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Conserved domains on  [gi|214010185|ref|NP_001135750|]
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amyloid beta precursor like protein 2 isoform 4 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
APP_E2 pfam12925
E2 domain of amyloid precursor protein; The E2 domain is the largest of the conserved domains ...
 136-318 4.89e-90

E2 domain of amyloid precursor protein; The E2 domain is the largest of the conserved domains of the amyloid precursor protein. The structure of E2 consists of two coiled-coil sub-structures connected through a continuous helix, and bears an unexpected resemblance to the spectrin family of protein structures.E 2 can reversibly dimerize in solution, and the dimerization occurs along the longest dimension of the molecule in an antiparallel orientation, which enables the N-terminal substructure of one monomer to pack against the C-terminal substructure of a second monomer. The high degree of conservation of residues at the putative dimer interface suggests that the E2 dimer observed in the crystal could be physiologically relevant. Heparin sulfate proteoglycans, the putative ligands for the precursor present in extracellular matrix, bind to E2 at a conserved and positively charged site near the dimer interface.


:

Pssm-ID: 463752  Cd Length: 190  Bit Score: 273.84  E-value: 4.89e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010185  136 PPTPLPTNDVDVYFETSADDNEHARFQKAKEQLEIRHRNRMDRVKKEWEEAELQAKNLPKAE-------RQTLIQHFQAM 208
Cdd:pfam12925   1 TTTPPPTDAVDPYFEHPDPRNEHESFKKAKKRLEEKHRERMTKVMKEWEEAEERYQNLPKADpkaaekfKKAMTARFQET 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010185  209 VKALEKEAASEKQQLVETHLARVEAMLNDRRRMALENYLAALQSDPPRPHRILQALRRYVRAENKDRLHTIRHYQHVLAV 288
Cdd:pfam12925  81 VEALEEEAAAERQQLVETHQQRVEAHLNDRRRDALECYLQALQENPPNPHRILKALKKLLRAEQKDRRHTLRHYRHLLAS 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 214010185  289 DPEKAAQMKSQVMTHLHVIEERRNQSLSLL 318
Cdd:pfam12925 161 DPEKAEQMKPQVLTHLRVIDRRMNQSLTLL 190
JMTM_APLP2 cd21709
juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 2 (APLP-2) and ...
 439-519 2.88e-53

juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 2 (APLP-2) and similar proteins; Amyloid-like protein 2 (APLP-2), also called amyloid protein homolog (APPH), or CDEI box-binding protein (CDEBP), may play a role in the regulation of hemostasis. Its soluble form may have inhibitory properties towards coagulation factors. APLP-2 may bind to the DNA 5'-GTCACATG-3'(CDEI box). It inhibits trypsin, chymotrypsin, plasmin, factor XIA, and plasma and glandular kallikrein. This model corresponds to juxtamembrane and transmembrane (JMTM) domain of APLP-2, which consists of the intact transmembrane (TM) domain with adjacent N-terminal juxtamembrane (JM) region.


:

Pssm-ID: 411992  Cd Length: 81  Bit Score: 174.73  E-value: 2.88e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010185 439 SVGPLREDFSLSSSALIGLLVIAVAIATVIVISLVMLRKRQYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLE 518
Cdd:cd21709    1 SDGPLRDDFSFSSSALIGLLVIAVAIATVIVISLVLLRKRQYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLE 80


                 .
gi 214010185 519 Q 519
Cdd:cd21709   81 Q 81
A4_EXTRA super family cl30964
amyloid A4; amyloid A4 precursor of Alzheimers disease
 42-137 5.22e-53

amyloid A4; amyloid A4 precursor of Alzheimers disease


The actual alignment was detected with superfamily member smart00006:

Pssm-ID: 128326 [Multi-domain]  Cd Length: 165  Bit Score: 176.92  E-value: 5.22e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010185    42 GTGFAVAEPQIAMFCGKLNMHVNIQTGKWEPDPTGTKSCFETKEEVLQYCQEMYPELQITNVMEANQRVSIDNWCRRDKK 121
Cdd:smart00006   1 GAAGALAEPQIAMLCGRLNMHMNVQTGRWETDPSRTKTCLRDKEDILQYCRKAYPELQITNVVEASQPVTIQNWCRRGRS 80

                           90
                   ....*....|....*...
gi 214010185   122 QCKS--RFVTPFKCLVPP 137
Cdd:smart00006  81 QCKThhHFVIPFRCLVGE 98
 
Name Accession Description Interval E-value
APP_E2 pfam12925
E2 domain of amyloid precursor protein; The E2 domain is the largest of the conserved domains ...
 136-318 4.89e-90

E2 domain of amyloid precursor protein; The E2 domain is the largest of the conserved domains of the amyloid precursor protein. The structure of E2 consists of two coiled-coil sub-structures connected through a continuous helix, and bears an unexpected resemblance to the spectrin family of protein structures.E 2 can reversibly dimerize in solution, and the dimerization occurs along the longest dimension of the molecule in an antiparallel orientation, which enables the N-terminal substructure of one monomer to pack against the C-terminal substructure of a second monomer. The high degree of conservation of residues at the putative dimer interface suggests that the E2 dimer observed in the crystal could be physiologically relevant. Heparin sulfate proteoglycans, the putative ligands for the precursor present in extracellular matrix, bind to E2 at a conserved and positively charged site near the dimer interface.


Pssm-ID: 463752  Cd Length: 190  Bit Score: 273.84  E-value: 4.89e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010185  136 PPTPLPTNDVDVYFETSADDNEHARFQKAKEQLEIRHRNRMDRVKKEWEEAELQAKNLPKAE-------RQTLIQHFQAM 208
Cdd:pfam12925   1 TTTPPPTDAVDPYFEHPDPRNEHESFKKAKKRLEEKHRERMTKVMKEWEEAEERYQNLPKADpkaaekfKKAMTARFQET 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010185  209 VKALEKEAASEKQQLVETHLARVEAMLNDRRRMALENYLAALQSDPPRPHRILQALRRYVRAENKDRLHTIRHYQHVLAV 288
Cdd:pfam12925  81 VEALEEEAAAERQQLVETHQQRVEAHLNDRRRDALECYLQALQENPPNPHRILKALKKLLRAEQKDRRHTLRHYRHLLAS 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 214010185  289 DPEKAAQMKSQVMTHLHVIEERRNQSLSLL 318
Cdd:pfam12925 161 DPEKAEQMKPQVLTHLRVIDRRMNQSLTLL 190
JMTM_APLP2 cd21709
juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 2 (APLP-2) and ...
 439-519 2.88e-53

juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 2 (APLP-2) and similar proteins; Amyloid-like protein 2 (APLP-2), also called amyloid protein homolog (APPH), or CDEI box-binding protein (CDEBP), may play a role in the regulation of hemostasis. Its soluble form may have inhibitory properties towards coagulation factors. APLP-2 may bind to the DNA 5'-GTCACATG-3'(CDEI box). It inhibits trypsin, chymotrypsin, plasmin, factor XIA, and plasma and glandular kallikrein. This model corresponds to juxtamembrane and transmembrane (JMTM) domain of APLP-2, which consists of the intact transmembrane (TM) domain with adjacent N-terminal juxtamembrane (JM) region.


Pssm-ID: 411992  Cd Length: 81  Bit Score: 174.73  E-value: 2.88e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010185 439 SVGPLREDFSLSSSALIGLLVIAVAIATVIVISLVMLRKRQYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLE 518
Cdd:cd21709    1 SDGPLRDDFSFSSSALIGLLVIAVAIATVIVISLVLLRKRQYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLE 80


                 .
gi 214010185 519 Q 519
Cdd:cd21709   81 Q 81
A4_EXTRA smart00006
amyloid A4; amyloid A4 precursor of Alzheimers disease
 42-137 5.22e-53

amyloid A4; amyloid A4 precursor of Alzheimers disease


Pssm-ID: 128326 [Multi-domain]  Cd Length: 165  Bit Score: 176.92  E-value: 5.22e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010185    42 GTGFAVAEPQIAMFCGKLNMHVNIQTGKWEPDPTGTKSCFETKEEVLQYCQEMYPELQITNVMEANQRVSIDNWCRRDKK 121
Cdd:smart00006   1 GAAGALAEPQIAMLCGRLNMHMNVQTGRWETDPSRTKTCLRDKEDILQYCRKAYPELQITNVVEASQPVTIQNWCRRGRS 80

                           90
                   ....*....|....*...
gi 214010185   122 QCKS--RFVTPFKCLVPP 137
Cdd:smart00006  81 QCKThhHFVIPFRCLVGE 98
APP_N pfam02177
Amyloid A4 N-terminal heparin-binding; This N-terminal domain of APP, amyloid precursor ...
 49-135 1.17e-51

Amyloid A4 N-terminal heparin-binding; This N-terminal domain of APP, amyloid precursor protein, is the heparin-binding domain of the protein. this region is also responsible for stimulation of neurite outgrowth. The structure reveals both a highly charged basic surface that may interact with glycosaminoglycans in the brain and an abutting hydrophobic surface that is proposed to play an important functional role such as in dimerization or ligand-binding. Structural similarities with cysteine-rich growth factors, taken together with its known growth-promoting properties, suggest the APP N-terminal domain could function as a growth factor in vivo.


Pssm-ID: 460474  Cd Length: 100  Bit Score: 170.95  E-value: 1.17e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010185   49 EPQIAMFCGKLNMHVNIQTGKWEPDPTGTKSCFETKEEVLQYCQEMYPELQITNVMEANQRVSIDNWCRRDKKQCK-SRF 127
Cdd:pfam02177   1 EPQVAMFCGKLNQHMDLETGRWEPDPSGKATCFKDKEEILDYCQKVYPELDITNIVEASQPVTIDNWCKKGRKKCKgHHI 80


                  ....*...
gi 214010185  128 VTPFKCLV 135
Cdd:pfam02177  81 VKPYRCLV 88
APP_amyloid pfam10515
Beta-amyloid precursor protein C-terminus; This is the amyloid, C-terminal, protein of the ...
 468-518 4.03e-25

Beta-amyloid precursor protein C-terminus; This is the amyloid, C-terminal, protein of the beta-Amyloid precursor protein (APP) which is a conserved and ubiquitous transmembrane glycoprotein strongly implicated in the pathogenesis of Alzheimer's disease but whose normal biological function is unknown. The C-terminal 100 residues are released and aggregate into amyloid deposits which are strongly implicated in the pathology of Alzheimer's disease plaque-formation. The domain is associated with family A4_EXTRA, pfam02177, further towards the N-terminus.


Pssm-ID: 463129  Cd Length: 52  Bit Score: 97.79  E-value: 4.03e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 214010185  468 IVISLVMLRKR-QYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLE 518
Cdd:pfam10515   1 IVVGMALLRRRaARSPSAHGFVEVDPNVTPEERHVANMQVNGYENPTYKYFE 52
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 160-352 3.77e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 3.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010185 160 RFQKAKEQLEIRHRN----RMDRVKKEWEEAELQAknlpkAERQTLIQHFQAMVKALEKEAASEKQQLVETHLaRVEAML 235
Cdd:COG1196  214 RYRELKEELKELEAEllllKLRELEAELEELEAEL-----EELEAELEELEAELAELEAELEELRLELEELEL-ELEEAQ 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010185 236 NDRRRmaLENYLAALQSDpprpHRILQALRRYVRAENKDRLHTIRHYQHVLAVDPEKAAQMKSQVMTHLHVIEERRNQSL 315
Cdd:COG1196  288 AEEYE--LLAELARLEQD----IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 214010185 316 SLLYKVPYVAQEIQEEIDELLQEQRADMDQFTASISE 352
Cdd:COG1196  362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
 
Name Accession Description Interval E-value
APP_E2 pfam12925
E2 domain of amyloid precursor protein; The E2 domain is the largest of the conserved domains ...
 136-318 4.89e-90

E2 domain of amyloid precursor protein; The E2 domain is the largest of the conserved domains of the amyloid precursor protein. The structure of E2 consists of two coiled-coil sub-structures connected through a continuous helix, and bears an unexpected resemblance to the spectrin family of protein structures.E 2 can reversibly dimerize in solution, and the dimerization occurs along the longest dimension of the molecule in an antiparallel orientation, which enables the N-terminal substructure of one monomer to pack against the C-terminal substructure of a second monomer. The high degree of conservation of residues at the putative dimer interface suggests that the E2 dimer observed in the crystal could be physiologically relevant. Heparin sulfate proteoglycans, the putative ligands for the precursor present in extracellular matrix, bind to E2 at a conserved and positively charged site near the dimer interface.


Pssm-ID: 463752  Cd Length: 190  Bit Score: 273.84  E-value: 4.89e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010185  136 PPTPLPTNDVDVYFETSADDNEHARFQKAKEQLEIRHRNRMDRVKKEWEEAELQAKNLPKAE-------RQTLIQHFQAM 208
Cdd:pfam12925   1 TTTPPPTDAVDPYFEHPDPRNEHESFKKAKKRLEEKHRERMTKVMKEWEEAEERYQNLPKADpkaaekfKKAMTARFQET 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010185  209 VKALEKEAASEKQQLVETHLARVEAMLNDRRRMALENYLAALQSDPPRPHRILQALRRYVRAENKDRLHTIRHYQHVLAV 288
Cdd:pfam12925  81 VEALEEEAAAERQQLVETHQQRVEAHLNDRRRDALECYLQALQENPPNPHRILKALKKLLRAEQKDRRHTLRHYRHLLAS 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 214010185  289 DPEKAAQMKSQVMTHLHVIEERRNQSLSLL 318
Cdd:pfam12925 161 DPEKAEQMKPQVLTHLRVIDRRMNQSLTLL 190
JMTM_APLP2 cd21709
juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 2 (APLP-2) and ...
 439-519 2.88e-53

juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 2 (APLP-2) and similar proteins; Amyloid-like protein 2 (APLP-2), also called amyloid protein homolog (APPH), or CDEI box-binding protein (CDEBP), may play a role in the regulation of hemostasis. Its soluble form may have inhibitory properties towards coagulation factors. APLP-2 may bind to the DNA 5'-GTCACATG-3'(CDEI box). It inhibits trypsin, chymotrypsin, plasmin, factor XIA, and plasma and glandular kallikrein. This model corresponds to juxtamembrane and transmembrane (JMTM) domain of APLP-2, which consists of the intact transmembrane (TM) domain with adjacent N-terminal juxtamembrane (JM) region.


Pssm-ID: 411992  Cd Length: 81  Bit Score: 174.73  E-value: 2.88e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010185 439 SVGPLREDFSLSSSALIGLLVIAVAIATVIVISLVMLRKRQYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLE 518
Cdd:cd21709    1 SDGPLRDDFSFSSSALIGLLVIAVAIATVIVISLVLLRKRQYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLE 80


                 .
gi 214010185 519 Q 519
Cdd:cd21709   81 Q 81
A4_EXTRA smart00006
amyloid A4; amyloid A4 precursor of Alzheimers disease
 42-137 5.22e-53

amyloid A4; amyloid A4 precursor of Alzheimers disease


Pssm-ID: 128326 [Multi-domain]  Cd Length: 165  Bit Score: 176.92  E-value: 5.22e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010185    42 GTGFAVAEPQIAMFCGKLNMHVNIQTGKWEPDPTGTKSCFETKEEVLQYCQEMYPELQITNVMEANQRVSIDNWCRRDKK 121
Cdd:smart00006   1 GAAGALAEPQIAMLCGRLNMHMNVQTGRWETDPSRTKTCLRDKEDILQYCRKAYPELQITNVVEASQPVTIQNWCRRGRS 80

                           90
                   ....*....|....*...
gi 214010185   122 QCKS--RFVTPFKCLVPP 137
Cdd:smart00006  81 QCKThhHFVIPFRCLVGE 98
APP_N pfam02177
Amyloid A4 N-terminal heparin-binding; This N-terminal domain of APP, amyloid precursor ...
 49-135 1.17e-51

Amyloid A4 N-terminal heparin-binding; This N-terminal domain of APP, amyloid precursor protein, is the heparin-binding domain of the protein. this region is also responsible for stimulation of neurite outgrowth. The structure reveals both a highly charged basic surface that may interact with glycosaminoglycans in the brain and an abutting hydrophobic surface that is proposed to play an important functional role such as in dimerization or ligand-binding. Structural similarities with cysteine-rich growth factors, taken together with its known growth-promoting properties, suggest the APP N-terminal domain could function as a growth factor in vivo.


Pssm-ID: 460474  Cd Length: 100  Bit Score: 170.95  E-value: 1.17e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010185   49 EPQIAMFCGKLNMHVNIQTGKWEPDPTGTKSCFETKEEVLQYCQEMYPELQITNVMEANQRVSIDNWCRRDKKQCK-SRF 127
Cdd:pfam02177   1 EPQVAMFCGKLNQHMDLETGRWEPDPSGKATCFKDKEEILDYCQKVYPELDITNIVEASQPVTIDNWCKKGRKKCKgHHI 80


                  ....*...
gi 214010185  128 VTPFKCLV 135
Cdd:pfam02177  81 VKPYRCLV 88
JMTM_APLP1 cd21708
juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 1 (APLP-1) and ...
 448-519 2.11e-35

juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 1 (APLP-1) and similar proteins; Amyloid-like protein 1 (APLP-1), also called APLP, may play a role in postsynaptic function. It couples to JIP signal transduction through C-terminal binding. APLP-1 may interact with cellular G-protein signaling pathways. It can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I. This model corresponds to the juxtamembrane and transmembrane (JMTM) domain of APLP-1, which consists of the intact transmembrane (TM) domain with adjacent N-terminal juxtamembrane (JM) region.


Pssm-ID: 411991  Cd Length: 85  Bit Score: 127.25  E-value: 2.11e-35
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 214010185 448 SLSSSALIGLLVIAVAIATVIVISLVMLRKRQYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLEQ 519
Cdd:cd21708   14 TFNRGALIGLLVVAVAVAMVIVISLLLVRRKPYGTISHGIVEVDPMLTPEERQLSKMQNHGYENPTYRFLEE 85
APP_amyloid pfam10515
Beta-amyloid precursor protein C-terminus; This is the amyloid, C-terminal, protein of the ...
 468-518 4.03e-25

Beta-amyloid precursor protein C-terminus; This is the amyloid, C-terminal, protein of the beta-Amyloid precursor protein (APP) which is a conserved and ubiquitous transmembrane glycoprotein strongly implicated in the pathogenesis of Alzheimer's disease but whose normal biological function is unknown. The C-terminal 100 residues are released and aggregate into amyloid deposits which are strongly implicated in the pathology of Alzheimer's disease plaque-formation. The domain is associated with family A4_EXTRA, pfam02177, further towards the N-terminus.


Pssm-ID: 463129  Cd Length: 52  Bit Score: 97.79  E-value: 4.03e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 214010185  468 IVISLVMLRKR-QYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLE 518
Cdd:pfam10515   1 IVVGMALLRRRaARSPSAHGFVEVDPNVTPEERHVANMQVNGYENPTYKYFE 52
JMTM_APP_like cd21699
juxtamembrane and transmembrane (JMTM) domain found in the amyloid-beta precursor protein (APP) ...
 439-478 1.41e-09

juxtamembrane and transmembrane (JMTM) domain found in the amyloid-beta precursor protein (APP) family; The amyloid-beta precursor protein (APP) family includes amyloid-like proteins APLP-1 and APLP-2. APP (also called ABPP, APPI, Alzheimer disease (AD) amyloid protein, amyloid precursor protein, amyloid-beta A4 protein, cerebral vascular amyloid peptide (CVAP), PreA4, or protease nexin-II (PN-II)) functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Amyloid-beta peptides are lipophilic metal chelators with metal-reducing activity; they bind transient metals such as copper, zinc and iron. APLP-1, also called APLP, may play a role in postsynaptic function. It couples to JIP signal transduction through C-terminal binding. APLP-1 may interact with cellular G-protein signaling pathways. It can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I. APLP-2 (also called amyloid protein homolog (APPH), or CDEI box-binding protein (CDEBP)) may play a role in the regulation of hemostasis. Its soluble form may have inhibitory properties towards coagulation factors. APLP-2 may bind to the DNA 5'-GTCACATG-3'(CDEI box). It inhibits trypsin, chymotrypsin, plasmin, factor XIA, and plasma and glandular kallikrein. This model corresponds to juxtamembrane and transmembrane (JMTM) domain of APP, which consists of the intact transmembrane (TM) domain with adjacent N-terminal juxtamembrane (JM) region. More than half of all familial APP mutations of Alzheimer's disease are seen in its JMTM domain region.


Pssm-ID: 411982  Cd Length: 41  Bit Score: 53.44  E-value: 1.41e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 214010185 439 SVGPLREDFS-LSSSALIGLLVIAVAIATVIVISLVMLRKR 478
Cdd:cd21699    1 ERVFLAEDSSnSSFGAVIGLAVGGVAVAIVIVVAVVMLRRR 41
JMTM_APP cd21707
juxtamembrane and transmembrane (JMTM) domain found in amyloid-beta precursor protein (APP) ...
 445-478 1.52e-04

juxtamembrane and transmembrane (JMTM) domain found in amyloid-beta precursor protein (APP) and similar proteins; Amyloid-beta precursor protein (APP), also called APPI, ABPP, Alzheimer disease amyloid protein, amyloid precursor protein, amyloid-beta A4 protein, cerebral vascular amyloid peptide (CVAP), PreA4, or protease nexin-II (PN-II), functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Amyloid-beta peptides are lipophilic metal chelators with metal-reducing activity; they bind transient metals such as copper, zinc and iron. This model corresponds to juxtamembrane and transmembrane (JMTM) domain of APP, which consists of the intact transmembrane (TM) domain with adjacent N-terminal juxtamembrane (JM) region. More than half of all familial APP mutations of Alzheimer's disease are seen in its JMTM domain region.


Pssm-ID: 411990  Cd Length: 40  Bit Score: 39.16  E-value: 1.52e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 214010185 445 EDFSLSSSALIGLLVIAVAIATVIVISLVMLRKR 478
Cdd:cd21707    7 EDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKK 40
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 160-352 3.77e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 3.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010185 160 RFQKAKEQLEIRHRN----RMDRVKKEWEEAELQAknlpkAERQTLIQHFQAMVKALEKEAASEKQQLVETHLaRVEAML 235
Cdd:COG1196  214 RYRELKEELKELEAEllllKLRELEAELEELEAEL-----EELEAELEELEAELAELEAELEELRLELEELEL-ELEEAQ 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010185 236 NDRRRmaLENYLAALQSDpprpHRILQALRRYVRAENKDRLHTIRHYQHVLAVDPEKAAQMKSQVMTHLHVIEERRNQSL 315
Cdd:COG1196  288 AEEYE--LLAELARLEQD----IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 214010185 316 SLLYKVPYVAQEIQEEIDELLQEQRADMDQFTASISE 352
Cdd:COG1196  362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
158-341 5.03e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 5.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010185  158 HARFQKAKEQLEI-----RHRNRMDRVKKEWEEAELQAKNLPKAERQTLIQHFQAMVKALEKEAASEKQQL--VETHLAR 230
Cdd:COG4913   241 HEALEDAREQIELlepirELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELerLEARLDA 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010185  231 VEAMLNDRRRMALENYLAALQSdpprphriLQALRRYVRAENKDRLHTIRHYQHVLAV-------DPEKAAQMKSQVMTH 303
Cdd:COG4913   321 LREELDELEAQIRGNGGDRLEQ--------LEREIERLERELEERERRRARLEALLAAlglplpaSAEEFAALRAEAAAL 392

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 214010185  304 LHVIEERRNQSLSLLYKVPYVAQEIQEEIDELLQEQRA 341
Cdd:COG4913   393 LEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
 
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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