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 24-JUL-2024, entry version 181. 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; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION, AND RP 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 LOCATION, AND RP 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 patterns RT 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., Brandon R.C., RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., RA Glasser K., 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., Hostin D., RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., RA Shen H., 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., Svirskas R., RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., RA 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., Stapleton M., RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic RT 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., 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., Champe M., RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A., RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., 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 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. AP- CC 2alpha is a subunit of the plasma membrane adapter. CC {ECO:0000269|PubMed:9118220, ECO:0000269|PubMed:9285813}. 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:0000269|PubMed:9118220, CC ECO:0000269|PubMed:9285813}; Peripheral membrane protein {ECO:0000305}; CC Cytoplasmic side {ECO:0000305}. Membrane, coated pit CC {ECO:0000269|PubMed:9118220}; Peripheral membrane protein CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Component of the CC coat surrounding the cytoplasmic face of coated vesicles in the plasma CC membrane. {ECO:0000269|PubMed:9118220}. 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 -!- TISSUE SPECIFICITY: Expressed in the Garland cells, imaginal disks, CC adult midgut precursors, the antenno-maxillary complex, the endoderm, CC the fat bodies, and the visceral mesoderm and cells of the CNS and PNS CC including neuroblasts, the presumptive stomatogastric nervous system, CC and the lateral chordotonal sense organs. {ECO:0000269|PubMed:9118220, CC ECO:0000269|PubMed:9285813}. CC -!- RNA EDITING: Modified_positions=207 {ECO:0000269|PubMed:17018572, CC ECO:0000269|Ref.6}; Note=Partially edited. Target of Adar.; CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAO39461.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; 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 AlphaFoldDB; P91926; -. DR SMR; P91926; -. DR BioGRID; 59467; 25. DR ComplexPortal; CPX-2725; Adaptor complex AP-2. DR IntAct; P91926; 2. DR STRING; 7227.FBpp0088945; -. DR iPTMnet; P91926; -. DR PaxDb; 7227-FBpp0088945; -. DR DNASU; 33211; -. DR EnsemblMetazoa; FBtr0089488; FBpp0088490; FBgn0264855. [P91926-1] DR EnsemblMetazoa; FBtr0089489; FBpp0088945; FBgn0264855. [P91926-2] DR GeneID; 33211; -. DR KEGG; dme:Dmel_CG4260; -. DR AGR; FB:FBgn0264855; -. DR CTD; 33211; -. DR FlyBase; FBgn0264855; AP-2alpha. DR VEuPathDB; VectorBase:FBgn0264855; -. DR eggNOG; KOG1077; Eukaryota. DR GeneTree; ENSGT00950000182838; -. DR HOGENOM; CLU_003824_1_0_1; -. DR InParanoid; P91926; -. DR OMA; PVLMHRY; -. DR OrthoDB; 25313at2759; -. DR PhylomeDB; P91926; -. DR Reactome; R-DME-177504; Retrograde neurotrophin signalling. DR Reactome; R-DME-3928665; EPH-ephrin mediated repulsion of cells. DR Reactome; R-DME-416993; Trafficking of GluR2-containing AMPA receptors. DR Reactome; R-DME-437239; Recycling pathway of L1. DR Reactome; R-DME-5099900; WNT5A-dependent internalization of FZD4. DR Reactome; R-DME-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2. DR Reactome; R-DME-6798695; Neutrophil degranulation. DR Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis. DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis. DR Reactome; R-DME-8866427; VLDLR internalisation and degradation. DR Reactome; R-DME-8964038; LDL clearance. DR SignaLink; P91926; -. DR BioGRID-ORCS; 33211; 0 hits in 3 CRISPR screens. DR GenomeRNAi; 33211; -. DR PRO; PR:P91926; -. DR Proteomes; UP000000803; Chromosome 2L. DR Bgee; FBgn0264855; Expressed in embryonic/larval hemocyte (Drosophila) and 40 other cell types or tissues. DR ExpressionAtlas; P91926; baseline and differential. DR GO; GO:0030122; C:AP-2 adaptor complex; IMP:FlyBase. DR GO; GO:0005905; C:clathrin-coated pit; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase. DR GO; GO:0098793; C:presynapse; IEA:GOC. DR GO; GO:0035615; F:clathrin adaptor activity; IMP:FlyBase. DR GO; GO:0008356; P:asymmetric cell division; TAS:FlyBase. DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central. DR GO; GO:0006897; P:endocytosis; IMP:FlyBase. DR GO; GO:0030707; P:follicle cell of egg chamber development; IMP:FlyBase. DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro. DR GO; GO:1990386; P:mitotic cleavage furrow ingression; IMP:UniProtKB. DR GO; GO:0010508; P:positive regulation of autophagy; IMP:FlyBase. DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:FlyBase. DR GO; GO:0038010; P:positive regulation of signal transduction by receptor internalization; IMP:FlyBase. DR GO; GO:0008104; P:protein localization; IMP:FlyBase. DR GO; GO:0015031; P:protein transport; IDA:UniProtKB. DR GO; GO:0031623; P:receptor internalization; IGI:FlyBase. DR GO; GO:0030100; P:regulation of endocytosis; IDA:FlyBase. DR GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:UniProtKB. DR GO; GO:0048489; P:synaptic vesicle transport; TAS:FlyBase. DR Gene3D; 2.60.40.1230; -; 1. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR Gene3D; 3.30.310.10; TATA-Binding Protein; 1. DR InterPro; IPR050840; Adaptor_Complx_Large_Subunit. 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 PANTHER; PTHR22780; ADAPTIN, ALPHA/GAMMA/EPSILON; 1. DR PANTHER; PTHR22780:SF4; AP-2 COMPLEX SUBUNIT ALPHA; 1. 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; ARM repeat; 1. DR SUPFAM; SSF49348; Clathrin adaptor appendage domain; 1. DR SUPFAM; SSF55711; Subdomain of clathrin and coatomer appendage domain; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Coated pit; Endocytosis; Membrane; KW Phosphoprotein; Protein transport; Reference proteome; RNA editing; KW Transport. FT CHAIN 1..940 FT /note="AP-2 complex subunit alpha" FT /id="PRO_0000193735" FT REGION 651..679 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 632 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 634 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT VAR_SEQ 2..21 FT /note="APVRGDGMRGLAVFISDIRN -> ERAEGCEVVSPIDQSRGGKESEASADES FT LLFY (in isoform B)" FT /evidence="ECO:0000305" FT /id="VSP_023135" FT VARIANT 207 FT /note="T -> A (in RNA edited version)" FT CONFLICT 325 FT /note="N -> E (in Ref. 2; CAA73533)" FT /evidence="ECO:0000305" FT CONFLICT 489 FT /note="A -> P (in Ref. 2; CAA73533)" FT /evidence="ECO:0000305" FT CONFLICT 587 FT /note="S -> N (in Ref. 2; CAA73533)" FT /evidence="ECO:0000305" FT CONFLICT 709..712 FT /note="KFLF -> FVS (in Ref. 2; CAA73533)" FT /evidence="ECO:0000305" FT CONFLICT 722..723 FT /note="EM -> GK (in Ref. 2; CAA73533)" FT /evidence="ECO:0000305" FT CONFLICT 741..743 FT /note="LFY -> FSN (in Ref. 2; CAA73533)" FT /evidence="ECO:0000305" FT CONFLICT 877 FT /note="Q -> P (in Ref. 2; CAA73533)" FT /evidence="ECO:0000305" 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 //