ID A0A163JPG1_ABSGL Unreviewed; 967 AA.
AC A0A163JPG1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 13-SEP-2023, entry version 33.
DE RecName: Full=AP-2 complex subunit alpha {ECO:0000256|PIRNR:PIRNR037091};
GN Name=ABSGL_06589.1 scaffold 8461 {ECO:0000313|EMBL:SAM00863.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM00863.1};
RN [1] {ECO:0000313|EMBL:SAM00863.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM00863.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-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|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; LT553433; SAM00863.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163JPG1; -.
DR STRING; 4829.A0A163JPG1; -.
DR InParanoid; A0A163JPG1; -.
DR OMA; PVLMHRY; -.
DR OrthoDB; 123661at2759; -.
DR Proteomes; UP000078561; Unassembled WGS sequence.
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; 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 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000078561};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037091}.
FT DOMAIN 736..842
FT /note="Clathrin adaptor alpha/beta/gamma-adaptin appendage
FT Ig-like subdomain"
FT /evidence="ECO:0000259|SMART:SM00809"
FT BINDING 2..3
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 65
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 69..73
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 967 AA; 108789 MW; AB14CCE265CFD185 CRC64;
MRGLTLFIAD IRNYDGIYLP TRLSPFCWLY VGRVRELEEK RINKEMANIR SKFKGIKAKG
NLNGYQKKKY VCKLLYMYIL GWDIEFGHLE AVNLISSQVY SEKQIGYLAV TLLFHENSDL
VRLVVNSTKK DLDDMNEINN CLALHAIANI GGREMAETLA NDVHRLLISP TSKSFVKKKA
ALTLLRLFRK YPDVIPVTDW AERIVNLMDE YDLGVALSVT TLVLVLAQTY PLEYGACYGK
AVNRLKRILV DRDYSLDYIY YKVPTPWLQV KCLRLLQYYP PPDDPKLRSD ISELLQIILT
NSQDAPKNVQ HSNAQNAVLF EAINLAIHLD SNSTICAQAA ALLGRFISSK ETNVRYLGLD
TMAHLAACVD SLAPIKRHQE TILMSLRDKD ISVRRRGLDL LYSMCDTSNA KIIVSELLRY
LQVADFAMRE EMVLKIAILA EKFATAYSWY VDIILQLIST AGEQVGEEVW YRVVQIVTNN
EELQEYAAKT VLNYLNFPQY NETMVKVGAY ILGEFGHLIA NYPGSSPIEQ FNAVHSKFNL
CSLQTRALML TTYVKFVNLF PEIKGQVLDV FNQYRYVLDS ELQQRACEYL AISTMPTDDM
LQTVCEEMPP FPERESTLLL KLNQKHGDTE DKRVWVIGGK EANVEQQDGL KRIATLRANS
YSESGSSPKQ IMPASPSANI TMATTSTAVA MTTNSLPTTP SHDLLGLDDL SLQDPPTVKA
LPTNIPLAPG YELGFNRLHY TQEGVLYEDS QVQISVKSEY HGHQGRLAIY ISNKLTFPMS
QISVQTSDHD SFLVNVAAPH QHTIAPGAQV QRLVQIECRD AFSEPPSLFI GFNDQMLHLK
LPVVLTKFQE PVEMDGQSFF KRWNQIGGPP RENQAIFNSP GPIKLDQVGA ILRGFRFGLL
QGVDPNANNF VGVGIISAGA KGGKIGALLR LEPNMEQNMY RLTVRTPSET VSEHIRSILQ
QSLANGL
//
