Entry euk:AP2A1_HUMAN

ID   AP2A1_HUMAN             Reviewed;         977 AA.
AC   O95782; Q96CI7; Q96PP6; Q96PP7; Q9H070;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 3.
DT   10-MAY-2017, entry version 162.
DE   RecName: Full=AP-2 complex subunit alpha-1;
DE   AltName: Full=100 kDa coated vesicle protein A;
DE   AltName: Full=Adaptor protein complex AP-2 subunit alpha-1;
DE   AltName: Full=Adaptor-related protein complex 2 subunit alpha-1;
DE   AltName: Full=Alpha-adaptin A;
DE   AltName: Full=Alpha1-adaptin;
DE   AltName: Full=Clathrin assembly protein complex 2 alpha-A large chain;
DE   AltName: Full=Plasma membrane adaptor HA2/AP2 adaptin alpha A subunit;
GN   Name=AP2A1; Synonyms=ADTAA, CLAPA1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A AND B).
RX   PubMed=12036598; DOI=10.1016/S0378-1119(02)00504-8;
RA   Scorilas A., Levesque M.A., Ashworth L.K., Diamandis E.P.;
RT   "Cloning, physical mapping and structural characterization of the
RT   human alpha(A)-adaptin gene.";
RL   Gene 289:191-199(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC   TISSUE=Uterus;
RX   PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA   Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA   Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA   Wambutt R., Korn B., Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and
RT   analysis of 500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA   Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA   Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA   Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA   Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA   Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA   Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA   Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA   Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA   Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA   Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA   Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA   Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA   Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA   Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B), AND VARIANT
RP   LEU-270.
RC   TISSUE=Muscle;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INTERACTION WITH HIP1.
RX   PubMed=11532990; DOI=10.1093/hmg/10.17.1807;
RA   Waelter S., Scherzinger E., Hasenbank R., Nordhoff E., Lurz R.,
RA   Goehler H., Gauss C., Sathasivam K., Bates G.P., Lehrach H.,
RA   Wanker E.E.;
RT   "The huntingtin interacting protein HIP1 is a clathrin and alpha-
RT   adaptin-binding protein involved in receptor-mediated endocytosis.";
RL   Hum. Mol. Genet. 10:1807-1817(2001).
RN   [6]
RP   INTERACTION WITH RAB11FIP2.
RX   PubMed=12364336; DOI=10.1074/jbc.M206316200;
RA   Cullis D.N., Philip B., Baleja J.D., Feig L.A.;
RT   "Rab11-FIP2, an adaptor protein connecting cellular components
RT   involved in internalization and recycling of epidermal growth factor
RT   receptors.";
RL   J. Biol. Chem. 277:49158-49166(2002).
RN   [7]
RP   FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX   PubMed=14745134; DOI=10.1247/csf.28.419;
RA   Nakatsu F., Ohno H.;
RT   "Adaptor protein complexes as the key regulators of protein sorting in
RT   the post-Golgi network.";
RL   Cell Struct. Funct. 28:419-429(2003).
RN   [8]
RP   FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX   PubMed=15473838; DOI=10.1146/annurev.cellbio.20.010403.104543;
RA   Owen D.J., Collins B.M., Evans P.R.;
RT   "Adaptors for clathrin coats: structure and function.";
RL   Annu. Rev. Cell Dev. Biol. 20:153-191(2004).
RN   [9]
RP   FUNCTION OF THE AP-2 COMPLEX IN NON-CLATHRIN-DEPENDENT ENDOCYTOSIS.
RX   PubMed=19033387; DOI=10.1242/jcs.033522;
RA   Lau A.W., Chou M.M.;
RT   "The adaptor complex AP-2 regulates post-endocytic trafficking through
RT   the non-clathrin Arf6-dependent endocytic pathway.";
RL   J. Cell Sci. 121:4008-4017(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-652; THR-653 AND
RP   SER-655, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-653, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [17]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA   Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
CC   -!- FUNCTION: Component of the adaptor protein complex 2 (AP-2).
CC       Adaptor protein complexes function in protein transport via
CC       transport vesicles in different membrane traffic pathways. Adaptor
CC       protein complexes are vesicle coat components and appear to be
CC       involved in cargo selection and vesicle formation. AP-2 is
CC       involved in clathrin-dependent endocytosis in which cargo proteins
CC       are incorporated into vesicles surrounded by clathrin (clathrin-
CC       coated vesicles, CCVs) which are destined for fusion with the
CC       early endosome. The clathrin lattice serves as a mechanical
CC       scaffold but is itself unable to bind directly to membrane
CC       components. Clathrin-associated adaptor protein (AP) complexes
CC       which can bind directly to both the clathrin lattice and to the
CC       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
CC       proteins involved in receptor-mediated endocytosis. AP-2 seems to
CC       play a role in the recycling of synaptic vesicle membranes from
CC       the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi)
CC       and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the
CC       cytosolic tails of transmembrane cargo molecules. AP-2 may also
CC       play a role in maintaining normal post-endocytic trafficking
CC       through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha
CC       subunit binds polyphosphoinositide-containing lipids, positioning
CC       AP-2 on the membrane. The AP-2 alpha subunit acts via its C-
CC       terminal appendage domain as a scaffolding platform for endocytic
CC       accessory proteins. The AP-2 alpha and AP-2 sigma subunits are
CC       thought to contribute to the recognition of the [ED]-X-X-X-L-[LI]
CC       motif (By similarity). {ECO:0000250, ECO:0000269|PubMed:14745134,
CC       ECO:0000269|PubMed:15473838, ECO:0000269|PubMed:19033387}.
CC   -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer
CC       composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2
CC       and beta-type subunit AP2B1), a medium adaptin (mu-type subunit
CC       AP2M1) and a small adaptin (sigma-type subunit AP2S1). Interacts
CC       with SGIP1 (By similarity). Interacts with HIP1 and RAB11FIP2.
CC       Interacts with SLC12A5. Interacts with clathrin. {ECO:0000250,
CC       ECO:0000269|PubMed:11532990, ECO:0000269|PubMed:12364336}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Membrane,
CC       coated pit {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=AP-2 appears
CC       to be excluded from internalizing CCVs and to disengage from sites
CC       of endocytosis seconds before internalization of the nascent CCV.
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A;
CC         IsoId=O95782-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=O95782-2; Sequence=VSP_000161;
CC   -!- TISSUE SPECIFICITY: Isoform A expressed in forebrain, skeletal
CC       muscle, spinal cord, cerebellum, salivary gland, heart and colon.
CC       Isoform B is widely expressed in tissues and also in breast cancer
CC       and in prostate carcinoma cells.
CC   -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD15564.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF289221; AAL11039.1; -; Genomic_DNA.
DR   EMBL; AF289221; AAL11040.1; -; Genomic_DNA.
DR   EMBL; AL136925; CAB66859.1; -; mRNA.
DR   EMBL; AC006942; AAD15564.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC011495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC098783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC014214; AAH14214.1; -; mRNA.
DR   CCDS; CCDS46148.1; -. [O95782-1]
DR   CCDS; CCDS46149.1; -. [O95782-2]
DR   RefSeq; NP_055018.2; NM_014203.2. [O95782-1]
DR   RefSeq; NP_570603.2; NM_130787.2. [O95782-2]
DR   UniGene; Hs.467125; -.
DR   ProteinModelPortal; O95782; -.
DR   SMR; O95782; -.
DR   BioGrid; 106669; 121.
DR   DIP; DIP-33164N; -.
DR   IntAct; O95782; 67.
DR   MINT; MINT-5002322; -.
DR   STRING; 9606.ENSP00000351926; -.
DR   iPTMnet; O95782; -.
DR   PhosphoSitePlus; O95782; -.
DR   SwissPalm; O95782; -.
DR   BioMuta; AP2A1; -.
DR   EPD; O95782; -.
DR   MaxQB; O95782; -.
DR   PaxDb; O95782; -.
DR   PeptideAtlas; O95782; -.
DR   PRIDE; O95782; -.
DR   DNASU; 160; -.
DR   Ensembl; ENST00000354293; ENSP00000346246; ENSG00000196961. [O95782-2]
DR   Ensembl; ENST00000359032; ENSP00000351926; ENSG00000196961. [O95782-1]
DR   GeneID; 160; -.
DR   KEGG; hsa:160; -.
DR   UCSC; uc002ppn.4; human. [O95782-1]
DR   CTD; 160; -.
DR   DisGeNET; 160; -.
DR   GeneCards; AP2A1; -.
DR   HGNC; HGNC:561; AP2A1.
DR   HPA; CAB004306; -.
DR   MIM; 601026; gene.
DR   neXtProt; NX_O95782; -.
DR   OpenTargets; ENSG00000196961; -.
DR   PharmGKB; PA24852; -.
DR   eggNOG; KOG1077; Eukaryota.
DR   eggNOG; ENOG410XNQE; LUCA.
DR   GeneTree; ENSGT00550000074757; -.
DR   HOGENOM; HOG000170596; -.
DR   HOVERGEN; HBG050518; -.
DR   InParanoid; O95782; -.
DR   KO; K11824; -.
DR   OMA; INIKFRY; -.
DR   OrthoDB; EOG091G01JZ; -.
DR   PhylomeDB; O95782; -.
DR   TreeFam; TF300308; -.
DR   Reactome; R-HSA-167590; Nef Mediated CD4 Down-regulation.
DR   Reactome; R-HSA-171052; LDL-mediated lipid transport.
DR   Reactome; R-HSA-177504; Retrograde neurotrophin signalling.
DR   Reactome; R-HSA-182218; Nef Mediated CD8 Down-regulation.
DR   Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR   Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
DR   Reactome; R-HSA-416993; Trafficking of GluR2-containing AMPA receptors.
DR   Reactome; R-HSA-437239; Recycling pathway of L1.
DR   Reactome; R-HSA-5099900; WNT5A-dependent internalization of FZD4.
DR   Reactome; R-HSA-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR   Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR   Reactome; R-HSA-8866427; VLDLR internalisation and degradation.
DR   SignaLink; O95782; -.
DR   ChiTaRS; AP2A1; human.
DR   GeneWiki; Adaptor-related_protein_complex_2,_alpha_1; -.
DR   GenomeRNAi; 160; -.
DR   PRO; PR:O95782; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   Bgee; ENSG00000196961; -.
DR   CleanEx; HS_AP2A1; -.
DR   ExpressionAtlas; O95782; baseline and differential.
DR   Genevisible; O95782; HS.
DR   GO; GO:0030122; C:AP-2 adaptor complex; TAS:BHF-UCL.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR   GO; GO:0030130; C:clathrin coat of trans-Golgi network vesicle; NAS:UniProtKB.
DR   GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR   GO; GO:0036020; C:endolysosome membrane; TAS:Reactome.
DR   GO; GO:0032433; C:filopodium tip; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR   GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
DR   GO; GO:0019901; F:protein kinase binding; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR   GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR   GO; GO:0072583; P:clathrin-dependent endocytosis; TAS:BHF-UCL.
DR   GO; GO:0006897; P:endocytosis; NAS:UniProtKB.
DR   GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0006895; P:Golgi to endosome transport; NAS:UniProtKB.
DR   GO; GO:0006886; P:intracellular protein transport; NAS:UniProtKB.
DR   GO; GO:0061024; P:membrane organization; TAS:Reactome.
DR   GO; GO:0007018; P:microtubule-based movement; TAS:Reactome.
DR   GO; GO:1900126; P:negative regulation of hyaluronan biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
DR   GO; GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
DR   GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
DR   Gene3D; 1.25.10.10; -; 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; IPR009028; Coatomer/calthrin_app_sub_C.
DR   InterPro; IPR013041; Coatomer/clathrin_app_Ig-like.
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   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Coated pit; Complete proteome;
KW   Endocytosis; Membrane; Phosphoprotein; Polymorphism;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN         1    977       AP-2 complex subunit alpha-1.
FT                                /FTId=PRO_0000193730.
FT   MOD_RES     626    626       Phosphoserine.
FT                                {ECO:0000244|PubMed:18691976}.
FT   MOD_RES     652    652       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     653    653       Phosphothreonine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:20068231}.
FT   MOD_RES     655    655       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   VAR_SEQ     706    727       Missing (in isoform B).
FT                                {ECO:0000303|PubMed:11230166,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_000161.
FT   VARIANT     270    270       P -> L (in dbSNP:rs17851121).
FT                                {ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_060544.
FT   CONFLICT    804    804       Q -> H (in Ref. 1; AAL11039/AAL11040).
FT                                {ECO:0000305}.
FT   CONFLICT    924    977       ENFVGAGIIQTKALQVGCLLRLEPNAQAQMYRLTLRTSKEP
FT                                VSRHLCELLAQQF -> GDREDTRVWGMPGTFLRPFVFLFL
FT                                FICCCLHSGGLGGVPLPPFPPQAQRGEGPGKWMSPPLPPHP
FT                                VVAPPTPSPSRGCVLL (in Ref. 4; AAH14214).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       751    852       ipfam:Alpha_adaptinC2 [T]
FT   MYHIT        31    588       ipfam:Adaptin_N [T]
FT   MYHIT       745    858       ismart:Alpha_adaptinC2 [T]
FT   MYHIT       864    972       ipfam:Alpha_adaptin_C [T]
SQ   SEQUENCE   977 AA;  107546 MW;  D9FB569E7EDDF6ED CRC64;
     MPAVSKGDGM RGLAVFISDI RNCKSKEAEI KRINKELANI RSKFKGDKAL DGYSKKKYVC
     KLLFIFLLGH DIDFGHMEAV NLLSSNKYTE KQIGYLFISV LVNSNSELIR LINNAIKNDL
     ASRNPTFMCL ALHCIANVGS REMGEAFAAD IPRILVAGDS MDSVKQSAAL CLLRLYKASP
     DLVPMGEWTA RVVHLLNDQH MGVVTAAVSL ITCLCKKNPD DFKTCVSLAV 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 GPGAGSALDD GRRDPSSNDI NGGMEPTPST VSTPSPSADL
     LGLRAAPPPA APPASAGAGN LLVDVFDGPA AQPSLGPTPE EAFLSELEPP APESPMALLA
     DPAPAADPGP EDIGPPIPEA DELLNKFVCK NNGVLFENQL LQIGVKSEFR QNLGRMYLFY
     GNKTSVQFQN FSPTVVHPGD LQTQLAVQTK RVAAQVDGGA QVQQVLNIEC LRDFLTPPLL
     SVRFRYGGAP QALTLKLPVT INKFFQPTEM AAQDFFQRWK QLSLPQQEAQ KIFKANHPMD
     AEVTKAKLLG FGSALLDNVD PNPENFVGAG IIQTKALQVG CLLRLEPNAQ AQMYRLTLRT
     SKEPVSRHLC ELLAQQF
//