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Protein

AP-2 complex subunit alpha

Gene

AP-2alpha

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Adaptins are components of the adapter complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. AP-2alpha is a subunit of the plasma membrane adapter.2 Publications

GO - Molecular functioni

  • protein transporter activity Source: UniProtKB

GO - Biological processi

  • asymmetric cell division Source: FlyBase
  • endocytosis Source: FlyBase
  • intracellular protein transport Source: InterPro
  • neurogenesis Source: FlyBase
  • neurotransmitter secretion Source: FlyBase
  • ovarian follicle cell development Source: FlyBase
  • positive regulation of endocytosis Source: FlyBase
  • protein localization Source: FlyBase
  • protein transport Source: UniProtKB
  • regulation of endocytosis Source: FlyBase
  • sensory perception of pain Source: FlyBase
  • synaptic vesicle coating Source: FlyBase
  • synaptic vesicle endocytosis Source: UniProtKB
  • synaptic vesicle transport Source: FlyBase
  • vesicle coating Source: FlyBase
  • vesicle-mediated transport Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

Endocytosis, Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-DME-416993. Trafficking of GluR2-containing AMPA receptors.
R-DME-437239. Recycling pathway of L1.
R-DME-5099900. WNT5A-dependent internalization of FZD4.
SignaLinkiP91926.

Names & Taxonomyi

Protein namesi
Recommended name:
AP-2 complex subunit alpha
Alternative name(s):
Alpha-adaptin
Gene namesi
Name:AP-2alpha
ORF Names:CG4260
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0264855. AP-2alpha.

Subcellular locationi

GO - Cellular componenti

  • AP-2 adaptor complex Source: FlyBase
  • coated pit Source: UniProtKB
  • coated vesicle Source: FlyBase
  • cytosol Source: GOC
  • plasma membrane Source: FlyBase
  • synaptic vesicle Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 940940AP-2 complex subunit alphaPRO_0000193735Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei632 – 6321Phosphoserine1 Publication
Modified residuei634 – 6341Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP91926.
PRIDEiP91926.

PTM databases

iPTMnetiP91926.

Expressioni

Tissue specificityi

Expressed in the Garland cells, imaginal disks, adult midgut precursors, the antenno-maxillary complex, the endoderm, the fat bodies, and the visceral mesoderm and cells of the CNS and PNS including neuroblasts, the presumptive stomatogastric nervous system, and the lateral chordotonal sense organs.2 Publications

Gene expression databases

BgeeiP91926.
ExpressionAtlasiP91926. differential.
GenevisibleiP91926. DM.

Interactioni

Subunit structurei

Adaptor protein complex 2 (AP-2) is a heterotetramer composed of two large adaptins (alpha-type and beta-type subunits), a medium adaptin (mu-type subunit AP50) and a small adaptin (sigma-type subunit AP17).By similarity

Protein-protein interaction databases

BioGridi59467. 12 interactions.
IntActiP91926. 2 interactions.
MINTiMINT-7714518.
STRINGi7227.FBpp0088945.

Structurei

3D structure databases

ProteinModelPortaliP91926.
SMRiP91926. Positions 5-614, 706-940.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi644 – 71572Asn-richAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1077. Eukaryota.
ENOG410XNQE. LUCA.
GeneTreeiENSGT00550000074757.
InParanoidiP91926.
KOiK11824.
OMAiFMEAPIL.
PhylomeDBiP91926.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
2.60.40.1030. 1 hit.
3.30.310.30. 1 hit.
InterProiIPR017104. AP2_complex_asu.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR002553. Clathrin/coatomer_adapt-like_N.
IPR013038. Clathrin_a-adaptin_app_Ig-like.
IPR003164. Clathrin_a-adaptin_app_sub_C.
IPR008152. Clathrin_a/b/g-adaptin_app_Ig.
IPR015873. Clathrin_a/coatomer_app_sub_C.
IPR009028. Coatomer/calthrin_app_sub_C.
IPR013041. Coatomer/clathrin_app_Ig-like.
[Graphical view]
PfamiPF01602. Adaptin_N. 1 hit.
PF02296. Alpha_adaptin_C. 1 hit.
PF02883. Alpha_adaptinC2. 1 hit.
[Graphical view]
PIRSFiPIRSF037091. AP2_complex_alpha. 1 hit.
SMARTiSM00809. Alpha_adaptinC2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF49348. SSF49348. 1 hit.
SSF55711. SSF55711. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: P91926-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAPVRGDGMR GLAVFISDIR NCKSKEAEVK RINKELANIR SKFKGDKTLD
60 70 80 90 100
GYQKKKYVCK LLFIFLLGHD IDFGHMEAVN LLSSNKYSEK QIGYLFISVL
110 120 130 140 150
VNTNSDLIRL IIQSIKNDLQ SRNPVHVNLA LQCIANIGSR DMAESFSNEI
160 170 180 190 200
PKLLVSGDTM DVVKQSAALC LLRLFRSSPD IIPGGEWTSR IIHLLNDQHM
210 220 230 240 250
GVVTAATSLI DALVKRNPDE YKGCVNLAVS RLSRIVTASY TDLQDYTYYF
260 270 280 290 300
VPAPWLSVKL LRLLQNYNPV TEEAGVRARL NETLETILNK AQEPPKSKKV
310 320 330 340 350
QHSNAKNAVL FEAINLIIHS DSEPNLLVRA CNQLGQFLSN RETNLRYLAL
360 370 380 390 400
ESMCHLATSE FSHEEVKKHQ EVVILSMKME KDVSVRQMAV DLLYAMCDRG
410 420 430 440 450
NAEEIVQEML NYLETADYSI REEMVLKVAI LAEKYATDYT WYVDVILNLI
460 470 480 490 500
RIAGDYVSEE VWYRVIQIVI NREEVQGYAA KTVFEALQAP ACHENMVKVG
510 520 530 540 550
GYILGEFGNL IAGDSRSAPL VQFKLLHSKY HLCSPMTRAL LLSTYIKFIN
560 570 580 590 600
LFPEIRTNIQ DVFRQHSNLR SADAELQQRA SEYLQLSIVA STDVLATVLE
610 620 630 640 650
EMPSFPERES SILAVLKKKK PGRVPENEIR ESKSPAPLTS AAQNNALVNN
660 670 680 690 700
SHSKLNNSNA NTDLLGLSTP PSNNIGSGSN SNSTLIDVLG DMYGSNSNNN
710 720 730 740 750
SSAVYNTKKF LFKNNGVLFE NEMLQIGVKS EFRQNLGRLG LFYGNKTQVP
760 770 780 790 800
LTNFNPVLQW SAEDALKLNV QMKVVEPTLE AGAQIQQLLT AECIEDYADA
810 820 830 840 850
PTIEISFRYN GTQQKFSIKL PLSVNKFFEP TEMNAESFFA RWKNLSGEQQ
860 870 880 890 900
RSQKVFKAAQ PLDLPGARNK LMGFGMQLLD QVDPNPDNMV CAGIIHTQSQ
910 920 930 940
QVGCLMRLEP NKQAQMFRLT VRASKETVTR EICDLLTDQF
Length:940
Mass (Da):105,620
Last modified:May 1, 1997 - v1
Checksum:iF745045CD2C1D9C5
GO
Isoform B (identifier: P91926-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-21: APVRGDGMRGLAVFISDIRN → ERAEGCEVVSPIDQSRGGKESEASADESLLFY

Note: No experimental confirmation available.
Show »
Length:952
Mass (Da):106,935
Checksum:iA98F090B3B6464BE
GO

Sequence cautioni

The sequence AAO39461.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti325 – 3251N → E in CAA73533 (PubMed:9285813).Curated
Sequence conflicti489 – 4891A → P in CAA73533 (PubMed:9285813).Curated
Sequence conflicti587 – 5871S → N in CAA73533 (PubMed:9285813).Curated
Sequence conflicti709 – 7124KFLF → FVS in CAA73533 (PubMed:9285813).Curated
Sequence conflicti722 – 7232EM → GK in CAA73533 (PubMed:9285813).Curated
Sequence conflicti741 – 7433LFY → FSN in CAA73533 (PubMed:9285813).Curated
Sequence conflicti877 – 8771Q → P in CAA73533 (PubMed:9285813).Curated

RNA editingi

Edited at position 207.2 Publications
Partially edited. Target of Adar.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti207 – 2071T → A in RNA edited version.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2 – 2120APVRG…SDIRN → ERAEGCEVVSPIDQSRGGKE SEASADESLLFY in isoform B. CuratedVSP_023135Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11104 mRNA. Translation: CAA71991.1.
Y13092 mRNA. Translation: CAA73533.1.
AE014134 Genomic DNA. Translation: AAF56103.2.
AE014134 Genomic DNA. Translation: AAS64634.1.
BT032839 mRNA. Translation: ACD81853.1.
BT003458 mRNA. Translation: AAO39461.1. Different initiation.
RefSeqiNP_476819.2. NM_057471.6. [P91926-1]
NP_995607.1. NM_205885.2. [P91926-2]
UniGeneiDm.246.

Genome annotation databases

EnsemblMetazoaiFBtr0089488; FBpp0088490; FBgn0264855. [P91926-1]
GeneIDi33211.
KEGGidme:Dmel_CG4260.

Keywords - Coding sequence diversityi

Alternative splicing, RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11104 mRNA. Translation: CAA71991.1.
Y13092 mRNA. Translation: CAA73533.1.
AE014134 Genomic DNA. Translation: AAF56103.2.
AE014134 Genomic DNA. Translation: AAS64634.1.
BT032839 mRNA. Translation: ACD81853.1.
BT003458 mRNA. Translation: AAO39461.1. Different initiation.
RefSeqiNP_476819.2. NM_057471.6. [P91926-1]
NP_995607.1. NM_205885.2. [P91926-2]
UniGeneiDm.246.

3D structure databases

ProteinModelPortaliP91926.
SMRiP91926. Positions 5-614, 706-940.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59467. 12 interactions.
IntActiP91926. 2 interactions.
MINTiMINT-7714518.
STRINGi7227.FBpp0088945.

PTM databases

iPTMnetiP91926.

Proteomic databases

PaxDbiP91926.
PRIDEiP91926.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0089488; FBpp0088490; FBgn0264855. [P91926-1]
GeneIDi33211.
KEGGidme:Dmel_CG4260.

Organism-specific databases

CTDi33211.
FlyBaseiFBgn0264855. AP-2alpha.

Phylogenomic databases

eggNOGiKOG1077. Eukaryota.
ENOG410XNQE. LUCA.
GeneTreeiENSGT00550000074757.
InParanoidiP91926.
KOiK11824.
OMAiFMEAPIL.
PhylomeDBiP91926.

Enzyme and pathway databases

ReactomeiR-DME-416993. Trafficking of GluR2-containing AMPA receptors.
R-DME-437239. Recycling pathway of L1.
R-DME-5099900. WNT5A-dependent internalization of FZD4.
SignaLinkiP91926.

Miscellaneous databases

GenomeRNAii33211.
PROiP91926.

Gene expression databases

BgeeiP91926.
ExpressionAtlasiP91926. differential.
GenevisibleiP91926. DM.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
2.60.40.1030. 1 hit.
3.30.310.30. 1 hit.
InterProiIPR017104. AP2_complex_asu.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR002553. Clathrin/coatomer_adapt-like_N.
IPR013038. Clathrin_a-adaptin_app_Ig-like.
IPR003164. Clathrin_a-adaptin_app_sub_C.
IPR008152. Clathrin_a/b/g-adaptin_app_Ig.
IPR015873. Clathrin_a/coatomer_app_sub_C.
IPR009028. Coatomer/calthrin_app_sub_C.
IPR013041. Coatomer/clathrin_app_Ig-like.
[Graphical view]
PfamiPF01602. Adaptin_N. 1 hit.
PF02296. Alpha_adaptin_C. 1 hit.
PF02883. Alpha_adaptinC2. 1 hit.
[Graphical view]
PIRSFiPIRSF037091. AP2_complex_alpha. 1 hit.
SMARTiSM00809. Alpha_adaptinC2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF49348. SSF49348. 1 hit.
SSF55711. SSF55711. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Role of Drosophila alpha-adaptin in presynaptic vesicle recycling."
    Gonzalez-Gaitan M.A., Jaeckle H.
    Cell 88:767-776(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: Canton-S.
    Tissue: Embryo.
  2. "Alpha-adaptin, a marker for endocytosis, is expressed in complex patterns during Drosophila development."
    Dornan S.C., Jackson A.P., Gay N.J.
    Mol. Biol. Cell 8:1391-1403(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Embryo.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  5. Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: Berkeley.
    Tissue: Embryo.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 93-940, RNA EDITING OF POSITION 207.
    Strain: Berkeley.
    Tissue: Head.
  7. "RNA editing in Drosophila melanogaster: new targets and functional consequences."
    Stapleton M., Carlson J.W., Celniker S.E.
    RNA 12:1922-1932(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA EDITING OF POSITION 207.
  8. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632 AND SER-634, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiAP2A_DROME
AccessioniPrimary (citable) accession number: P91926
Secondary accession number(s): B3DN51
, O01937, Q7KTZ5, Q86P64, Q9VPP4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 1, 1997
Last modified: June 8, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.