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Conserved domains on  [gi|1002235614|ref|XP_015622004|]
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putative clathrin assembly protein At2g01600 [Oryza sativa Japonica Group]

Protein Classification

ANTH domain-containing protein( domain architecture ID 10541692)

ANTH (AP180 N-Terminal Homology) domain-containing protein may act as clathrin coat assembly protein; ANTH (AP180 N-Terminal Homology) domain-containing protein may act as clathrin coat assembly protein; ANTH (AP180 N-Terminal Homology) domain-containing protein may act as clathrin coat assembly protein; ANTH (AP180 N-Terminal Homology) domain-containing protein may act as clathrin coat assembly protein; similar to phosphatidylinositol-binding clathrin assembly protein (PICALM) and clathrin coat assembly protein AP180 (SNAP91); ANTH (AP180 N-Terminal Homology) domain-containing protein may act as clathrin coat assembly protein; ANTH (AP180 N-Terminal Homology) domain-containing protein may act as clathrin coat assembly protein; similar to phosphatidylinositol-binding clathrin assembly protein (PICALM) and clathrin coat assembly protein AP180 (SNAP91)

CATH:  1.20.58.150|1.25.40.90
Gene Ontology:  GO:0030136|GO:0005545|GO:0030276|GO:0048268
PubMed:  12740367|12742163|22748146

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 31-307 5.49e-111

ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats.


:

Pssm-ID: 400137  Cd Length: 272  Bit Score: 332.34  E-value: 5.49e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235614  31 DLDVAIVKATNHVECPPKERHLRKIAAATSigrPRADVAYCIHALARRLAKTRNWIVALKTLVVIHRLLRDGDPTFREEF 110
Cdd:pfam07651   1 DLEVAVVKATSHDEAPPKEKHVREILVGTS---SSAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235614 111 LTFTQRV-RILQLSNFkddstPVAWDYSSWVRTYGLFLEERLECFRVLKYD-IEAERLSKQGQGP-EKGHSRTRELDSPD 187
Cdd:pfam07651  78 LRARRRIsSLLRISSF-----SLSWDYGAFIRAYAKYLDERLDFHRKLPRDpGTFERVEYGSLVAvGDPNERYLTMSMED 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235614 188 LLEQLPALQQLLYRLIGCRPEGAANSNYLVQYALALVLKESFKIYCAINDGIINLVDKFFEMPRHEALKALEIYRRAGQQ 267
Cdd:pfam07651 153 LLDSIPKLQKLLFRLLKCRPTGNALSNECIIAALILLVKESFGLYRAINEGIINLLEKFFELSKPDADRALGIYKRFVKQ 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1002235614 268 AGSLSDFYENCRGLELARNFQFPTLREPPQSFLSTMEEYV 307
Cdd:pfam07651 233 FERLKEFYEVCKNLGYFRSLEIPKLPHIPPNLLEALEEYL 272
 
Name Accession Description Interval E-value
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 31-307 5.49e-111

ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats.


Pssm-ID: 400137  Cd Length: 272  Bit Score: 332.34  E-value: 5.49e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235614  31 DLDVAIVKATNHVECPPKERHLRKIAAATSigrPRADVAYCIHALARRLAKTRNWIVALKTLVVIHRLLRDGDPTFREEF 110
Cdd:pfam07651   1 DLEVAVVKATSHDEAPPKEKHVREILVGTS---SSAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235614 111 LTFTQRV-RILQLSNFkddstPVAWDYSSWVRTYGLFLEERLECFRVLKYD-IEAERLSKQGQGP-EKGHSRTRELDSPD 187
Cdd:pfam07651  78 LRARRRIsSLLRISSF-----SLSWDYGAFIRAYAKYLDERLDFHRKLPRDpGTFERVEYGSLVAvGDPNERYLTMSMED 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235614 188 LLEQLPALQQLLYRLIGCRPEGAANSNYLVQYALALVLKESFKIYCAINDGIINLVDKFFEMPRHEALKALEIYRRAGQQ 267
Cdd:pfam07651 153 LLDSIPKLQKLLFRLLKCRPTGNALSNECIIAALILLVKESFGLYRAINEGIINLLEKFFELSKPDADRALGIYKRFVKQ 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1002235614 268 AGSLSDFYENCRGLELARNFQFPTLREPPQSFLSTMEEYV 307
Cdd:pfam07651 233 FERLKEFYEVCKNLGYFRSLEIPKLPHIPPNLLEALEEYL 272
ANTH_N cd03564
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ...
 32-154 4.09e-62

ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal Homology) domain family is composed of Adaptor Protein 180 (AP180), Clathrin Assembly Lymphoid Myeloid Leukemia protein (CALM), and similar proteins. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ANTH-bearing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that the ANTH domain is a universal component of the machinery for clathrin-mediated membrane budding. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains.


Pssm-ID: 340767  Cd Length: 120  Bit Score: 200.19  E-value: 4.09e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235614  32 LDVAIVKATNHVECPPKERHLRKIAAATSIGRPRADVAYCIHALARRLAKtRNWIVALKTLVVIHRLLRDGDPTFREEFL 111
Cdd:cd03564     1 LDVAVVKATNHDEVPPKEKHVRKLLLATSNGGGRADVAYIVHALAKRLHK-KNWIVVLKTLIVIHRLLREGSPSFLEELL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1002235614 112 TFtqRVRILQLSNFKDDSTPVAWDYSSWVRTYGLFLEERLECF 154
Cdd:cd03564    80 RY--SGHIFNLSNFKDDSSPEAWDLSAFIRRYARYLEERLECF 120
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
31-160 2.47e-40

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 142.77  E-value: 2.47e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235614   31 DLDVAIVKATNHVECPPKERHLRKIAAATSigRPRADVAYCIHALARRLAKTRNWIVALKTLVVIHRLLRDGDPtfrEEF 110
Cdd:smart00273   2 DLEVKVRKATNNDEWGPKGKHLREIIQGTH--NEKSSFAEIMAVLWRRLNDTKNWRVVYKALILLHYLLRNGSP---RVI 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1002235614  111 LTFTQRV-RILQLSNFKDDStPVAWDYSSWVRTYGLFLEERLECFRVLKYD 160
Cdd:smart00273  77 LEALRNRnRILNLSDFQDID-SRGKDQGANIRTYAKYLLERLEDDRRLKEE 126
 
Name Accession Description Interval E-value
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 31-307 5.49e-111

ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats.


Pssm-ID: 400137  Cd Length: 272  Bit Score: 332.34  E-value: 5.49e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235614  31 DLDVAIVKATNHVECPPKERHLRKIAAATSigrPRADVAYCIHALARRLAKTRNWIVALKTLVVIHRLLRDGDPTFREEF 110
Cdd:pfam07651   1 DLEVAVVKATSHDEAPPKEKHVREILVGTS---SSAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235614 111 LTFTQRV-RILQLSNFkddstPVAWDYSSWVRTYGLFLEERLECFRVLKYD-IEAERLSKQGQGP-EKGHSRTRELDSPD 187
Cdd:pfam07651  78 LRARRRIsSLLRISSF-----SLSWDYGAFIRAYAKYLDERLDFHRKLPRDpGTFERVEYGSLVAvGDPNERYLTMSMED 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235614 188 LLEQLPALQQLLYRLIGCRPEGAANSNYLVQYALALVLKESFKIYCAINDGIINLVDKFFEMPRHEALKALEIYRRAGQQ 267
Cdd:pfam07651 153 LLDSIPKLQKLLFRLLKCRPTGNALSNECIIAALILLVKESFGLYRAINEGIINLLEKFFELSKPDADRALGIYKRFVKQ 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1002235614 268 AGSLSDFYENCRGLELARNFQFPTLREPPQSFLSTMEEYV 307
Cdd:pfam07651 233 FERLKEFYEVCKNLGYFRSLEIPKLPHIPPNLLEALEEYL 272
ANTH_N cd03564
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ...
 32-154 4.09e-62

ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal Homology) domain family is composed of Adaptor Protein 180 (AP180), Clathrin Assembly Lymphoid Myeloid Leukemia protein (CALM), and similar proteins. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ANTH-bearing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that the ANTH domain is a universal component of the machinery for clathrin-mediated membrane budding. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains.


Pssm-ID: 340767  Cd Length: 120  Bit Score: 200.19  E-value: 4.09e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235614  32 LDVAIVKATNHVECPPKERHLRKIAAATSIGRPRADVAYCIHALARRLAKtRNWIVALKTLVVIHRLLRDGDPTFREEFL 111
Cdd:cd03564     1 LDVAVVKATNHDEVPPKEKHVRKLLLATSNGGGRADVAYIVHALAKRLHK-KNWIVVLKTLIVIHRLLREGSPSFLEELL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1002235614 112 TFtqRVRILQLSNFKDDSTPVAWDYSSWVRTYGLFLEERLECF 154
Cdd:cd03564    80 RY--SGHIFNLSNFKDDSSPEAWDLSAFIRRYARYLEERLECF 120
ANTH_N_AP180_plant cd16987
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of plant Clathrin coat assembly ...
 32-154 1.37e-52

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of plant Clathrin coat assembly protein AP180 and similar proteins; This subfamily is composed of plant clathrin coat assembly protein AP180 and other ANTH domain containing proteins that are yet to be characterized. Arabidopsis thaliana AP180 (At-AP180) is a binding partner of plant alphaC-adaptin; it functions as a clathrin assembly protein that promotes the formation of cages with an almost uniform size distribution. In addition to At-AP180, Arabidopsis thaliana contains many ANTH domain containing proteins labelled as putative clathrin assembly proteins included in this subfamily such as At4g02650, At5g10410, At2g25430, and At1g33340, among others. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains of plant clathrin coat assembly protein AP180 and similar proteins.


Pssm-ID: 340784  Cd Length: 122  Bit Score: 175.12  E-value: 1.37e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235614  32 LDVAIVKATNHVECPPKERHLRKIAAATSIGRPRAdvAYCIHALARRLAKTRNWIVALKTLVVIHRLLRDGDPTFREEFL 111
Cdd:cd16987     1 LEVAVVKATSHDDAPPDEKYVREILSLGSSSRAYA--SACVSALSRRLNRTRDWVVALKCLMLLHRLLRDGSPILEQELS 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1002235614 112 TFTQR-VRILQLSNFKDDSTPVAWDYSSWVRTYGLFLEERLECF 154
Cdd:cd16987    79 LAPSGgRNPLNLSDFRDGSSSKSWDFSAFVRAYAAYLDERLIFS 122
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
31-160 2.47e-40

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 142.77  E-value: 2.47e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235614   31 DLDVAIVKATNHVECPPKERHLRKIAAATSigRPRADVAYCIHALARRLAKTRNWIVALKTLVVIHRLLRDGDPtfrEEF 110
Cdd:smart00273   2 DLEVKVRKATNNDEWGPKGKHLREIIQGTH--NEKSSFAEIMAVLWRRLNDTKNWRVVYKALILLHYLLRNGSP---RVI 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1002235614  111 LTFTQRV-RILQLSNFKDDStPVAWDYSSWVRTYGLFLEERLECFRVLKYD 160
Cdd:smart00273  77 LEALRNRnRILNLSDFQDID-SRGKDQGANIRTYAKYLLERLEDDRRLKEE 126
ANTH_N_YAP180 cd16988
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of yeast clathrin coat assembly ...
 33-154 6.22e-14

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of yeast clathrin coat assembly protein AP180 (YAP180) and similar proteins; This subfamily includes yeast clathrin coat assembly protein AP180 (YAP180) and similar proteins. There are two YAP180 proteins in Saccharomyces cerevisiae, AP180A (yAP180A or YAP1801) and AP180B (yAP180B or YAP1802). They are involved in endocytosis and clathrin cage assembly. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains of plant clathrin coat assembly protein AP180 and similar proteins.


Pssm-ID: 340785  Cd Length: 117  Bit Score: 68.36  E-value: 6.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235614  33 DVAIVKATNHVECPPKERHLRKIAAATSigRPRADVAYCIHALARRLaKTRNWIVALKTLVVIHRLLRDGDPtfREEFLT 112
Cdd:cd16988     2 EKLVKGATKIKLAPPKAKYLDPILLATY--SSDASFGEIVRALSRRL-RDNSWTVVFKSLIVLHLMIREGET--DDVLLY 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1002235614 113 FTQRVRILQLSNFKDDStpvAWDYSSW--VRTYGLFLEERLECF 154
Cdd:cd16988    77 YLSRPDFLDLRKIRNGS---SAGSGQLqnIQRYAAYLKERVKEY 117
ANTH_N_Sla2p_HIP1_like cd16986
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; ...
 34-152 3.00e-13

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; Members of the Sla2p/HIP1/HIP1R subfamily share a common domain architecture, containing an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. Both HIP1 and HIP1R promote clathrin assembly in vitro. Yeast Sla2p, is a regulator of membrane cytoskeleton assembly. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. While the ANTH domain of Sla2p preferentially binds PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome, mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively. This model describes the N-terminal region of ANTH domains of the Sla2p/HIP1/HIP1R subfamily.


Pssm-ID: 340783  Cd Length: 117  Bit Score: 66.25  E-value: 3.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235614  34 VAIVKATNHVECPPKERHLRKIAAATSigrPRADVAYCIHALARRLAKTrNWIVALKTLVVIHRLLRDGDPtfrEEFLTF 113
Cdd:cd16986     3 KAVNKATNKTDSPPKPKHVRTIIVKSW---THQKGPQFYEELSKRLLLN-NPVVQFKALVTLHKVLRDGPP---ELSLLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1002235614 114 TQRVR-ILQLSNFKDDSTPVAWDYSSWVRTYGLFLEERLE 152
Cdd:cd16986    76 GYLDAwLPELVRVKNTQQSLSEFYSQLIKKYVRYLELKVV 115
ANTH_N_AP180 cd16985
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of adaptor protein 180 (AP180) ...
 35-151 1.47e-11

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of adaptor protein 180 (AP180) subfamily; The Adaptor Protein 180 (AP180) subfamily members are phosphatidylinositol-binding clathrin assembly proteins, including mammalian clathrin coat assembly protein AP180 and Clathrin Assembly Lymphoid Myeloid Leukemia protein (CALM), Drosophila LAP (also called Like-AP180 or AP180), and Caenorhabditis elegans Uncoordinated protein 11 (unc-11, also called AP180-like adaptor protein). They are components of the adaptor complexes which link clathrin to receptors in coated vesicles. AP180 and CALM play important roles in clathrin-mediated endocytosis. AP180, also called 91 kDa synaptosomal-associated protein (SNAP91) or phosphoprotein F1-20, is a brain-specific clathrin-binding protein which stimulates clathrin assembly during the recycling of synaptic vesicles. CALM, also called phosphatidylinositol binding clathrin assembly protein (PICALM), is ubiquitously expressed. Members of this subfamily contain ANTH domains, which bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains of the Adaptor Protein 180 (AP180) subfamily.


Pssm-ID: 340782  Cd Length: 117  Bit Score: 61.67  E-value: 1.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235614  35 AIVKATNHVECPPKERHLRKIAAATsiGRPRADVAYCIHALARRlAKTRNWIVALKTLVVIHRLLRDGDptfrEEFLTF- 113
Cdd:cd16985     4 AVCKATTHEVMGPKKKHLDYLVQCT--NEPNVNIPQLADLLFER-TQNSSWVVVFKALITTHHLMVYGN----ERFIQYl 76

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1002235614 114 TQRVRILQLSNFKDDSTPVAWDYSSWVRTYGLFLEERL 151
Cdd:cd16985    77 ASRNSLFNLSNFLDKSGSQGYDMSTFIRRYAKYLNEKA 114
ENTH cd03571
Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is ...
 39-126 6.50e-09

Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, contributing to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


Pssm-ID: 340772  Cd Length: 117  Bit Score: 54.06  E-value: 6.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235614  39 ATNHVECPPKERHLRKIAAATSigrpraDVAYC---IHALARRLA-KTRNWIVALKTLVVIHRLLRDGDPTFREEFLtfT 114
Cdd:cd03571     8 ATSNEPWGPTGSQLAEIAQATF------DYDDYqriMKVLWKRLNdKGKNWRHVYKALTLLEYLLKNGSERVVDEFR--D 79

                          90
                  ....*....|..
gi 1002235614 115 QRVRILQLSNFK 126
Cdd:cd03571    80 NLYLIRTLQDFQ 91
ANTH_N_HIP1_like cd17006
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ...
 34-152 3.69e-08

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1 and related proteins; This subfamily includes Huntingtin-interacting protein 1 (HIP1), HIP1-related protein (HIP1R), and similar proteins. Mammalian HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. HIP1 is expressed only in neurons while HIP1R is ubiquitously expressed. Together with its interacting partner HIPPI, HIP1 regulates apoptosis and gene expression. Both HIP1 and HIP1R promote clathrin assembly in vitro, and they share a common domain architecture, containing an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. Mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively, instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of the ANTH domain of Huntingtin-interacting protein 1 and related proteins.


Pssm-ID: 340803  Cd Length: 114  Bit Score: 51.90  E-value: 3.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235614  34 VAIVKATNHVECPPKERHLRKIAaatsIGRPRADVAYCIHALARRLAKTRNWIVALKTLVVIHRLLRDGDPT-FREeflT 112
Cdd:cd17006     3 ISINKAINPQEVPVKEKHVRSII----IGTHQEKGASTFWSIVSRLPLQGNPIVCWKFCHLLHKLLREGHPSvLRD---S 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1002235614 113 FTQRVRILQLSNFkddstpvaW-----DYSSWVRTYGLFLEERLE 152
Cdd:cd17006    76 QRYRSRLKELGKL--------WghlkdGYGKLIAQYCKLLITKLE 112
ANTH_N_HIP1R cd17014
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ...
 34-104 8.73e-06

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1-related protein; Huntingtin-interacting protein 1-related protein (HIP1R), also called HIP12, promotes clathrin assembly in vitro. It is an endocytic protein involved in receptor trafficking, including regulating cell surface expression of receptor tyrosine kinases. Low HIP1R protein expression is associated with worse survival in diffuse large B-cell lymphoma (DLBCL) patients; it is preferentially expressed in germinal center B-cell (GCB)-like DLBCL, and may be potentially useful in subtyping DLBCL cases. HIP1R contains an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domain. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of mammalian HIP1R was found to preferentially bind PtdIns(3,5)P2 instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domain of Huntingtin-interacting protein 1-related protein.


Pssm-ID: 340811  Cd Length: 114  Bit Score: 44.86  E-value: 8.73e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002235614  34 VAIVKATNHVECPPKERHLRKIAaatsIGRPRADVAYCIHALARRLAKTRNWIVALKTLVVIHRLLRDGDP 104
Cdd:cd17014     3 ISISKAINTQEAPVKEKHARRII----LGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHP 69
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 38-127 2.97e-04

ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in endocytosis and cytoskeletal machinery. The function of the ENTH domain is unknown.


Pssm-ID: 426255  Cd Length: 124  Bit Score: 40.62  E-value: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235614  38 KATNHVECPPKERHLRKIAAATSIGRPRADVAYCIHalaRRLAKT-RNWIVALKTLVVIHRLLRDGDPTFREEFltftqR 116
Cdd:pfam01417  10 EATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLW---KRLNDKgKNWRHIYKALTLLEYLLKNGSERVVDDL-----R 81

                          90
                  ....*....|.
gi 1002235614 117 VRILQLSNFKD 127
Cdd:pfam01417  82 ENIYIIRTLTD 92
ANTH_N_HIP1 cd17013
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ...
 34-105 6.94e-03

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1; Huntingtin-interacting protein 1 (HIP1) was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. HIP1 promotes clathrin assembly in vitro. Together with its interacting partner HIPPI, it regulates apoptosis and gene expression. HIP1 contains an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domain. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of mammalian HIP1 was found to preferentially bind PtdIns(3,4)P2 instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domain of Huntingtin-interacting protein 1.


Pssm-ID: 340810  Cd Length: 114  Bit Score: 36.55  E-value: 6.94e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002235614  34 VAIVKATNHVECPPKERHLRKIAaatsIGRPRADVAYCIHALARRLAKTRNWIVALKTLVVIHRLLRDGDPT 105
Cdd:cd17013     3 VSINKAINTQEVAVKEKHARTCI----LGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPN 70
 
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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