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Conserved domains on  [gi|332688231|ref|NP_001193875|]
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phosphatidylinositol-binding clathrin assembly protein isoform 3 [Homo sapiens]

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; similar to Homo sapiens phosphatidylinositol-binding clathrin assembly protein and clathrin coat assembly protein AP180

CATH:  1.20.58.150|1.25.40.90
Gene Ontology:  GO:0030276|GO:0048268|GO:0072583
PubMed:  12740367|12742163|22748146|14657269
SCOP:  4000571|4000581

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 ...
 24-282 3.83e-94

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: 291.13  E-value: 3.83e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332688231   24 KTVCKATTHEiMGPKKKHLDYLIQCTNEMNVNIPQLADSLFERTTNS-SWVVVFKSLITTHHLMVYGNERFIQYLASRNT 102
Cdd:pfam07651   4 VAVVKATSHD-EAPPKEKHVREILVGTSSSAKLAALFWALSRRLPLTrSWVVAFKALILVHKLLREGHPSVLQELLRARR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332688231  103 LFNLSNFLDKSGLqGYDMSTFIRRYSRYLNEKAVSYRQVAFD---FTKVKRGA-----DGVMR--TMNTEKLLKTVPIIQ 172
Cdd:pfam07651  83 RISSLLRISSFSL-SWDYGAFIRAYAKYLDERLDFHRKLPRDpgtFERVEYGSlvavgDPNERylTMSMEDLLDSIPKLQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332688231  173 NQMDALLDFNVNSNELTNGVINAAFMLLFKDAIRLFAAYNEGIINLLEKYFDMKKNQCKEGLDIYKKFLTRMTRISEFLK 252
Cdd:pfam07651 162 KLLFRLLKCRPTGNALSNECIIAALILLVKESFGLYRAINEGIINLLEKFFELSKPDADRALGIYKRFVKQFERLKEFYE 241

                         250       260       270
                  ....*....|....*....|....*....|.
gi 332688231  253 VAEQVGIDRG-DIPDLSQAPSSLLDALEQHL 282
Cdd:pfam07651 242 VCKNLGYFRSlEIPKLPHIPPNLLEALEEYL 272
 
Name Accession Description Interval E-value
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 24-282 3.83e-94

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: 291.13  E-value: 3.83e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332688231   24 KTVCKATTHEiMGPKKKHLDYLIQCTNEMNVNIPQLADSLFERTTNS-SWVVVFKSLITTHHLMVYGNERFIQYLASRNT 102
Cdd:pfam07651   4 VAVVKATSHD-EAPPKEKHVREILVGTSSSAKLAALFWALSRRLPLTrSWVVAFKALILVHKLLREGHPSVLQELLRARR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332688231  103 LFNLSNFLDKSGLqGYDMSTFIRRYSRYLNEKAVSYRQVAFD---FTKVKRGA-----DGVMR--TMNTEKLLKTVPIIQ 172
Cdd:pfam07651  83 RISSLLRISSFSL-SWDYGAFIRAYAKYLDERLDFHRKLPRDpgtFERVEYGSlvavgDPNERylTMSMEDLLDSIPKLQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332688231  173 NQMDALLDFNVNSNELTNGVINAAFMLLFKDAIRLFAAYNEGIINLLEKYFDMKKNQCKEGLDIYKKFLTRMTRISEFLK 252
Cdd:pfam07651 162 KLLFRLLKCRPTGNALSNECIIAALILLVKESFGLYRAINEGIINLLEKFFELSKPDADRALGIYKRFVKQFERLKEFYE 241

                         250       260       270
                  ....*....|....*....|....*....|.
gi 332688231  253 VAEQVGIDRG-DIPDLSQAPSSLLDALEQHL 282
Cdd:pfam07651 242 VCKNLGYFRSlEIPKLPHIPPNLLEALEEYL 272
ANTH_N_AP180 cd16985
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of adaptor protein 180 (AP180) ...
 22-138 7.92e-85

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: 261.20  E-value: 7.92e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332688231  22 VSKTVCKATTHEIMGPKKKHLDYLIQCTNEMNVNIPQLADSLFERTTNSSWVVVFKSLITTHHLMVYGNERFIQYLASRN 101
Cdd:cd16985    1 LAKAVCKATTHEVMGPKKKHLDYLVQCTNEPNVNIPQLADLLFERTQNSSWVVVFKALITTHHLMVYGNERFIQYLASRN 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 332688231 102 TLFNLSNFLDKSGLQGYDMSTFIRRYSRYLNEKAVSY 138
Cdd:cd16985   81 SLFNLSNFLDKSGSQGYDMSTFIRRYAKYLNEKAISY 117
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
20-145 2.71e-42

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 148.93  E-value: 2.71e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332688231    20 SAVSKTVCKATTHEIMGPKKKHLDYLIQCTNEMNVNIPQLADSLFERTTNS-SWVVVFKSLITTHHLMVYGNERFI-QYL 97
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTkNWRVVYKALILLHYLLRNGSPRVIlEAL 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 332688231    98 ASRNTLFNLSNFLDKSGlQGYDMSTFIRRYSRYLNEKAVSYRQVAFDF 145
Cdd:smart00273  81 RNRNRILNLSDFQDIDS-RGKDQGANIRTYAKYLLERLEDDRRLKEER 127
 
Name Accession Description Interval E-value
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 24-282 3.83e-94

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: 291.13  E-value: 3.83e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332688231   24 KTVCKATTHEiMGPKKKHLDYLIQCTNEMNVNIPQLADSLFERTTNS-SWVVVFKSLITTHHLMVYGNERFIQYLASRNT 102
Cdd:pfam07651   4 VAVVKATSHD-EAPPKEKHVREILVGTSSSAKLAALFWALSRRLPLTrSWVVAFKALILVHKLLREGHPSVLQELLRARR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332688231  103 LFNLSNFLDKSGLqGYDMSTFIRRYSRYLNEKAVSYRQVAFD---FTKVKRGA-----DGVMR--TMNTEKLLKTVPIIQ 172
Cdd:pfam07651  83 RISSLLRISSFSL-SWDYGAFIRAYAKYLDERLDFHRKLPRDpgtFERVEYGSlvavgDPNERylTMSMEDLLDSIPKLQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332688231  173 NQMDALLDFNVNSNELTNGVINAAFMLLFKDAIRLFAAYNEGIINLLEKYFDMKKNQCKEGLDIYKKFLTRMTRISEFLK 252
Cdd:pfam07651 162 KLLFRLLKCRPTGNALSNECIIAALILLVKESFGLYRAINEGIINLLEKFFELSKPDADRALGIYKRFVKQFERLKEFYE 241

                         250       260       270
                  ....*....|....*....|....*....|.
gi 332688231  253 VAEQVGIDRG-DIPDLSQAPSSLLDALEQHL 282
Cdd:pfam07651 242 VCKNLGYFRSlEIPKLPHIPPNLLEALEEYL 272
ANTH_N_AP180 cd16985
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of adaptor protein 180 (AP180) ...
 22-138 7.92e-85

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: 261.20  E-value: 7.92e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332688231  22 VSKTVCKATTHEIMGPKKKHLDYLIQCTNEMNVNIPQLADSLFERTTNSSWVVVFKSLITTHHLMVYGNERFIQYLASRN 101
Cdd:cd16985    1 LAKAVCKATTHEVMGPKKKHLDYLVQCTNEPNVNIPQLADLLFERTQNSSWVVVFKALITTHHLMVYGNERFIQYLASRN 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 332688231 102 TLFNLSNFLDKSGLQGYDMSTFIRRYSRYLNEKAVSY 138
Cdd:cd16985   81 SLFNLSNFLDKSGSQGYDMSTFIRRYAKYLNEKAISY 117
ANTH_N cd03564
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ...
 24-138 4.41e-43

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: 150.89  E-value: 4.41e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332688231  24 KTVCKATTHEIMGPKKKHLDYLIQCTNEM--NVNIPQLADSLFERTTNSSWVVVFKSLITTHHLMVYGNERFIQYLASRN 101
Cdd:cd03564    3 VAVVKATNHDEVPPKEKHVRKLLLATSNGggRADVAYIVHALAKRLHKKNWIVVLKTLIVIHRLLREGSPSFLEELLRYS 82

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 332688231 102 -TLFNLSNFLDKSGLQGYDMSTFIRRYSRYLNEKAVSY 138
Cdd:cd03564   83 gHIFNLSNFKDDSSPEAWDLSAFIRRYARYLEERLECF 120
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
20-145 2.71e-42

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 148.93  E-value: 2.71e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332688231    20 SAVSKTVCKATTHEIMGPKKKHLDYLIQCTNEMNVNIPQLADSLFERTTNS-SWVVVFKSLITTHHLMVYGNERFI-QYL 97
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTkNWRVVYKALILLHYLLRNGSPRVIlEAL 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 332688231    98 ASRNTLFNLSNFLDKSGlQGYDMSTFIRRYSRYLNEKAVSYRQVAFDF 145
Cdd:smart00273  81 RNRNRILNLSDFQDIDS-RGKDQGANIRTYAKYLLERLEDDRRLKEER 127
VHS_ENTH_ANTH cd00197
VHS, ENTH and ANTH domain superfamily; This superfamily is composed of proteins containing a ...
 22-137 6.27e-42

VHS, ENTH and ANTH domain superfamily; This superfamily is composed of proteins containing a VHS, CID, ENTH, or ANTH domain. The VHS domain is present in Vps27 (Vacuolar Protein Sorting), Hrs (Hepatocyte growth factor-regulated tyrosine kinase substrate) and STAM (Signal Transducing Adaptor Molecule). It is located at the N-termini of proteins involved in intracellular membrane trafficking. The CTD-Interacting Domain (CID) is present in several RNA-processing factors and binds tightly to the carboxy-terminal domain (CTD) of RNA polymerase II (RNAP II or Pol II). The epsin N-terminal homology (ENTH) domain is an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. A set of proteins previously designated as harboring an ENTH domain in fact contains a highly similar, yet unique module referred to as an AP180 N-Terminal Homology (ANTH) domain. VHS, ENTH, and ANTH domains are structurally similar and are composed of a superhelix of eight alpha helices. ENTH and ANTH (E/ANTH) domains bind both inositol phospholipids and proteins and contribute 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. E/ANTH domain-bearing 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: 340764  Cd Length: 115  Bit Score: 147.57  E-value: 6.27e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332688231  22 VSKTVCKATTHEIMGPKKKHLDYLIQCTNEMNVNIPQLADSLFERTTNSSWVVVFKSLITTHHLMVYGNERFIQYLASRN 101
Cdd:cd00197    1 FEKTVEKATSNENMGPDWPLIMEICDLINETNVGPKEAVDAIKKRINNKNPHVVLKALTLLEYCVKNCGERFHQEVASND 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 332688231 102 TLFNLSNFlDKSGLQGYDMSTFIRRYSRYLNEKAVS 137
Cdd:cd00197   81 FAVELLKF-DKSGLLGDDVSTNVREKAIELVQLWAS 115
ANTH_N_YAP180 cd16988
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of yeast clathrin coat assembly ...
 24-138 6.24e-24

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: 96.87  E-value: 6.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332688231  24 KTVCKATTHEIMGPKKKHLDYLIQCTNEMNVNIPQLADSLFERTTNSSWVVVFKSLITTHHLMVYGN-ERFIQYLASRNT 102
Cdd:cd16988    3 KLVKGATKIKLAPPKAKYLDPILLATYSSDASFGEIVRALSRRLRDNSWTVVFKSLIVLHLMIREGEtDDVLLYYLSRPD 82

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 332688231 103 LFNLSNFLDKSGlQGYDMSTFIRRYSRYLNEKAVSY 138
Cdd:cd16988   83 FLDLRKIRNGSS-AGSGQLQNIQRYAAYLKERVKEY 117
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 19-131 4.41e-18

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: 80.68  E-value: 4.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332688231   19 GSAVSKTVCKATTHEIMGPKKKHLDYLIQCTNEMnVNIPQLADSLFER--TTNSSWVVVFKSLITTHHLMVYGNERFIQY 96
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNY-VEFPEIMKMLWKRlnDKGKNWRHIYKALTLLEYLLKNGSERVVDD 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 332688231   97 L-ASRNTLFNLSNFLDKSGlQGYDMSTFIRRYSRYL 131
Cdd:pfam01417  80 LrENIYIIRTLTDFHYIDE-NGKDQGINVRKKAKEI 114
ANTH_N_AP180_plant cd16987
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of plant Clathrin coat assembly ...
 26-134 7.39e-11

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: 59.94  E-value: 7.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332688231  26 VCKATTHEIMGPKKKHLDYLIQCT--NEMNVN--IPQLADSLfERTTNssWVVVFKSLITTHHLMVYGNERFIQ----YL 97
Cdd:cd16987    5 VVKATSHDDAPPDEKYVREILSLGssSRAYASacVSALSRRL-NRTRD--WVVALKCLMLLHRLLRDGSPILEQelslAP 81

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 332688231  98 ASRNTLFNLSNFLDKSGLQGYDMSTFIRRYSRYLNEK 134
Cdd:cd16987   82 SGGRNPLNLSDFRDGSSSKSWDFSAFVRAYAAYLDER 118
ANTH_N_Sla2p_HIP1_like cd16986
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; ...
 22-136 1.58e-07

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: 50.07  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332688231  22 VSKTVCKATTHEIMGPKKKHLDYLIQCTNEMNvNIPQLADSLFERTTNSSWVVVFKSLITTHHLMVYGNERFI---QYLa 98
Cdd:cd16986    1 FEKAVNKATNKTDSPPKPKHVRTIIVKSWTHQ-KGPQFYEELSKRLLLNNPVVQFKALVTLHKVLRDGPPELSllgGYL- 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 332688231  99 sRNTLFNLSNFLDKSGLQGYDMSTFIRRYSRYLNEKAV 136
Cdd:cd16986   79 -DAWLPELVRVKNTQQSLSEFYSQLIKKYVRYLELKVV 115
ANTH_N_Sla2p cd17007
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; ...
 28-134 4.80e-05

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; This subfamily is composed of Saccharomyces cerevisiae Sla2 protein (Sla2p, also called transmembrane protein MOP2), Schizosaccharomyces pombe endocytosis protein End4 (End4p, also called Sla2 protein homolog), and similar proteins. In yeast, cells lacking Sla2p have severe defects in actin organization, cell morphology, and endocytosis, suggesting roles in these processes. Sla2p regulates the Eps15-like Arp2/3 complex activator, Pan1p, controlling actin polymerization during endocytosis. In fission yeast, End4p has been implicated in cellular morphogenesis. Sla2p contains an N-terminal ANTH, a central 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. The ANTH domain of Sla2p preferentially binds 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 domains f Sla2p and similar proteins.


Pssm-ID: 340804  Cd Length: 115  Bit Score: 43.06  E-value: 4.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332688231  28 KATTHEIMGPKKKHLDYLIQCTNEMNVNIPQLaDSLFERTTNSSWVVVFKSLITTHHLMVYGNERFI-QYLASRNTLFNL 106
Cdd:cd17007    7 KACSSDETAPKRKHVRACIVYTWDHKSSKPFW-NALKTQPLLSDEVQCFKALITIHKVLQEGHPSALkEAIRNIEWLESL 85

                         90       100
                 ....*....|....*....|....*...
gi 332688231 107 SNFLDKSGLQGYdmSTFIRRYSRYLNEK 134
Cdd:cd17007   86 GRQSSGSGAKGY--GRLIKEYVRYLLDK 111
ENTH cd03571
Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is ...
 29-97 2.52e-03

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: 38.27  E-value: 2.52e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332688231  29 ATTHEIMGPKKKHLDYLIQCTNEMNvNIPQLADSLFER--TTNSSWVVVFKSLITTHHLMVYGNERFIQYL 97
Cdd:cd03571    8 ATSNEPWGPTGSQLAEIAQATFDYD-DYQRIMKVLWKRlnDKGKNWRHVYKALTLLEYLLKNGSERVVDEF 77
 
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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