ID   AP2A_SCHPO              Reviewed;         878 AA.
AC   Q9C0W7; O13623; O13624;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 128.
DE   RecName: Full=AP-2 complex subunit alpha;
DE   AltName: Full=Alpha-adaptin;
DE   AltName: Full=Clathrin assembly protein complex 2 alpha large chain;
DE   AltName: Full=Clathrin assembly protein large alpha chain;
GN   Name=apl3; ORFNames=pi033, SPBC691.03c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=10620777;
RX   DOI=10.1002/(sici)1097-0061(20000115)16:1<71::aid-yea505>3.0.co;2-5;
RA   Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K.,
RA   Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y.,
RA   Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.;
RT   "A 38 kb segment containing the cdc2 gene from the left arm of fission
RT   yeast chromosome II: sequence analysis and characterization of the genomic
RT   DNA and cDNAs encoded on the segment.";
RL   Yeast 16:71-80(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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. Alpha
CC       adaptin is a subunit of the plasma membrane adaptor (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer composed
CC       of two large adaptins (alpha-type subunit apl3 and beta-type subunit
CC       apl1), a medium chain (mu-type subunit apm4) and a small adaptin
CC       (sigma-type subunit aps2). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Membrane, coated pit
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Note=Component of the coat surrounding the
CC       cytoplasmic face of coated vesicles in the plasma membrane.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC       {ECO:0000305}.
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DR   EMBL; CU329671; CAC37364.1; -; Genomic_DNA.
DR   EMBL; AB004535; BAA21411.1; -; Genomic_DNA.
DR   EMBL; AB004536; BAA21412.1; -; Genomic_DNA.
DR   RefSeq; NP_595595.1; NM_001021491.2.
DR   AlphaFoldDB; Q9C0W7; -.
DR   SMR; Q9C0W7; -.
DR   BioGRID; 277677; 7.
DR   STRING; 4896.SPBC691.03c.1; -.
DR   MaxQB; Q9C0W7; -.
DR   PaxDb; Q9C0W7; -.
DR   PRIDE; Q9C0W7; -.
DR   EnsemblFungi; SPBC691.03c.1; SPBC691.03c.1:pep; SPBC691.03c.
DR   GeneID; 2541162; -.
DR   KEGG; spo:SPBC691.03c; -.
DR   PomBase; SPBC691.03c; apl3.
DR   VEuPathDB; FungiDB:SPBC691.03c; -.
DR   eggNOG; KOG1077; Eukaryota.
DR   HOGENOM; CLU_003824_1_0_1; -.
DR   InParanoid; Q9C0W7; -.
DR   OMA; SPIEQFM; -.
DR   PhylomeDB; Q9C0W7; -.
DR   Reactome; R-SPO-437239; Recycling pathway of L1.
DR   Reactome; R-SPO-6798695; Neutrophil degranulation.
DR   Reactome; R-SPO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-SPO-8856828; Clathrin-mediated endocytosis.
DR   Reactome; R-SPO-8866427; VLDLR internalisation and degradation.
DR   Reactome; R-SPO-8964038; LDL clearance.
DR   PRO; PR:Q9C0W7; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0030122; C:AP-2 adaptor complex; EXP:PomBase.
DR   GO; GO:0005938; C:cell cortex; HDA:PomBase.
DR   GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR   GO; GO:0032153; C:cell division site; IDA:PomBase.
DR   GO; GO:0005905; C:clathrin-coated pit; EXP:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0140312; F:cargo adaptor activity; IBA:GO_Central.
DR   GO; GO:0035615; F:clathrin adaptor activity; EXP:PomBase.
DR   GO; GO:0072583; P:clathrin-dependent endocytosis; EXP:PomBase.
DR   GO; GO:0006886; P:intracellular protein transport; IC:PomBase.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
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..878
FT                   /note="AP-2 complex subunit alpha"
FT                   /id="PRO_0000193736"
SQ   SEQUENCE   878 AA;  100079 MW;  1EDBB442A61FDDBD CRC64;
     MVASNNMKGL RAFISDLRSL EHDDEEKRVN VELAKIRAKF QSSTLSAYDR KKYVSKLLYI
     YMLGYPITFG HMEAAKLLSG TKYSEKLIGY LAVALLLNEN HELMKLVINS IKKDLLSHDS
     LQNSLALHTI ANIGGRELCE TVYYDIYKLL MSASNENIVR QKSALALLHI YRKFPDLINP
     EWFEPIVMIL GDDDLNVSLA VSNFVNLIVI REPKYQKFAY GKAVGKLKNI VFEHGYSSDY
     LYYSVPCPWL QVNLCRILLA CERPSDNPTR ATLIRVLDRI LSLPNDNSNV QQVNAVNAIL
     FEAIKLAFLV DESHSLYEKC MDRLADMIAD KESNIRYLAF ETTAYLISCG HSITSLKHYK
     ELILSSLRYK DVSLRKKSLE LLYMMCDEEN AKLIVADLLQ YLPHLDSVTQ EDLISKVAII
     SETFATDYEW YVDVTIQLLR IAGKSADDGV WHQLVHVIVN NEEIQEYATK RLFSLLQSET
     IHECLVKAGG YVLGEFGHLI TDYPDSQPVH QFSTIYRKLN VSSPSTRVLL LTTLIKLANL
     QPELNDRIAK VFQEYSTIIN PEVQQRACEY LQLLKMPRDF LQLVCDEVPP FLDGNRDGVH
     PKSRPSSKVN LVDTYPQTIP NVSKPSTPID VPEYDISACL PGFYRLCWKD KGILYQDSQI
     QIGVRSEYHN SEGAIYLYYE NRQSNTLKSL SSTLIRTFST FHLATTFQDT NLPSGVQLQQ
     KYVMSGVNEI FEPPIIHVSY VTGVIRSIDL QLPVLLSKFM KPTIFDSYDF FNHWGQMGVE
     REAQLTFGLN SKDRKLDAKR LTKIVSGFHW GICQNVDSIA LNIVGAGIIR FGTQNVGCLL
     RIEPNYEQNL IRLSIRSTNT SIANTLAKEM QEILRNSF