AP2A_DROME
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-AUG-2022, entry version 173.
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 IntAct; P91926; 2.
DR MINT; P91926; -.
DR STRING; 7227.FBpp0088945; -.
DR iPTMnet; P91926; -.
DR PaxDb; P91926; -.
DR PRIDE; P91926; -.
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 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; SPIEQFM; -.
DR PhylomeDB; P91926; -.
DR Reactome; R-DME-177504; Retrograde neurotrophin signalling.
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 tissues.
DR ExpressionAtlas; P91926; baseline and differential.
DR Genevisible; P91926; DM.
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:0140312; F:cargo adaptor activity; IBA:GO_Central.
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:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:1990386; P:mitotic cleavage furrow ingression; IMP:UniProtKB.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
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:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
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; 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 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
