ID A0A1L0G634_9ASCO Unreviewed; 998 AA.
AC A0A1L0G634;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=AP-2 complex subunit alpha {ECO:0000256|PIRNR:PIRNR037091};
GN ORFNames=SAMEA4029010_CIC11G00000002849 {ECO:0000313|EMBL:SGZ52013.1};
OS [Candida] intermedia.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=45354 {ECO:0000313|EMBL:SGZ52013.1, ECO:0000313|Proteomes:UP000182334};
RN [1] {ECO:0000313|EMBL:SGZ52013.1, ECO:0000313|Proteomes:UP000182334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 141442 {ECO:0000313|EMBL:SGZ52013.1,
RC ECO:0000313|Proteomes:UP000182334};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Membrane, coated pit
CC {ECO:0000256|PIRNR:PIRNR037091}.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000256|PIRNR:PIRNR037091}.
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DR EMBL; LT635758; SGZ52013.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L0G634; -.
DR STRING; 45354.A0A1L0G634; -.
DR OrthoDB; 123661at2759; -.
DR Proteomes; UP000182334; Chromosome iii.
DR GO; GO:0030122; C:AP-2 adaptor complex; IEA:InterPro.
DR GO; GO:0035615; F:clathrin adaptor activity; IEA:InterPro.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
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; 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; 2.
DR PIRSF; PIRSF037091; AP2_complex_alpha; 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 3: Inferred from homology;
KW Coated pit {ECO:0000256|PIRNR:PIRNR037091};
KW Endocytosis {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 Reference proteome {ECO:0000313|Proteomes:UP000182334};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037091}.
FT DOMAIN 24..138
FT /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01602"
FT DOMAIN 186..636
FT /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01602"
FT REGION 706..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38
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 46
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 50..54
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 998 AA; 111844 MW; 2686A89966FDDFB8 CRC64;
MAPQMKGLTQ FITDLRNSHD YDEERKRINV EINNIRTKFA SGMNSYQKKK YVCKLIYMHL
LGYTEEVKFG LVQSLDLIRL PDYLEKLLGY LLVSVLFTRD GGTLLEFYSD LLDLVHPELV
LDLRANSEDV NCLALQFIAA NFNVMPENGL VLFEPVVSDG HADAVLWQEI IDMVYSFCVS
PIARANTKKR AVTALNVLLK LYPQVILNND NWIPRLLTLV DETDLSVVLS AVPLVRLLTD
VSPHYAKSIV PSIANRLYAL VVDQDCPREY FYYDNPSPWL VINLIQLVEH FFLPSEQLKV
VPLTTAVLDN STVSKLRQVV SRSIQNASKS VKGLPNRNSQ SAILFQAVSL ATFLDASPEA
IEGAIHALLT LLDSSETNTR YLVLDALIKL SARTKHTSFF NEALENIFKC LHDKDVSVRK
KTVDLLFTIC DSSTYTSIIS KFLDYYPVAE SSLKVDIAVK VAVLAEQFAT DSIWYVSTML
RLLALGGQSS KTTGVTNRSN VEVWERITQI VVNNEDLHTK ASRYIINLLR KAEGGTVPEN
LVKVAAFILG EFGYKLVDKD DASSHFTPSK QFQLLFEAYF KVSLASRPII LTAFLKFIYR
FSLEDYVPDI LDLLEAETQS LDLEIQTRAY EYLKVASYMV SGDEADRRFA KSLITSMPPF
ENKKNTLLNY LGSVKLVNGR SSSTVNVLKI PNHSVLVNAI KSTKDIPERS TSPNSGYSDE
EHFDETTNDP FGDGLTELPQ LSPNWYPGYH RMLQYDAGIF YEDQLVKITY RTTKEAHNIH
VQFSIINNAA KTASATITAF TVREIHNAFR GTDPAYIVSL TQVPELTIQV KSNMEIDVKV
RDIFENSQSP VLSLTYKCSG SFNTLNLKVP TVLIKTLSGT ALGSLDEFKK RWLQIGEHLG
TVDGERRGVI SAQFRHSSSN IVRILQRIGF AIVHSTQDSE EGVLVMGAGI LHTMKSKSGV
LVTMKSLDQV GKEFDIVVRS TGGGVSGTIY ETLEEIFL
//
