ID   AP2A_ANOGA              Reviewed;         934 AA.
AC   Q7QG73;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 4.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=AP-2 complex subunit alpha;
DE   AltName: Full=Alpha-adaptin;
GN   Name=alpha-Adaptin {ECO:0000250|UniProtKB:P91926}; ORFNames=AGAP009538;
OS   Anopheles gambiae (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEST;
RX   PubMed=12364791; DOI=10.1126/science.1076181;
RA   Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA   Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA   Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA   Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA   Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA   Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA   Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA   Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA   Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA   Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA   Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA   Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA   McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA   O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA   Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA   Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA   Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA   Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA   Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA   Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA   Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA   Collins F.H., Hoffman S.L.;
RT   "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL   Science 298:129-149(2002).
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}.
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DR   EMBL; AAAB01008839; EAA05923.4; -; Genomic_DNA.
DR   RefSeq; XP_310153.4; XM_310153.4.
DR   AlphaFoldDB; Q7QG73; -.
DR   SMR; Q7QG73; -.
DR   STRING; 7165.AGAP009538-PA; -.
DR   PaxDb; Q7QG73; -.
DR   PRIDE; Q7QG73; -.
DR   GeneID; 1271372; -.
DR   KEGG; aga:AgaP_AGAP009538; -.
DR   CTD; 1271372; -.
DR   VEuPathDB; VectorBase:AGAP009538; -.
DR   eggNOG; KOG1077; Eukaryota.
DR   HOGENOM; CLU_003824_1_0_1; -.
DR   InParanoid; Q7QG73; -.
DR   OMA; SPIEQFM; -.
DR   OrthoDB; 751651at2759; -.
DR   PhylomeDB; Q7QG73; -.
DR   Proteomes; UP000007062; Chromosome 3R.
DR   GO; GO:0030122; C:AP-2 adaptor complex; IBA:GO_Central.
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:0140312; F:cargo adaptor activity; IBA:GO_Central.
DR   GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR   GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
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..934
FT                   /note="AP-2 complex subunit alpha"
FT                   /id="PRO_0000278176"
FT   REGION          623..670
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        633..670
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   934 AA;  104378 MW;  87F5BA86D152BDCA CRC64;
     MAPVRGDGMR GLAVFISDIR NCKSKEAEIK RINKELANIR SKFKGDKTLD GYQKKKYVCK
     LLFIFLLGHD IDFGHMEAVN LLSSNKYSEK QIGYLFISVL VNTNSDLIKL IIQSIKNDLQ
     SRNPIHVNLA LQCIANIGSQ DMAEAFSNEI PKLLVSGDTM DVVKQSAALC LLRLFRTCPD
     IIPGGEWTSR IIHLLNDQHM GVVTAATSLI DALVKKNPEE YKGCVSLAVS RLSRIVTASY
     TDLQDYTYYF VPAPWLSVKL LRLLQNYNPP TEDPGVRGRL NECLETILNK AQEPPKSKKV
     QHSNAKNAVL FEAINLIIHN DSEPSLLVRA CNQLGQFLSN RETNLRYLAL ESMCHLATSE
     FSHEAVKKHQ EVVILSMKME KDVSVRQQAV DLLYAMCDRS NAEEIVQEML NYLETADYSI
     REEMVLKVAI LAEKYATDYT WYVDVILNLI RIAGDYVSEE VWYRVIQIVI NREEVQGYAA
     KTVFEALQAP ACHENMVKVG GYILGEFGNL IAGDSRSAPM VQFKLLHSKY HLCSSMTRAL
     LLSTYIKFIN LFPEIRGTIQ DVFRQHSNLR SADAELQQRA SEYLQLSIVA STDVLATVLE
     EMPSFPERES SILAVLKKKK PGRVPENAEI RETKSPVPNS HNNAHSNAQT NHTSSANNAN
     ASSDLLGLST PPASQSGTLI DVLGDIYSTA NGNSNVVNNS KKFVFKNNGV LFENDLLQIG
     VKSEFRQNLG RLGLYYGNKT QTALQNFVPT LQWSAEDALK LNVQIKAVEP TLEAGAQIQQ
     LLTAECIDHY LGAPSIVISF RVSGGAPQKI TVNLPLTINK FFEPTEMNAE SFFARWRNLG
     GEQQRAQRVF KAQQPLDLPG ARNKLTGFGM QLLDSIDPNP DNMVCAGIIH TQAHKVGCLL
     RLEPNKQAQM FRLTIRSSLE AVTQEICDLL VDQF