ID AP2A_DROME Reviewed; 940 AA. AC P91926; O01937; Q7KTZ5; Q86P64; Q9VPP4; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 20-MAR-2007, entry version 50. DE AP-2 complex subunit alpha (Alpha-adaptin). GN Name=alpha-Adaptin; ORFNames=CG4260; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. 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 MEDLINE=97236497; 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 MEDLINE=97431776; PubMed=9285813; 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 MEDLINE=20196006; 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., 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., 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., Zhu X., Smith H.O., RA 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. RX MEDLINE=22426069; PubMed=12537572; 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] 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 [6] 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). 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. Alpha adaptin is a subunit of the plasma membrane CC adapter. CC -!- SUBUNIT: Assembly protein complex 2 (AP-2) is a heterotetramer CC composed of two large chains (alpha and beta), a medium chain CC (mu/AP50) and a small chain (sigma/AP17). CC -!- SUBCELLULAR LOCATION: Cell membrane; coated pit; cytoplasmic side. CC Note=Component of the coat surrounding the cytoplasmic face of CC coated vesicles in 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 --------------------------------------------------------------------------- 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; BT003458; AAO39461.1; ALT_INIT; mRNA. DR UniGene; Dm.246; -. DR HSSP; P17427; 1GW5. DR Ensembl; CG4260; Drosophila melanogaster. DR KEGG; dme:Dmel_CG4260; -. DR FlyBase; FBgn0015567; alpha-Adaptin. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-006702-MONOMER; -. DR GermOnline; CG4260; Drosophila melanogaster. DR GO; GO:0005905; C:coated pit; IDA:UniProtKB. 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:0007269; P:neurotransmitter secretion; NAS:FlyBase. DR GO; GO:0015031; P:protein transport; IDA:UniProtKB. DR GO; GO:0016183; P:synaptic vesicle coating; TAS:FlyBase. DR InterPro; IPR008152; A/G_adapt_C. DR InterPro; IPR002553; Adaptin_N. DR InterPro; IPR003164; AP2_A_adaptin_C. DR InterPro; IPR009028; AP2_adap_app. DR InterPro; IPR011989; ARM-like. DR Gene3D; G3DSA:3.30.310.30; AP2_A_adaptin_C; 1. DR Gene3D; G3DSA:1.25.10.10; ARM-like; 1. DR Pfam; PF01602; Adaptin_N; 1. DR Pfam; PF02296; Alpha_adaptin_C; 1. DR Pfam; PF02883; Alpha_adaptinC2; 1. KW Alternative splicing; Coated pits; Complete proteome; Endocytosis; KW Protein transport; RNA editing; Transport. FT CHAIN 1 940 AP-2 complex subunit alpha. FT /FTId=PRO_0000193735. FT COMPBIAS 644 715 Asn-rich. 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 //