ID A0A2K6SW34_SAIBB Unreviewed; 945 AA.
AC A0A2K6SW34;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=AP-2 complex subunit alpha {ECO:0000256|PIRNR:PIRNR037091};
GN Name=AP2A1 {ECO:0000313|Ensembl:ENSSBOP00000011587.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000011587.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000011587.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor
CC protein complexes function in protein transport via transport vesicles
CC in different membrane traffic pathways. Adaptor protein complexes are
CC vesicle coat components and appear to be involved in cargo selection
CC and vesicle formation. AP-2 is involved in clathrin-dependent
CC endocytosis in which cargo proteins are incorporated into vesicles
CC surrounded by clathrin (clathrin-coated vesicles, CCVs) which are
CC destined for fusion with the early endosome. The clathrin lattice
CC serves as a mechanical scaffold but is itself unable to bind directly
CC to membrane components. Clathrin-associated adaptor protein (AP)
CC complexes which can bind directly to both the clathrin lattice and to
CC the lipid and protein components of membranes are considered to be the
CC major clathrin adaptors contributing the CCV formation. AP-2 also
CC serves as a cargo receptor to selectively sort the membrane proteins
CC involved in receptor-mediated endocytosis. AP-2 seems to play a role in
CC the recycling of synaptic vesicle membranes from the presynaptic
CC surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-
CC [LI] endocytosis signal motifs within the cytosolic tails of
CC transmembrane cargo molecules. AP-2 may also play a role in maintaining
CC normal post-endocytic trafficking through the ARF6-regulated, non-
CC clathrin pathway. The AP-2 alpha subunit binds polyphosphoinositide-
CC containing lipids, positioning AP-2 on the membrane. The AP-2 alpha
CC subunit acts via its C-terminal appendage domain as a scaffolding
CC platform for endocytic accessory proteins. The AP-2 alpha and AP-2
CC sigma subunits are thought to contribute to the recognition of the
CC [ED]-X-X-X-L-[LI] motif. {ECO:0000256|PIRNR:PIRNR037091}.
CC -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer composed
CC of two large adaptins (alpha-type subunit AP2A1 or AP2A2 and beta-type
CC subunit AP2B1), a medium adaptin (mu-type subunit AP2M1) and a small
CC adaptin (sigma-type subunit AP2S1). {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|ARBA:ARBA00006613, ECO:0000256|PIRNR:PIRNR037091}.
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DR AlphaFoldDB; A0A2K6SW34; -.
DR Ensembl; ENSSBOT00000028373.1; ENSSBOP00000011587.1; ENSSBOG00000022105.1.
DR GeneTree; ENSGT00950000182838; -.
DR Proteomes; UP000233220; 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: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:SF33; AP-2 COMPLEX SUBUNIT ALPHA-1; 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:UP000233220};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037091}.
FT DOMAIN 723..844
FT /note="Clathrin adaptor alpha/beta/gamma-adaptin appendage
FT Ig-like subdomain"
FT /evidence="ECO:0000259|SMART:SM00809"
FT REGION 615..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 945 AA; 104159 MW; 6D780A0FCF13E03A CRC64;
MPAVSKGDGM RGLAVFISDI RNCKSKEAEI KRINKELANI RSKFKGDKAL DGYSKKKYVC
KLLFIFLLGH DIDFGHMEAV NLLSSNKYTE KQIGYLFISV LVNSNSELIR LINNAIKNDL
ASRNPTFMCL ALHCIANVGS REMGEAFAAD IPRILVAGDS MDSVKQSAAL CLLRLYKASP
DLVPMGEWTA RVVHLLNDQH MGVVTAAVSL ITCLCKKNPD DFKTCISLAV SRLSRIVSSA
STDLQDYTYY FVPAPWLSVK LLRLLQCYPP PEDAAVKGRL VECLETVLNK AQEPPKSKKV
QHSNAKNAIL FETISLIIHY DSEPNLLVRA CNQLGQFLQH RETNLRYLAL ESMCTLASSE
FSHEAVKTHI DTVINALKTE RDVSVRQRAA DLLYAMCDRS NAKQIVSEML RYLETADYAI
REEIVLKVAI LAEKYAVDYS WYVDTILNLI RIAGDYVSEE VWYRVLQIVT NRDDVQGYAA
KTVFEALQAP ACHENMVKVG GYILGEFGNL IAGDPRSSPP VQFSLLHSKF HLCSVATRAL
LLSTYIKFIN LFPETKATIQ GVLRAGSQLR NADVELQQRA VEYLTLSSVA STDVLATVLE
EMPPFPERES SILAKLKRKK GPGAASALDD GRRDPSSNDI NGGVEPTPST VSTPSPSADL
LGLRAAPPPA APPASAGAGN LLVDVFDGPA AQPSLGPTPE EAFLSPGPED IGPPIPEADE
LLNKFVCKNN GVLFENQLLQ IGVKSEFRQN LGRMYLFYGN KTSVQFQNFS PTVVHPGDLQ
THILSGLGQP PTKRVAAQVD GGAQVQQVLN IECLRDFLTP PLLSLPVTIN KFFQPTEMAA
QDFFQRWKQL SLPQQEAQKI FKANHPMDAE VTKAKLLGFG SALLDNVDPN PENFVGAGII
QTKALQVGCL LRLEPNAQAQ MYRLTLRTSK EPVSRHLCEL LAQQF
//
