ID A0A151X1G5_9HYME Unreviewed; 921 AA.
AC A0A151X1G5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 13-SEP-2023, entry version 28.
DE RecName: Full=AP-2 complex subunit alpha {ECO:0000256|PIRNR:PIRNR037091};
GN ORFNames=ALC60_07067 {ECO:0000313|EMBL:KYQ54033.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ54033.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ54033.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ54033.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ54033.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Adaptins are components of the adapter complexes which link
CC clathrin to receptors in coated vesicles.
CC {ECO:0000256|PIRNR:PIRNR037091}.
CC -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer composed
CC of two large adaptins (alpha-type and beta-type subunits), a medium
CC adaptin (mu-type subunit) and a small adaptin (sigma-type subunit).
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}.
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DR EMBL; KQ982600; KYQ54033.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151X1G5; -.
DR STRING; 64791.A0A151X1G5; -.
DR Proteomes; UP000075809; 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:UP000075809};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037091}.
FT DOMAIN 688..801
FT /note="Clathrin adaptor alpha/beta/gamma-adaptin appendage
FT Ig-like subdomain"
FT /evidence="ECO:0000259|SMART:SM00809"
FT REGION 605..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 24
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 34
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 38..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"
SQ SEQUENCE 921 AA; 103312 MW; 97F0AC7214A370BE CRC64;
MLLGKSKEAE IKRINKELAN IRSKFKGDKT LDGYQKKKYV CKLLFIFLLG HDIDFGHMEA
VNLLSSNKYS EKQIGYLFIS VLVNTNSDLI KLIIQSIKND LASRNPIHVN LALQCIANIG
SKEMAEAFGN EIPKLLVSGD TMDVVKQSAA LCLLRLLRTA PDVVPGGEWT SRIVHLLNDQ
HLGVVTAAAS LIDALVKRNP DEYKGCVSLA VSRLSRIVTS SYTDLQDYTY YFVPAPWLSV
KLLRLLQNYT PPAEDPGVRG RLNECLETIL NKAQEPPKSK KVQHSNAKNA VLFEAISLII
HNDSEANLLV RACNQLGQFL SNRETNLRYL ALESMCHLAT SEFSHEAVKK HQEVVILSMK
MEKDVSVRQQ AVDLLYAMCD KSNAEEIVQE MLNYLETADY SIREEMVLKV AILAEKYATD
YTWYVDVILN LIRIAGDYVS EEVWYRVIQI VINRDDVQGY AAKTVFEALQ APACHENMVK
VGGYILGEFG NLIAGDQRSS PAVQFQLLHS KYHLCSPMTR ALLLSTYIKF VNLFPEIRSQ
IQDVFRQHSN LRSADAELQQ RASEYLQLSI IASTDVLATV LEEMPAFPER ESSILAVLKK
KKPGRVPENE IRESKSPAPN TNHHTEPPAA ATTVTVNNSS ADLLGLSTPP SSQPSSNTGV
LLDVLGDIYN MPNKLGTTNG TQNTYNPKKF VCKNNGVLFE NDLIQIGVKS EFRQNLGRVG
LFYGNKTQYA LHSFQPQLSW TDENQAKLAV QVKPVDPILE AGAQIQQMIN AECIDDYNDS
PSMIISFIYN NVPQKITMKL PLTINKFFEP TEMNGESFFA RWKNLGGTNQ QRSQKIFKAQ
QPMDLTQVRT KLQGFGMQLL DGIDPNPDNF VCAGIVHMRA QQVGCLLRLE PNKQAQMFRL
TVRSSKETMS VEICDLLVDQ F
//
