ID   AP2A_DROPS              Reviewed;         939 AA.
AC   Q29N38;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=AP-2 complex subunit alpha;
DE   AltName: Full=Alpha-adaptin;
GN   Name=alpha-Adaptin {ECO:0000250|UniProtKB:P91926}; ORFNames=GA18063;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1] {ECO:0000312|EMBL:EAL33505.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
CC   -!- FUNCTION: Adaptins are components of the adapter 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. Alpha
CC       adaptin is a subunit of the plasma membrane adapter (By similarity).
CC       {ECO:0000250|UniProtKB:P91926}.
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 AP50) and a small adaptin (sigma-type subunit
CC       AP17). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P91926};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:P91926}; Cytoplasmic
CC       side {ECO:0000250|UniProtKB:P91926}. Membrane, coated pit
CC       {ECO:0000250|UniProtKB:P91926}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P91926}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P91926}. Note=Component of the coat surrounding
CC       the cytoplasmic face of coated vesicles in the plasma membrane.
CC       {ECO:0000250|UniProtKB:P91926}.
CC   -!- SIMILARITY: Belongs to the adapter complexes large subunit family.
CC       {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL33505.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH379060; EAL33505.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001356441.1; XM_001356405.3.
DR   AlphaFoldDB; Q29N38; -.
DR   SMR; Q29N38; -.
DR   STRING; 7237.FBpp0280380; -.
DR   EnsemblMetazoa; FBtr0281942; FBpp0280380; FBgn0078071.
DR   GeneID; 4817178; -.
DR   KEGG; dpo:Dpse_GA18063; -.
DR   eggNOG; KOG1077; Eukaryota.
DR   HOGENOM; CLU_003824_1_0_1; -.
DR   InParanoid; Q29N38; -.
DR   OMA; SPIEQFM; -.
DR   PhylomeDB; Q29N38; -.
DR   Proteomes; UP000001819; Chromosome 4.
DR   Bgee; FBgn0078071; Expressed in insect adult head and 2 other tissues.
DR   GO; GO:0030122; C:AP-2 adaptor complex; IEA:InterPro.
DR   GO; GO:0005905; C:clathrin-coated pit; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
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   GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR   GO; GO:0048488; P:synaptic vesicle endocytosis; ISS:UniProtKB.
DR   Gene3D; 1.25.10.10; -; 1.
DR   Gene3D; 3.30.310.10; -; 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   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; SSF48371; 1.
DR   SUPFAM; SSF49348; SSF49348; 1.
DR   SUPFAM; SSF55711; SSF55711; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Coated pit; Endocytosis; Membrane; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..939
FT                   /note="AP-2 complex subunit alpha"
FT                   /id="PRO_0000278177"
FT   REGION          623..660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        632..660
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   939 AA;  105412 MW;  34048C584401C6F0 CRC64;
     MAPVRGDGMR GLAVFISDIR NCKSKEAEVK RINKELANIR SKFKGDKTLD GYQKKKYVCK
     LLFIFLLGHD IDFGHMEAVN LLSSNKYSEK QIGYLFISVL VNTNSDLIRL IIQSIKNDLQ
     SRNPVHVNLA LQCIANIGSR DMAESFSNEI PKLLVSGDTM DVVKQSAALC LLRLFRSSPD
     IIPGGEWTSR IIHLLNDQHM GVVTAATSLI DALVKCNPDE YKGCVNLAVS RLSRIVTASY
     TDLQDYTYYF VPAPWLSVKL LRLLQNYNPV TEEAGVRARL NETLETILNK AQEPPKSKKV
     QHSNAKNAVL FEAINLIIHS DSEPNLLVRA CNQLGQFLSN RETNLRYLAL ESMCHLATSE
     FSHEEVKKHQ EVVILSMKME KDVSVRQMAV DLLYAMCDRG NAEEIVQEML NYLETADYSI
     REEMVLKVAI LAEKYATDYT WYVDVILNLI RIAGDYVSEE VWYRVIQIVI NREEVQGYAA
     KTVFEALQAP ACHENMVKVG GYILGEFGNL IAGDSRSAPL VQFKLLHSKY HLCSPMTRAL
     LLSTYIKFIN LFPEIRTNIQ DVFRQHSNLR SADAELQQRA SEYLQLSIVA STDVLATVLE
     EMPSFPERES SILAVLKKKK PGRVPENEIR ESKSPAPTSG PGSVLQNNVH VNNSHSKLNN
     SNANTDLLGL STPPANNVGS NSNSTLIDVL GDIYGSNNNS SAVYNTKKFL FKNNGVLFEN
     EMLQIGVKSE FRQNLGRLGL FYGNKTQVPL SNFNPVLQWS AEETLKLNVQ MKAVEPTLEA
     GAQIQQLLTA ECIEDYADAP TIEISFRYNG TQQKFSIKLP LSVNKFFEPT EMNAESFFAR
     WKNLSGEQQR SQKVFKAAQP LDLPGARNKL MGFGMQLLDS VDPNPDNMVC AGIIHTQSQQ
     VGCLMRLEPN KQAQMFRLTV RASKETVTRE ICDLLADQF