd22195  241 VTKMYDLLLIKCAKLYPDCNLEAILNNDGMSPLMMAAKLGKIGIFQHIIRREIKDEEARHLSRKFKDWAYGPVYSSLYDL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 375 SSLDTCGEEASVLEILVYNSKIENRHEMLAVEPINELLRDKWRKFGAVSFYINVVSYLCAMVIFTLTAYYQPLEGTPPYP 454
Cdd:cd22195  321 SSLDTCGEEVSVLEILVYNSKIENRHEMLAVEPINELLRDKWRKFGAVSFYISVVSYLVAMIIFTLIAYYRPMEGTPPYP 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 455 YRTTVDYLRLAGEVITLFTGVLFFFTNIKDLFMKKCPGVNSLFIDGSFQLLYFIYSVLVIVSAALYLAGIEAYLAVMVFA 534
Cdd:cd22195  401 YRTTVDYLRLAGEIITLLTGIFFFFTNIKDLFMKKCPGVNSLFIDGSFQLLYFIYSVLVIVTAALYLAGIEAYLAVMVFA 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 535 LVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLLFMIGYASALVSLLNPCANMKVCNEDQTNCTVPTYPSCR 614
Cdd:cd22195  481 LVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLLFMIGYASALVSLLNPCPTKETCKEDSTNCTVPTYPSCR 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 615 DSETFSTFLLDLFKLTIGMGDLEMLSSTKYPVVFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKHIWKLQWATTI 694
Cdd:cd22195  561 DSNTFSKFLLDLFKLTIGMGDLEMLNSAKYPAVFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKQIWKLQWATTI 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 695 LDIERSFPVFLRKAFRSGEMVTVGKSSDGTPDRRWCFRVDEVNWSHWNQNLGIINEDPGKNETYQYYGFSHTVGRLRRDR 774
Cdd:cd22195  641 LDIERSFPVFLRKAFRSGEMVTVGKNLDGTPDRRWCFRVDEVNWSHWNQNLGIINEDPGKNDTYQYYGFSQTVGRLRRDR 720
                        730
                 ....*....|...
gi 294459965 775 WSSVVPRVVELNK 787
Cdd:cd22195  721 WSTVVPRVVELNK 733
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
163-736 0e+00

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 878.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 163 TADLDGLLPFLLTHKKRLTDEEFREPSTGKTCLPKALLNLSNGRNDTIPVLLDIAERTGNMREFINSPFRDIYYRG---- 238
Cdd:cd22193    1 LEELLGFLQDLCRRRKDLTDSEFTESSTGKTCLMKALLNLNPGTNDTIRILLDIAEKTDNLKRFINAEYTDEYYEGqtal 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 239 -------------------------------------------ELPLSLAACTNQPHIVNYLTENPHKKADMRRQDSRGN 275
Cdd:cd22193   81 hiaierrqgdivallvengadvhahakgrffqpkyqgegfyfgELPLSLAACTNQPDIVQYLLENEHQPADIEAQDSRGN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 276 TVLHALVAIADNTRENTKFVTKMYDLLLLKCARLFPDSNLEAVLNNDGLSPLMMAAKTGKIGIFQHIIRREVTDEDTRHL 355
Cdd:cd22193  161 TVLHALVTVADNTKENTKFVTRMYDMILIRGAKLCPTVELEEIRNNDGLTPLQLAAKMGKIEILKYILQREIKEPELRHL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 356 SRKFKDWAYGPVYSSLYDLSSLDTCGEEaSVLEILVYNSKIENRHEMLAVEPINELLRDKWRKFGAVSFYINVVSYLCAM 435
Cdd:cd22193  241 SRKFTDWAYGPVSSSLYDLSNVDTCEKN-SVLEIIVYNSKIDNRHEMLTLEPLNTLLQDKWDKFAKYMFFFSFCFYLFYM 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 436 VIFTLTAYYQPLEGTPPYP--YRTTVDYLRLAGEVITLFTGVLFFFTNIKDLFMKKCPGVNSlFIDGSFQLLYFIYSVLV 513
Cdd:cd22193  320 IIFTLVAYYRPREDEPPPPlaKTTKMDYMRLLGEILVLLGGVYFFVKEIAYFLLRRSDLQSS-FSDSYFEILFFVQAVLV 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 514 IVSAALYLAGIEAYLAVMVFALVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLLFMIGYASALVSLLNPCA 593
Cdd:cd22193  399 ILSVVLYLFAYKEYLACLVLALALGWANMLYYTRGFQSMGIYSVMIQKVILRDLLRFLFVYLLFLFGFAVALVSLIEKCS 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 594 NMKVCnedqtnctvptypsCRDSETFSTFLLDLFKLTIGMGDLEMLSSTKYPVVFIILLVTYIILTFVLLLNMLIALMGE 673
Cdd:cd22193  479 SDKKD--------------CSSYGSFSDAVLELFKLTIGMGDLEFQENSTYPAVFLILLLTYVILTFVLLLNMLIALMGE 544
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 294459965 674 TVGQVSKESKHIWKLQWATTILDIERSFPVFLRKAFRSGEMVTVGKSSDGTPDRRWCFRVDEV 736
Cdd:cd22193  545 TVNNVSKESKRIWKLQRAITILEFEKSFPECMRKAFRSGRLLKVGLCKDGTPDFRWCFRVDEV 607
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
147-749 0e+00

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 788.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 147 KVFNRPILFDIVSRGSTADLDGLLPFLLTHKKRLTDEEFREPSTGKTCLPKALLNLSNGRNDTIPVLLDIAERTGNMREF 226
Cdd:cd22196    3 KLYDRRRIFDAVAKGDCKELDGLLEYLMRTKKRLTDSEFKDPETGKTCLLKAMLNLHNGQNDTISLLLDIAEKTGNLKEF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 227 INSPFRDIYYRG-----------------------------------------------ELPLSLAACTNQPHIVNYLTE 259
Cdd:cd22196   83 VNAAYTDSYYKGqtalhiaierrnmhlvellvqngadvharasgeffkkkkggpgfyfgELPLSLAACTNQLDIVKFLLE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 260 NPHKKADMRRQDSRGNTVLHALVAIADNTRENTKFVTKMYDLLLLKCARLFPDSNLEAVLNNDGLSPLMMAAKTGKIGIF 339
Cdd:cd22196  163 NPHSPADISARDSMGNTVLHALVEVADNTPENTKFVTKMYNEILILGAKIRPLLKLEEITNKKGLTPLKLAAKTGKIGIF 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 340 QHIIRREVTDEDTRHLSRKFKDWAYGPVYSSLYDLSSLDTCgEEASVLEILVYNSKIENRHEMLAVEPINELLRDKWRKF 419
Cdd:cd22196  243 AYILGREIKEPECRHLSRKFTEWAYGPVHSSLYDLSSIDTY-EKNSVLEIIAYSSETPNRHEMLLVEPLNKLLQDKWDKF 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 420 GAVSFYINVVSYLCAMVIFTLTAYYQPLEGTPPYPYR-TTVDYLRLAGEVITLFTGVLFFFTNIKDlFMKKCPGVNSLFI 498
Cdd:cd22196  322 VKRIFYFNFFVYFIYMIIFTLAAYYRPVNKTPPFPIEnTTGEYLRLTGEIISVSGGVYFFFRGIQY-FLQRRPSLKKLIV 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 499 DGSFQLLYFIYSVLVIVSAALYLAGIEAYLAVMVFALVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLLFM 578
Cdd:cd22196  401 DSYCEILFFVQSLFLLASTVLYFCGRNEYVAFMVISLALGWANVLYYTRGFQQMGIYSVMIQKMILRDICRFLFVYLVFL 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 579 IGYASALVSLL---NPCANMKV-CNEDQTNCTVPTYPScrdseTFSTFlLDLFKLTIGMGDLEMLSSTKYPVVFIILLVT 654
Cdd:cd22196  481 FGFSAALVTLIedgPPKGDVNTsQKECVCKSGYNSYNS-----LYSTC-LELFKFTIGMGDLEFTENYKFKEVFIFLLIS 554
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 655 YIILTFVLLLNMLIALMGETVGQVSKESKHIWKLQWATTILDIERSFPVFLRKAFRSGEMVTVGKSSDGTPDRRWCFRVD 734
Cdd:cd22196  555 YVILTYILLLNMLIALMGETVSKIAQESKNIWKLQRAITILDLEKSLLRCLRDRFRSGKSVLVGITPDGKEDYRWCFRVD 634
                        650
                 ....*....|....*
gi 294459965 735 EVNWSHWNQNLGIIN 749
Cdd:cd22196  635 EVNWNKWNTNLGIIN 649
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
146-736 0e+00

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 623.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 146 LKVFNRPILFDIVSRGSTADLDGLLPFLLTHKKRLTDEEFREPSTGKTCLPKALLNLSNGRNDTIPVLLDIAERTGNMRE 225
Cdd:cd22197    2 PNRFDRDRLFSVVSRGNPEELAGLLEYLRRTSKYLTDSEYTEGSTGKTCLMKAVLNLQDGVNACIMPLLEIDKDSGNPKP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 226 FINSPFRDIYYRG----------------------------------------------ELPLSLAACTNQPHIVNYLTE 259
Cdd:cd22197   82 LVNAQCTDEYYRGhsalhiaiekrslqcvkllvengadvharacgrffqkkqgtcfyfgELPLSLAACTKQWDVVNYLLE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 260 NPHKKADMRRQDSRGNTVLHALVAIADNTRENTKFVTKMYDLLLLKCARLFPDSNLEAVLNNDGLSPLMMAAKTGKIGIF 339
Cdd:cd22197  162 NPHQPASLQAQDSLGNTVLHALVMIADNSPENSALVIKMYDGLLQAGARLCPTVQLEEISNHEGLTPLKLAAKEGKIEIF 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 340 QHIIRREVTDEdTRHLSRKFKDWAYGPVYSSLYDLSSLDTcGEEASVLEILVYNSKIENRHEMLAVEPINELLRDKWRKF 419
Cdd:cd22197  242 RHILQREFSGP-YQHLSRKFTEWCYGPVRVSLYDLSSVDS-WEKNSVLEIIAFHSKSPNRHRMVVLEPLNKLLQEKWDRL 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 420 GAVsFYINVVSYLCAMVIFTLTAYYQPLEGTPPYPYR--TTVDYLRLAGEVITLFTGVLFFFTNIKdLFMKKCPGVNSLF 497
Cdd:cd22197  320 VSR-FYFNFLCYLVYMFIFTVVAYHQPLLDQPPIPPLkaTAGGSMLLLGHILILLGGIYLLLGQLW-YFWRRRLFIWISF 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 498 IDGSFQLLYFIYSVLVIVSAALYLAGIEAYLAVMVFALVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLLF 577
Cdd:cd22197  398 MDSYFEILFLLQALLTVLSQVLYFMGSEWYLPLLVFSLVLGWLNLLYYTRGFQHTGIYSVMIQKVILRDLLRFLLVYLVF 477
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 578 MIGYASALVSLLNPCANMKVcNEDQTNCTVPTYPSCRDSE--TFSTFL---LDLFKLTIGMGDLEMLSSTKYPVVFIILL 652
Cdd:cd22197  478 LFGFAVALVSLSREAPSPKA-PEDNNSTVTEQPTVGQEEEpaPYRSILdasLELFKFTIGMGELAFQEQLRFRGVVLLLL 556
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 653 VTYIILTFVLLLNMLIALMGETVGQVSKESKHIWKLQWATTILDIERSFPVFLRKAFRSGEMVTVGKSSDGTPDRRWCFR 732
Cdd:cd22197  557 LAYVLLTYVLLLNMLIALMSETVNHVADNSWSIWKLQKAISVLEMENGYWWCRRKKQREGRLLTVGTRPDGTPDERWCFR 636

                 ....
gi 294459965 733 VDEV 736
Cdd:cd22197  637 VEEM 640
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
150-754 0e+00

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 611.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 150 NRPI--LFDIVSRGSTADLDGLLP--------FLLTHKKRLTDEEFREPSTGKTCLPKALLNLSNGRNDTIPVLLDIAER 219
Cdd:cd22194   43 QRDKkkRLKKVSEAAVEELGELLKelkdlsrrRRKTDVPDFLMHKLTASDTGKTCLMKALLNINENTKEIVRILLAFAEE 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 220 TGNMREFINSPFR-----------------------------------------------DIYYRGELPLSLAACTNQPH 252
Cdd:cd22194  123 NGILDRFINAEYTeeayegqtalniaierrqgdivklliakgadvnahakgvffnpkykhEGFYFGETPLALAACTNQPE 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 253 IVNYLTENPHKKADMrrQDSRGNTVLHALVAIADNTRENTKFVTKMYDLLLLKCArlfpDSNLEAVLNNDGLSPLMMAAK 332
Cdd:cd22194  203 IVQLLMEKESTDITS--QDSRGNTVLHALVTVAEDSKTQNDFVKRMYDMILLKSE----NKNLETIRNNEGLTPLQLAAK 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 333 TGKIGIFQHIIRREVTDEDTRHLSRKFKDWAYGPVYSSLYDLSSLDTCgEEASVLEILVYNSKIENRHEMLAVEPINELL 412
Cdd:cd22194  277 MGKAEILKYILSREIKEKPNRSLSRKFTDWAYGPVSSSLYDLTNVDTT-TDNSVLEIIVYNTNIDNRHEMLTLEPLHTLL 355
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 413 RDKWRKFGAVSFYINVVSYLCAMVIFTLTAYYQPLEGT-PPYPYR--TTVDYLRLAGEVITLFTGVLFFFTNIKDLFMKK 489
Cdd:cd22194  356 HMKWKKFARYMFFISFLFYFFYNITLTLVSYYRPREDEdPPHPLAlsHKMGWLQLLGQMFVLIWATCLSVKEGIAIFLLR 435
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 490 CPGVNSLFIDGSFQLLYFIYSVLVIVSAALYLAGIEAYLAVMVFALVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFR 569
Cdd:cd22194  436 PSDLKSILSDAWFHILFFIQAVLVIVSVFLYLFAYKEYLACLVLAMALGWANMLYYTRGFQSLGIYSVMIQKVILNDVLK 515
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 570 FLLVYLLFMIGYASALVSLLNPCanmkvcnedqtnctvPTYPSCRDSETFSTFLLDLFKLTIGMGDLEMLSSTKYPVVFI 649
Cdd:cd22194  516 FLLVYILFLLGFGVALASLIEDC---------------PDDSECSSYGSFSDAVLELFKLTIGLGDLEIQQNSKYPILFL 580
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 650 ILLVTYIILTFVLLLNMLIALMGETVGQVSKESKHIWKLQWATTILDIERSFPVFLRKAFRSGEMVTVGKSsdgtpDRRW 729
Cdd:cd22194  581 LLLITYVILTFVLLLNMLIALMGETVENVSKESERIWRLQRARTILEFEKSLPEWLRKRFRLGELCKVADE-----DFRL 655
                        650       660
                 ....*....|....*....|....*
gi 294459965 730 CFRVDEVNWSHWNQNLGIINEDPGK 754
Cdd:cd22194  656 CLRINEVKWTEWKTHVSCLNEDPGP 680
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
166-736 0e+00

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 596.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 166 LDGLLPFLLTHKKRLTDEEFREPSTGKTCLPKALLNLSNGRNDTIPVLLDIAERTGNMREFINSPFRDIYYRG------- 238
Cdd:cd21882    1 LEELLGLLECLRWYLTDSAYQRGATGKTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPKELVNAPCTDEFYQGqtalhia 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 239 ---------------------------------------ELPLSLAACTNQPHIVNYLTENPHKKADMRRQDSRGNTVLH 279
Cdd:cd21882   81 ienrnlnlvrllvengadvsaratgrffrkspgnlfyfgELPLSLAACTNQEEIVRLLLENGAQPAALEAQDSLGNTVLH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 280 ALVAIADNTRENTKFVTKMYDLLLLKCARLFPDSNLEAVLNNDGLSPLMMAAKTGKIGIFQHIIRREVTdEDTRHLSRKF 359
Cdd:cd21882  161 ALVLQADNTPENSAFVCQMYNLLLSYGAHLDPTQQLEEIPNHQGLTPLKLAAVEGKIVMFQHILQREFS-GPYQPLSRKF 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 360 KDWAYGPVYSSLYDLSSLDTCGEEaSVLEILVYNSKIENRHEMLAVEPINELLRDKWRKFGAVSFYINVVSYLCAMVIFT 439
Cdd:cd21882  240 TEWTYGPVTSSLYDLSEIDSWEKN-SVLELIAFSKKREARHQMLVQEPLNELLQEKWDRYGRPYFCFNFACYLLYMIIFT 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 440 LTAYYQPLEGTPPYP--YRTTVDYLRLAGEVITLFTGVLFFFTNIKDLFMKKcPGVNSLFIDGSFQLLYFIYSVLVIVSA 517
Cdd:cd21882  319 VCAYYRPLKDRPANQeaKATFGDSIRLVGEILTVLGGVYILLGEIPYFFRRR-LSRWFGFLDSYFEILFITQALLVLLSM 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 518 ALYLAGIEAYLAVMVFALVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLLFMIGYASALVSLLNpcanmkv 597
Cdd:cd21882  398 VLRFMETEGYVVPLVFSLVLGWCNVLYYTRGFQMLGIYTVMIQKMILRDLMRFCWVYLVFLFGFASAFVILFQ------- 470
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 598 cNEDqtnctvptYPSCRDSETFSTFLLDLFKLTIGMGDLEMLSSTKYPVVFIILLVTYIILTFVLLLNMLIALMGETVGQ 677
Cdd:cd21882  471 -TED--------PNKLGEFRDYPDALLELFKFTIGMGDLPFNENVDFPFVYLILLLAYVILTYLLLLNMLIALMGETVNR 541
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 294459965 678 VSKESKHIWKLQWATTILDIERSFPVFLRKAFRSGEMVTVGKSSDGTPDRRWCFRVDEV 736
Cdd:cd21882  542 VAQESDEIWKLQKAITTLMLERKYPRCLRKRSREGRLLKVGCGGDGGLDDRWCFRVEEV 600
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
149-752 1.94e-144

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 443.37  E-value: 1.94e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965  149 FNRPILFDIVSRGSTADLDGLLPFLLthkkrltdeefREPSTGKTCLPKALLNLSNGRNDTIPVLLDIAERTGNM----- 223
Cdd:TIGR00870  51 LGRSALFVAAIENENLELTELLLNLS-----------CRGAVGDTLLHAISLEYVDAVEAILLHLLAAFRKSGPLeland 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965  224 -----------------------------------------REFINSPFRDIYYRGELPLSLAACTNQPHIVNYLTENPH 262
Cdd:TIGR00870 120 qytseftpgitalhlaahrqnyeivklllergasvparacgDFFVKSQGVDSFYHGESPLNAAACLGSPSIVALLSEDPA 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965  263 kkaDMRRQDSRGNTVLHALVAIADNTRENTKFVTKMYDLLLLKCARLFPDSNLEAVLNNDGLSPLMMAAKTGKIGIFQHI 342
Cdd:TIGR00870 200 ---DILTADSLGNTLLHLLVMENEFKAEYEELSCQMYNFALSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRLK 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965  343 IRREVTdedtrhlSRKFKDWAYGPVYSSLYDLSSLDTCGEEASVLEILVY---NSKIENRHEMLAVEPINELLRDKWRKF 419
Cdd:TIGR00870 277 LAIKYK-------QKKFVAWPNGQQLLSLYWLEELDGWRRKQSVLELIVVfviGLKFPELSDMYLIAPLSRLGQFKWKPF 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965  420 GAVSFYINVVSYLCAMVIFTLTAYYQP---------LEGTPPY-PYRTTVDYLRLAGEVITLFTGVLFFFTNIKDLFMKk 489
Cdd:TIGR00870 350 IKFIFHSASYLYFLYLIIFTSVAYYRPtrtdlrvtgLQQTPLEmLIVTWVDGLRLGEEKLIWLGGIFEYIHQLWNILDF- 428
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965  490 cpGVNSL----FIDGSFQLLYFIYSVLVIVSAALYLAGIEAYLAVMVFALVLGWMNALYFTRGLKLTGTYSIMIQKILFK 565
Cdd:TIGR00870 429 --GMNSFylatFLDRPFAILFVTQAFLVLREHWLRFDPTLIEEALFAFALVLSWLNLLYIFRGNQHLGPLQIMIGRMILG 506
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965  566 DLFRFLLVYLLFMIGYASALVSLLNPCANMKVcNEDqTNCTVPTypSCRDSETFSTFL---LDLFKLTIGMGDLEMLSST 642
Cdd:TIGR00870 507 DILRFLFIYAVVLFGFACGLNQLYQYYDELKL-NEC-SNPHARS--CEKQGNAYSTLFetsQELFWAIIGLGDLLANEHK 582
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965  643 KYPVVFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKHIWKLQWATTILDIERSFPVFLR-KAFRSGEMVTVG--- 718
Cdd:TIGR00870 583 FTEFVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKLWMSYEREGGTCPPpFNIIPGPKSFVGlfk 662
                         650       660       670
                  ....*....|....*....|....*....|....*.
gi 294459965  719 --KSSDGTPDRRWCFRVDEVNWSHWNQNLGIINEDP 752
Cdd:TIGR00870 663 riEKHDGKKRQRWCRRVEEVNWTTWERKAETLIEDG 698
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
234-737 5.33e-109

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 346.61  E-value: 5.33e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 234 IYYrGELPLSLAACTNQPHIVNYLTENphkKADMRRQDSRGNTVLHALVAIAdntreNTKFVTKMYDLLLLKCARLFPDS 313
Cdd:cd22192  133 IYY-GEHPLSFAACVGNEEIVRLLIEH---GADIRAQDSLGNTVLHILVLQP-----NKTFACQMYDLILSYDKEDDLQP 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 314 nLEAVLNNDGLSPLMMAAKTGKIGIFQHIIRRevtdedtrhlsRKFKDWAYGPVYSSLYDLSSLDTCGEEASVLEILVYN 393
Cdd:cd22192  204 -LDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK-----------RRHIQWTYGPLTSTLYDLTEIDSWGDEQSVLELIVSS 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 394 SKIENRHeMLAVEPINELLRDKWRKFGAVSFYINVVSYLCAMVIFTLTAYYQPLEgtpPYP------------------- 454
Cdd:cd22192  272 KKREARK-ILDVTPVKELVSLKWKRYGRPYFRILALLYLLYIIIFTLCCVYRPLK---PRPenntdprditlyvqktlqe 347
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 455 -YRTTVDYLRLAGEVITLFTGVLFFFTNIKDLF---MKKCPGVNSLfiDGSFQLLYFIYSVLVIVSAALYLAGIEAYLAV 530
Cdd:cd22192  348 sYVTPKDYLRLVGELISVLGAIVILLLEIPDILrvgVKRYFGQTVL--GGPFHVIIITYACLVLLTLVLRLTSLSGEVVP 425
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 531 MVFALVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLLFMIGYASALvsllnpcanMKVCNEDQTNCTVPTY 610
Cdd:cd22192  426 MSLALVLGWCNVMYFARGFQMLGPFTIMIQKIIFGDLMKFCWLMFVVILGFSSAF---------YMIFQTEDPDSLGHFY 496
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 611 PscrdsetFSTFLLDLFKLTIGMGDLEMLSSTKYPVVFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKHIWKLQW 690
Cdd:cd22192  497 D-------FPMTLFSTFELFLGLIDGPANYTVDLPFMYKVLYTAFAVIAYLLMLNLLIAMMGDTHWRVAHERDELWRAQV 569
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 294459965 691 ATTILDIERSFPVFLRKafRSGemvTVGKsSDGTPDrRWCFRVDEVN 737
Cdd:cd22192  570 VATTLMLERRLPRCLWP--RSG---ICGK-EYGLGD-RWYLRVEDRN 609
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
511-683 1.20e-13

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 71.14  E-value: 1.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965  511 VLVIVSAALYLAGIEAYLAVMVFALVLGWMNALYFTRGLKLTGTYSIMIQKILfKDLFRFLLVYLLFMIGYASALVSLLN 590
Cdd:pfam00520  74 VVVLPSLISLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSL-KSLGNLLLLLLLFLFIFAIIGYQLFG 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965  591 PCANMKV-CNEDQTNCTvpTYPSCrdsetfstfLLDLFKL--TIGMGD-LEMLSSTKYPVVFIILLVTYIILTFVLLLNM 666
Cdd:pfam00520 153 GKLKTWEnPDNGRTNFD--NFPNA---------FLWLFQTmtTEGWGDiMYDTIDGKGEFWAYIYFVSFIILGGFLLLNL 221
                         170
                  ....*....|....*..
gi 294459965  667 LIALMGETVGQVSKESK 683
Cdd:pfam00520 222 FIAVIIDNFQELTERTE 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
198-345 8.33e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.57  E-value: 8.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 198 ALLNLSNGRNDTIPVLLDIAERTGN---MREFINSPFrDIYYR---GELPLSLAACTNQPHIVNYLTEnphKKADMRRQD 271
Cdd:COG0666   75 AAGADINAKDDGGNTLLHAAARNGDleiVKLLLEAGA-DVNARdkdGETPLHLAAYNGNLEIVKLLLE---AGADVNAQD 150
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 294459965 272 SRGNTVLHAlvAIADNtreNTKFVtkmyDLLLLKCArlfpdsNLEAVlNNDGLSPLMMAAKTGKIGIFQHIIRR 345
Cdd:COG0666  151 NDGNTPLHL--AAANG---NLEIV----KLLLEAGA------DVNAR-DNDGETPLHLAAENGHLEIVKLLLEA 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
242-343 1.73e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.95  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965  242 LSLAACTNQPHIVNYLTENPHkkaDMRRQDSRGNTVLHAlvAIADNTRENTKfvtkmydlLLLKcarlFPDSNLeavlNN 321
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGA---DANLQDKNGRTALHL--AAKNGHLEIVK--------LLLE----HADVNL----KD 59
                          90       100
                  ....*....|....*....|..
gi 294459965  322 DGLSPLMMAAKTGKIGIFQHII 343
Cdd:pfam12796  60 NGRTALHYAARSGHLEIVKLLL 81
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
237-345 2.02e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 47.26  E-value: 2.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459965 237 RGELPLSLAACTNQPHIVNYLTENphkKADMRRQDSRGNTVLHAlvAIADNTRENTKfvtkmydLLLLKCArlfpDSNLE 316
Cdd:COG0666  152 DGNTPLHLAAANGNLEIVKLLLEA---GADVNARDNDGETPLHL--AAENGHLEIVK-------LLLEAGA----DVNAK 215
                         90       100
                 ....*....|....*....|....*....
gi 294459965 317 avlNNDGLSPLMMAAKTGKIGIFQHIIRR 345
Cdd:COG0666  216 ---DNDGKTALDLAAENGNLEIVKLLLEA 241
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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