ID Q22601_CAEEL Unreviewed; 925 AA. AC Q22601; DT 01-NOV-1996, integrated into UniProtKB/TrEMBL. DT 01-OCT-2001, sequence version 2. DT 24-JAN-2024, entry version 166. DE RecName: Full=AP-2 complex subunit alpha {ECO:0000256|PIRNR:PIRNR037091}; GN Name=apa-2 {ECO:0000313|EMBL:CCD68583.1, GN ECO:0000313|WormBase:T20B5.1}; GN ORFNames=CELE_T20B5.1 {ECO:0000313|EMBL:CCD68583.1}, T20B5.1 GN {ECO:0000313|WormBase:T20B5.1}; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD68583.1, ECO:0000313|Proteomes:UP000001940}; RN [1] {ECO:0000313|EMBL:CCD68583.1, ECO:0000313|Proteomes:UP000001940} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD68583.1, RC ECO:0000313|Proteomes:UP000001940}; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RA Sulson J.E., Waterston R.; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). CC -!- FUNCTION: Adaptins are components of the adaptor complexes which link CC clathrin to receptors in coated vesicles. Clathrin-associated protein CC complexes are believed to interact with the cytoplasmic tails of CC membrane proteins, leading to their selection and concentration. CC {ECO:0000256|PIRNR:PIRNR037091}. CC -!- INTERACTION: CC Q22601; G5ECW9: rme-4; NbExp=3; IntAct=EBI-5323248, EBI-315316; CC Q22601; Q9GYH7: rme-6; NbExp=3; IntAct=EBI-5323248, EBI-320814; CC -!- SUBCELLULAR LOCATION: Membrane, coated pit CC {ECO:0000256|ARBA:ARBA00004277}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004277}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004277}. CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family. CC {ECO:0000256|PIRNR:PIRNR037091}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX284606; CCD68583.1; -; Genomic_DNA. DR PIR; T16911; T16911. DR RefSeq; NP_509572.1; NM_077171.6. DR AlphaFoldDB; Q22601; -. DR SMR; Q22601; -. DR IntAct; Q22601; 2. DR MINT; Q22601; -. DR STRING; 6239.T20B5.1.1; -. DR EPD; Q22601; -. DR PaxDb; 6239-T20B5-1-1; -. DR PeptideAtlas; Q22601; -. DR EnsemblMetazoa; T20B5.1.1; T20B5.1.1; WBGene00000161. DR UCSC; T20B5.1.1; c. elegans. DR AGR; WB:WBGene00000161; -. DR WormBase; T20B5.1; CE28680; WBGene00000161; apa-2. DR eggNOG; KOG1077; Eukaryota. DR GeneTree; ENSGT00950000182838; -. DR HOGENOM; CLU_003824_1_1_1; -. DR InParanoid; Q22601; -. DR OMA; PVLMHRY; -. DR OrthoDB; 25313at2759; -. DR PhylomeDB; Q22601; -. DR Reactome; R-CEL-3928665; EPH-ephrin mediated repulsion of cells. DR Reactome; R-CEL-437239; Recycling pathway of L1. DR Reactome; R-CEL-5099900; WNT5A-dependent internalization of FZD4. DR Reactome; R-CEL-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2. DR Reactome; R-CEL-6798695; Neutrophil degranulation. DR Reactome; R-CEL-8856825; Cargo recognition for clathrin-mediated endocytosis. DR Reactome; R-CEL-8856828; Clathrin-mediated endocytosis. DR Reactome; R-CEL-8866427; VLDLR internalisation and degradation. DR Reactome; R-CEL-8964038; LDL clearance. DR Proteomes; UP000001940; Chromosome X. DR Bgee; WBGene00000161; Expressed in pharyngeal muscle cell (C elegans) and 4 other cell types or tissues. DR GO; GO:0030122; C:AP-2 adaptor complex; IBA:GO_Central. DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; IDA:WormBase. DR GO; GO:0030139; C:endocytic vesicle; IDA:WormBase. DR GO; GO:0005886; C:plasma membrane; IDA:WormBase. DR GO; GO:0036062; C:presynaptic periactive zone; IDA:WormBase. DR GO; GO:0045202; C:synapse; IDA:WormBase. DR GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central. DR GO; GO:0032794; F:GTPase activating protein binding; IPI:WormBase. DR GO; GO:0072583; P:clathrin-dependent endocytosis; IMP:WormBase. DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase. DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule. DR GO; GO:0008104; P:protein localization; IMP:WormBase. DR GO; GO:0006898; P:receptor-mediated endocytosis; IMP:WormBase. DR Gene3D; 2.60.40.1230; -; 1. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR Gene3D; 3.30.310.10; TATA-Binding Protein; 1. DR InterPro; IPR017104; AP2_complex_asu. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N. DR InterPro; IPR003164; Clathrin_a-adaptin_app_sub_C. DR InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig. DR InterPro; IPR013041; Clathrin_app_Ig-like_sf. DR InterPro; IPR009028; Coatomer/calthrin_app_sub_C. DR InterPro; IPR012295; TBP_dom_sf. DR PANTHER; PTHR22780; ADAPTIN, ALPHA/GAMMA/EPSILON; 1. DR PANTHER; PTHR22780:SF4; AP-2 COMPLEX SUBUNIT ALPHA; 1. DR Pfam; PF01602; Adaptin_N; 1. DR Pfam; PF02296; Alpha_adaptin_C; 1. DR Pfam; PF02883; Alpha_adaptinC2; 1. DR PIRSF; PIRSF037091; AP2_complex_alpha; 1. DR SMART; SM00809; Alpha_adaptinC2; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR SUPFAM; SSF49348; Clathrin adaptor appendage domain; 1. DR SUPFAM; SSF55711; Subdomain of clathrin and coatomer appendage domain; 1. PE 1: Evidence at protein level; KW Coated pit {ECO:0000256|ARBA:ARBA00023176, ECO:0000256|PIRNR:PIRNR037091}; KW Endocytosis {ECO:0000256|ARBA:ARBA00022583, ECO:0000256|PIRNR:PIRNR037091}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR037091}; KW Protein transport {ECO:0000256|ARBA:ARBA00022927, KW ECO:0000256|PIRNR:PIRNR037091}; KW Proteomics identification {ECO:0007829|EPD:Q22601, KW ECO:0007829|PeptideAtlas:Q22601}; KW Reference proteome {ECO:0000313|Proteomes:UP000001940}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037091}. FT DOMAIN 688..806 FT /note="Clathrin adaptor alpha/beta/gamma-adaptin appendage FT Ig-like subdomain" FT /evidence="ECO:0000259|SMART:SM00809" FT REGION 623..644 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 623..637 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 10..11 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol-3,4,5-trisphosphate)" FT /ligand_id="ChEBI:CHEBI:57836" FT /evidence="ECO:0000256|PIRSR:PIRSR037091-1" FT BINDING 42 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol-3,4,5-trisphosphate)" FT /ligand_id="ChEBI:CHEBI:57836" FT /evidence="ECO:0000256|PIRSR:PIRSR037091-1" FT BINDING 52 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol-3,4,5-trisphosphate)" FT /ligand_id="ChEBI:CHEBI:57836" FT /evidence="ECO:0000256|PIRSR:PIRSR037091-1" FT BINDING 56..60 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol-3,4,5-trisphosphate)" FT /ligand_id="ChEBI:CHEBI:57836" FT /evidence="ECO:0000256|PIRSR:PIRSR037091-1" SQ SEQUENCE 925 AA; 104180 MW; A816ADC042FD557C CRC64; MPAVKGDGMR GLAVFISDIR NCKSKEAELK RINKELANIR SKFKGDKTLD GYQKKKYVCK LLFIFLLGND IDFGHMEAVN LLSSNKYTEK QIGYLFISVL IEQQSDLMKL IVQGIRNDLT SRNPVHVNLA LQCISNMGSR EMVEAFCTDL PKLLVSGETI DFVKQSAALC ILKLFRNSPD SFQPGDYASR IVHLLNDSHM GVVTSAASLI EALSKKWPEE YKGAVPLAIS RLSRIVTATY TDLQDYTYYF VPAPWLCVKL LRLLQNYPPP DDPSNKARLL ECLEGILNKA QDAPKSKKVQ HSNAKNAVLF EAIALIIHMD SEPQLLVRAC NQLGTFLSHR ETNLRYLALE SMCLLATSEF SHDAVKKHQD TIINSLKTER DVSVRQRAVD LLYAMCDRSN ANQIVAEMLA YLETADYSIR EEMVLKVAIL AEKYATDYTW YVDVILKLIR IAGDYVSEEV WYRVIQIVVN REDVQGYAAK TVFEALQRPA CHENMVKVGG YILGEFGNFI AGDERSTAKI QFELLHSKFH LCSITTRCLL LTTYIKFCNL FPEIKPLVQQ VFQTDHNLRN PDAELQQRSI EYLQMTKLAS NDVLATILEV MPAFAEKESS LLAKLKKSKP QLEEIEREEK EKRSKPTAVM SEGSTSLVDF DSTNDTTASL ADVFANNSGT GLGAQGDEVE IANKDDYLKF VTKSNAILWE DDYIQIGCKL ETRNNLGRLG MFYGNKTSQP FNKFTPIITC PGALAVQLQA QAKPVEPVVA AGTQVQQLIN FVCVQEFQKM PIMNIKFTFT DRAGAVQNFD KNFYLPLFIS KFFEPTNMTS EQFFTRWKSL GAASQEAQKI FNALSPIEHA TIESRLKGFG ANLLTDVDPN PDNYVCAGII HTQTQQIGTL IRLEPNKQAK MYRLTIRSSK DTVVQTLVDL LGNQF //