ID AP2A_DROME Reviewed; 940 AA. AC P91926; B3DN51; O01937; Q7KTZ5; Q86P64; Q9VPP4; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 03-SEP-2014, entry version 111. DE RecName: Full=AP-2 complex subunit alpha; DE AltName: Full=Alpha-adaptin; GN Name=AP-2alpha; ORFNames=CG4260; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RC STRAIN=Canton-S; TISSUE=Embryo; RX PubMed=9118220; DOI=10.1016/S0092-8674(00)81923-6; RA Gonzalez-Gaitan M.A., Jaeckle H.; RT "Role of Drosophila alpha-adaptin in presynaptic vesicle recycling."; RL Cell 88:767-776(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Embryo; RX PubMed=9285813; DOI=10.1091/mbc.8.8.1391; RA Dornan S.C., Jackson A.P., Gay N.J.; RT "Alpha-adaptin, a marker for endocytosis, is expressed in complex RT patterns during Drosophila development."; RL Mol. Biol. Cell 8:1391-1403(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING. RC STRAIN=Berkeley; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). RC STRAIN=Berkeley; TISSUE=Embryo; RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., RA Celniker S.E.; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 93-940, AND RNA EDITING OF RP POSITION 207. RC STRAIN=Berkeley; TISSUE=Head; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [7] RP RNA EDITING OF POSITION 207. RX PubMed=17018572; DOI=10.1261/rna.254306; RA Stapleton M., Carlson J.W., Celniker S.E.; RT "RNA editing in Drosophila melanogaster: new targets and functional RT consequences."; RL RNA 12:1922-1932(2006). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632 AND SER-634, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Embryo; RX PubMed=18327897; DOI=10.1021/pr700696a; RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.; RT "Phosphoproteome analysis of Drosophila melanogaster embryos."; RL J. Proteome Res. 7:1675-1682(2008). CC -!- FUNCTION: Adaptins are components of the adapter complexes which CC link clathrin to receptors in coated vesicles. Clathrin-associated CC protein complexes are believed to interact with the cytoplasmic CC tails of membrane proteins, leading to their selection and CC concentration. AP-2alpha is a subunit of the plasma membrane CC adapter. CC -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer CC composed of two large adaptins (alpha-type and beta-type CC subunits), a medium adaptin (mu-type subunit AP50) and a small CC adaptin (sigma-type subunit AP17) (By similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane. Membrane, coated pit; CC Peripheral membrane protein; Cytoplasmic side. Note=Component of CC the coat surrounding the cytoplasmic face of coated vesicles in CC the plasma membrane. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; CC IsoId=P91926-1; Sequence=Displayed; CC Name=B; CC IsoId=P91926-2; Sequence=VSP_023135; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Expressed in the Garland cells, imaginal CC disks, adult midgut precursors, the antenno-maxillary complex, the CC endoderm, the fat bodies, and the visceral mesoderm and cells of CC the CNS and PNS including neuroblasts, the presumptive CC stomatogastric nervous system, and the lateral chordotonal sense CC organs. CC -!- RNA EDITING: Modified_positions=207; Note=Partially edited. Target CC of Adar. CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family. CC -!- SEQUENCE CAUTION: CC Sequence=AAO39461.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y11104; CAA71991.1; -; mRNA. DR EMBL; Y13092; CAA73533.1; -; mRNA. DR EMBL; AE014134; AAF56103.2; -; Genomic_DNA. DR EMBL; AE014134; AAS64634.1; -; Genomic_DNA. DR EMBL; BT032839; ACD81853.1; -; mRNA. DR EMBL; BT003458; AAO39461.1; ALT_INIT; mRNA. DR RefSeq; NP_476819.2; NM_057471.6. [P91926-1] DR RefSeq; NP_995607.1; NM_205885.2. [P91926-2] DR UniGene; Dm.246; -. DR ProteinModelPortal; P91926; -. DR SMR; P91926; 5-614, 706-940. DR BioGrid; 59467; 11. DR IntAct; P91926; 2. DR MINT; MINT-7714518; -. DR PaxDb; P91926; -. DR PRIDE; P91926; -. DR EnsemblMetazoa; FBtr0089488; FBpp0088490; FBgn0263350. [P91926-1] DR GeneID; 33211; -. DR KEGG; dme:Dmel_CG4260; -. DR CTD; 33211; -. DR FlyBase; FBgn0264855; AP-2alpha. DR eggNOG; NOG303101; -. DR GeneTree; ENSGT00550000074757; -. DR InParanoid; P91926; -. DR KO; K11824; -. DR OMA; QDVFRQH; -. DR PhylomeDB; P91926; -. DR Reactome; REACT_211983; WNT5A-dependent internalization of FZD4. DR SignaLink; P91926; -. DR GenomeRNAi; 33211; -. DR NextBio; 782454; -. DR Bgee; P91926; -. DR GO; GO:0030122; C:AP-2 adaptor complex; IMP:FlyBase. DR GO; GO:0005905; C:coated pit; IDA:UniProtKB. DR GO; GO:0030135; C:coated vesicle; TAS:FlyBase. DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase. DR GO; GO:0008021; C:synaptic vesicle; TAS:FlyBase. DR GO; GO:0008565; F:protein transporter activity; IDA:UniProtKB. DR GO; GO:0008356; P:asymmetric cell division; TAS:FlyBase. DR GO; GO:0006897; P:endocytosis; IMP:FlyBase. DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro. DR GO; GO:0022008; P:neurogenesis; IMP:FlyBase. DR GO; GO:0007269; P:neurotransmitter secretion; NAS:FlyBase. DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:FlyBase. DR GO; GO:0008104; P:protein localization; IMP:FlyBase. DR GO; GO:0015031; P:protein transport; IDA:UniProtKB. DR GO; GO:0030100; P:regulation of endocytosis; IDA:FlyBase. DR GO; GO:0016183; P:synaptic vesicle coating; TAS:FlyBase. DR GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:UniProtKB. DR GO; GO:0048489; P:synaptic vesicle transport; TAS:FlyBase. DR GO; GO:0006901; P:vesicle coating; TAS:FlyBase. DR Gene3D; 1.25.10.10; -; 1. DR Gene3D; 2.60.40.1030; -; 1. DR Gene3D; 3.30.310.30; -; 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; IPR013038; Clathrin_a-adaptin_app_Ig-like. DR InterPro; IPR003164; Clathrin_a-adaptin_app_sub_C. DR InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig. DR InterPro; IPR015873; Clathrin_a/coatomer_app_sub_C. 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; Protein transport; KW Reference proteome; RNA editing; Transport. FT CHAIN 1 940 AP-2 complex subunit alpha. FT /FTId=PRO_0000193735. FT COMPBIAS 644 715 Asn-rich. FT MOD_RES 632 632 Phosphoserine. FT MOD_RES 634 634 Phosphoserine. FT VAR_SEQ 2 21 APVRGDGMRGLAVFISDIRN -> ERAEGCEVVSPIDQSRG FT GKESEASADESLLFY (in isoform B). FT /FTId=VSP_023135. FT VARIANT 207 207 T -> A (in RNA edited version). FT CONFLICT 325 325 N -> E (in Ref. 2; CAA73533). FT CONFLICT 489 489 A -> P (in Ref. 2; CAA73533). FT CONFLICT 587 587 S -> N (in Ref. 2; CAA73533). FT CONFLICT 709 712 KFLF -> FVS (in Ref. 2; CAA73533). FT CONFLICT 722 723 EM -> GK (in Ref. 2; CAA73533). FT CONFLICT 741 743 LFY -> FSN (in Ref. 2; CAA73533). FT CONFLICT 877 877 Q -> P (in Ref. 2; CAA73533). SQ SEQUENCE 940 AA; 105620 MW; F745045CD2C1D9C5 CRC64; MAPVRGDGMR GLAVFISDIR NCKSKEAEVK RINKELANIR SKFKGDKTLD GYQKKKYVCK LLFIFLLGHD IDFGHMEAVN LLSSNKYSEK QIGYLFISVL VNTNSDLIRL IIQSIKNDLQ SRNPVHVNLA LQCIANIGSR DMAESFSNEI PKLLVSGDTM DVVKQSAALC LLRLFRSSPD IIPGGEWTSR IIHLLNDQHM GVVTAATSLI DALVKRNPDE 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 ESKSPAPLTS AAQNNALVNN SHSKLNNSNA NTDLLGLSTP PSNNIGSGSN SNSTLIDVLG DMYGSNSNNN SSAVYNTKKF LFKNNGVLFE NEMLQIGVKS EFRQNLGRLG LFYGNKTQVP LTNFNPVLQW SAEDALKLNV QMKVVEPTLE AGAQIQQLLT AECIEDYADA PTIEISFRYN GTQQKFSIKL PLSVNKFFEP TEMNAESFFA RWKNLSGEQQ RSQKVFKAAQ PLDLPGARNK LMGFGMQLLD QVDPNPDNMV CAGIIHTQSQ QVGCLMRLEP NKQAQMFRLT VRASKETVTR EICDLLTDQF //