ID A0A3Q2DUK4_CYPVA Unreviewed; 841 AA.
AC A0A3Q2DUK4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=AP-2 complex subunit alpha-2-like {ECO:0000313|Ensembl:ENSCVAP00000023523.1};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000023523.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000023523.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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|ARBA:ARBA00006613}.
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DR AlphaFoldDB; A0A3Q2DUK4; -.
DR STRING; 28743.ENSCVAP00000023523; -.
DR Ensembl; ENSCVAT00000006522.1; ENSCVAP00000023523.1; ENSCVAG00000006957.1.
DR GeneTree; ENSGT00950000182838; -.
DR OMA; PVLMHRY; -.
DR Proteomes; UP000265020; Unplaced.
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:InterPro.
DR Gene3D; 2.60.40.1230; -; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
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:SF30; AP-2 COMPLEX SUBUNIT ALPHA-2; 1.
DR Pfam; PF01602; Adaptin_N; 2.
DR Pfam; PF02296; Alpha_adaptin_C; 1.
DR Pfam; PF02883; Alpha_adaptinC2; 1.
DR PIRSF; PIRSF037091; AP2_complex_alpha; 3.
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 3: Inferred from homology;
KW Coated pit {ECO:0000256|ARBA:ARBA00023176};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000265020};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 609..722
FT /note="Clathrin adaptor alpha/beta/gamma-adaptin appendage
FT Ig-like subdomain"
FT /evidence="ECO:0000259|SMART:SM00809"
FT BINDING 11..12
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 43
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 53
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 57..61
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 841 AA; 94024 MW; A7120497EF56CDFA CRC64;
MPTVSKGDGM RGLAVFISDI RNCKSKEAEV KRINKELANI RSKFKGDKAL DGYSKKKYVC
KLLFIFLLGH DIDFGHMEAV NLLSSNKYTE KQIGYLFISV LVNSNSDLIR LINNAIKNDL
ASRNPTFMNL ALHCIANVGS REMAEAQKQI CFLTWICSCF QGVVTAATSL ITTLAQKSPD
DFKTSVCLAV ARLSRIVTSA SLDLQDYTYY FVAAPWLSVK LLRLLQCYPP PEDAALRSRL
TECLETILNK AQEPPKSKKV QHSNAKNAVL FEAIALIIHH DSEPNLLVRA CNQLGHFLQH
RETNLRYLAL ESMCTLASSE FSHEAVKTHI ETVINALKTE RDVSVRQRAV DLLYAMCDRS
NSKQIVAEML SYLETADYSI REEIVLKVAI LAEKYAVDYT WYVDTILNLI RIAGDYVSEE
VWYRVIQIVI NQDDVQGYAA KTVFEALQAP ACHENLVKVG GYILGEFGNL IAGDPRSSPL
VQFNLLHSKF HLCSVPTRAL LLSAYIKFIN LFPEVKGTIQ DVLRSDSQLR NADVELQQRA
VEYLRLSCIA STDILVSKNS AKRASSPSLG FNDALNLNST PSSGASLLVD VFTDLSNPAP
TEGSDEHFTR FVCKNNGVIY ENQLLQIGLK SEYRQNLGRI YVFYGNKTST QFLSFSTSVT
SNDLLTPQLN VQVKPVDPLI EAGAQLQQIL NIECVSDFSE APVLNIQFRY GGTLQNITVK
LPVMLNKFFQ PTEMTSQDFF QRWKQLGAPQ QEVQKIFKAK NQMDTDVAKA KLLGFGVALL
DGVDPNPANF VGAGIIHTKT TQVGCLLRLE PNTQAQMYRL TLRTSKESVS QRLCELLSEQ
F
//
