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AP-2 complex subunit alpha-2 (100 kDa coated vesicle protein C) (Adaptor protein complex AP-2 subunit alpha-2) (Adaptor-related protein complex 2 subunit alpha-2) (Alpha-adaptin C) (Alpha2-adaptin) (Clathrin assembly protein complex 2 alpha-C large chain) (Plasma membrane adaptor HA2/AP2 adaptin alpha C subunit)

 AP2A2_MOUSE             Reviewed;         938 AA.
P17427; Q8C2J5; Q921V0;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
30-AUG-2017, entry version 175.
RecName: Full=AP-2 complex subunit alpha-2;
AltName: Full=100 kDa coated vesicle protein C;
AltName: Full=Adaptor protein complex AP-2 subunit alpha-2;
AltName: Full=Adaptor-related protein complex 2 subunit alpha-2;
AltName: Full=Alpha-adaptin C;
AltName: Full=Alpha2-adaptin;
AltName: Full=Clathrin assembly protein complex 2 alpha-C large chain;
AltName: Full=Plasma membrane adaptor HA2/AP2 adaptin alpha C subunit;
Name=Ap2a2; Synonyms=Adtab;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=2564002; DOI=10.1083/jcb.108.3.833;
Robinson M.S.;
"Cloning of cDNAs encoding two related 100-kD coated vesicle proteins
(alpha-adaptins).";
J. Cell Biol. 108:833-842(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NOD; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 104-859.
TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 379-938.
TISSUE=Fetal liver;
PubMed=9618202; DOI=10.1006/abio.1998.2653;
Jurecic R., Nachtman R.G., Colicos S.M., Belmont J.W.;
"Identification and cloning of differentially expressed genes by long-
distance differential display.";
Anal. Biochem. 259:235-244(1998).
[6]
FUNCTION, SUBUNIT, INTERACTION WITH CLATHRIN, AND MUTAGENESIS OF
LYS-31; ARG-32; LYS-35; LYS-45; LYS-55; LYS-56; LYS-57 AND LYS-61.
PubMed=10459011; DOI=10.1083/jcb.146.4.755;
Gaidarov I., Keen J.H.;
"Phosphoinositide-AP-2 interactions required for targeting to plasma
membrane clathrin-coated pits.";
J. Cell Biol. 146:755-764(1999).
[7]
INTERACTION WITH DAB2.
PubMed=11247302; DOI=10.1034/j.1600-0854.2001.020206.x;
Morris S.M., Cooper J.A.;
"Disabled-2 colocalizes with the LDLR in clathrin-coated pits and
interacts with AP-2.";
Traffic 2:111-123(2001).
[8]
FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
PubMed=14745134; DOI=10.1247/csf.28.419;
Nakatsu F., Ohno H.;
"Adaptor protein complexes as the key regulators of protein sorting in
the post-Golgi network.";
Cell Struct. Funct. 28:419-429(2003).
[9]
SUBCELLULAR LOCATION.
PubMed=14530274; DOI=10.1074/jbc.C300390200;
Rappoport J.Z., Taha B.W., Lemeer S., Benmerah A., Simon S.M.;
"The AP-2 complex is excluded from the dynamic population of plasma
membrane-associated clathrin.";
J. Biol. Chem. 278:47357-47360(2003).
[10]
FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
PubMed=15473838; DOI=10.1146/annurev.cellbio.20.010403.104543;
Owen D.J., Collins B.M., Evans P.R.;
"Adaptors for clathrin coats: structure and function.";
Annu. Rev. Cell Dev. Biol. 20:153-191(2004).
[11]
SUBCELLULAR LOCATION.
PubMed=17035303; DOI=10.1152/ajpcell.00160.2006;
Rappoport J.Z., Kemal S., Benmerah A., Simon S.M.;
"Dynamics of clathrin and adaptor proteins during endocytosis.";
Am. J. Physiol. 291:C1072-C1081(2006).
[12]
INTERACTION WITH DKGD, AND MUTAGENESIS OF TRP-840.
PubMed=17880279; DOI=10.1042/BJ20070755;
Kawasaki T., Kobayashi T., Ueyama T., Shirai Y., Saito N.;
"Regulation of clathrin-dependent endocytosis by diacylglycerol kinase
delta: importance of kinase activity and binding to AP2alpha.";
Biochem. J. 409:471-479(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[14]
INTERACTION WITH DENND1A; DENND1B AND DENND1C, AND MUTAGENESIS OF
GLN-782 AND ARG-916.
PubMed=20154091; DOI=10.1074/jbc.M109.050930;
Marat A.L., McPherson P.S.;
"The connecdenn family, Rab35 guanine nucleotide exchange factors
interfacing with the clathrin machinery.";
J. Biol. Chem. 285:10627-10637(2010).
[15]
INTERACTION WITH FCHO1.
PubMed=22484487; DOI=10.1038/ncb2473;
Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B.,
Tsang M., Traub L.M.;
"Distinct and separable activities of the endocytic clathrin-coat
components Fcho1/2 and AP-2 in developmental patterning.";
Nat. Cell Biol. 14:488-501(2012).
[16]
INTERACTION WITH ATAT1.
PubMed=24097348; DOI=10.1038/nature12571;
Montagnac G., Meas-Yedid V., Irondelle M., Castro-Castro A.,
Franco M., Shida T., Nachury M.V., Benmerah A., Olivo-Marin J.C.,
Chavrier P.;
"alphaTAT1 catalyses microtubule acetylation at clathrin-coated
pits.";
Nature 502:567-570(2013).
[17]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 701-938, MUTAGENESIS OF
PHE-837; TRP-840; GLU-849; ARG-905; GLU-907 AND ARG-920, AND
INTERACTION WITH AMPH; EPS15; EPN1; SNAP91; BIN1 AND AUXILIN.
PubMed=10380931; DOI=10.1016/S0092-8674(00)80791-6;
Owen D.J., Vallis Y., Noble M.E.M., Hunter J.B., Dafforn T.R.,
Evans P.R., McMahon H.T.;
"A structural explanation for the binding of multiple ligands by the
alpha-adaptin appendage domain.";
Cell 97:805-815(1999).
[18]
X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 9-592 IN COMPLEX WITH AP2B1;
AP2M1; AP2S1 AND AN INOSITOL POLYPHOSPHATE HEADGROUP.
PubMed=12086608; DOI=10.1016/S0092-8674(02)00735-3;
Collins B.M., McCoy A.J., Kent H.M., Evans P.R., Owen D.J.;
"Molecular architecture and functional model of the endocytic AP2
complex.";
Cell 109:523-535(2002).
[19]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 701-938 IN COMPLEX WITH
EPS15; EPN1 OR AMPH.
PubMed=12057195; DOI=10.1016/S0969-2126(02)00784-0;
Brett T.J., Traub L.M., Fremont D.H.;
"Accessory protein recruitment motifs in clathrin-mediated
endocytosis.";
Structure 10:797-809(2002).
[20]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 692-938, MUTAGENESIS OF
PHE-837; ARG-905 AND ARG-916, AND INTERACTION WITH EPN1; EPS15; AMPH;
SNAP91 AND BIN1.
PubMed=10430869; DOI=10.1073/pnas.96.16.8907;
Traub L.M., Downs M.A., Westrich J.L., Fremont D.H.;
"Crystal structure of the alpha appendage of AP-2 reveals a
recruitment platform for clathrin-coat assembly.";
Proc. Natl. Acad. Sci. U.S.A. 96:8907-8912(1999).
[21]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-620 IN COMPLEX WITH AP2B1;
AP2M1; AP2S1 AND CD4 INTERNALIZATION SIGNAL, AND MUTAGENESIS OF
ARG-21.
PubMed=19140243; DOI=10.1038/nature07422;
Kelly B.T., McCoy A.J., Spaete K., Miller S.E., Evans P.R.,
Hoening S., Owen D.J.;
"A structural explanation for the binding of endocytic dileucine
motifs by the AP2 complex.";
Nature 456:976-979(2008).
-!- FUNCTION: Component of the adaptor protein complex 2 (AP-2).
Adaptor protein complexes function in protein transport via
transport vesicles in different membrane traffic pathways. Adaptor
protein complexes are vesicle coat components and appear to be
involved in cargo selection and vesicle formation. AP-2 is
involved in clathrin-dependent endocytosis in which cargo proteins
are incorporated into vesicles surrounded by clathrin (clathrin-
coated vesicles, CCVs) which are destined for fusion with the
early endosome. The clathrin lattice serves as a mechanical
scaffold but is itself unable to bind directly to membrane
components. Clathrin-associated adaptor protein (AP) complexes
which can bind directly to both the clathrin lattice and to the
lipid and protein components of membranes are considered to be the
major clathrin adaptors contributing the CCV formation. AP-2 also
serves as a cargo receptor to selectively sort the membrane
proteins involved in receptor-mediated endocytosis. AP-2 seems to
play a role in the recycling of synaptic vesicle membranes from
the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi)
and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the
cytosolic tails of transmembrane cargo molecules. AP-2 may also
play a role in maintaining normal post-endocytic trafficking
through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha
subunit binds polyphosphoinositide-containing lipids, positioning
AP-2 on the membrane. The AP-2 alpha subunit acts via its C-
terminal appendage domain as a scaffolding platform for endocytic
accessory proteins. The AP-2 alpha and AP-2 sigma subunits are
thought to contribute to the recognition of the [ED]-X-X-X-L-[LI]
motif. {ECO:0000269|PubMed:10459011, ECO:0000269|PubMed:14745134,
ECO:0000269|PubMed:15473838}.
-!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer
composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2
and beta-type subunit AP2B1), a medium adaptin (mu-type subunit
AP2M1) and a small adaptin (sigma-type subunit AP2S1). Binds EPN1,
EPS15, AMPH, SNAP91 and BIN1. Interacts with HIP1 (By similarity).
Interacts with DGKD isoform 2. Interacts with DENND1A, DENND1B and
DENND1C. Interacts with FCHO1 and DAB2. Interacts with ATAT1; this
interaction is required for efficient alpha-tubulin acetylation by
ATAT1. {ECO:0000250, ECO:0000269|PubMed:10380931,
ECO:0000269|PubMed:10430869, ECO:0000269|PubMed:10459011,
ECO:0000269|PubMed:11247302, ECO:0000269|PubMed:12057195,
ECO:0000269|PubMed:12086608, ECO:0000269|PubMed:17880279,
ECO:0000269|PubMed:19140243, ECO:0000269|PubMed:20154091,
ECO:0000269|PubMed:22484487, ECO:0000269|PubMed:24097348}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14530274,
ECO:0000269|PubMed:17035303}; Peripheral membrane protein
{ECO:0000305}; Cytoplasmic side {ECO:0000305}. Membrane, coated
pit {ECO:0000269|PubMed:17035303}; Peripheral membrane protein
{ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=AP-2 appears
to be excluded from internalizing CCVs and to disengage from sites
of endocytosis seconds before internalization of the nascent CCV.
{ECO:0000269|PubMed:17035303}.
-!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
{ECO:0000305}.
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EMBL; X14972; CAA33097.1; -; mRNA.
EMBL; AK088500; BAC40392.1; -; mRNA.
EMBL; AC158224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC102524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC010597; AAH10597.1; -; mRNA.
EMBL; AF006990; AAB62703.1; -; mRNA.
CCDS; CCDS40188.1; -.
PIR; B30111; B30111.
PIR; S12471; S12471.
RefSeq; NP_031485.3; NM_007459.3.
UniGene; Mm.253090; -.
PDB; 1B9K; X-ray; 1.90 A; A=701-938.
PDB; 1KY6; X-ray; 2.00 A; A=701-938.
PDB; 1KY7; X-ray; 2.15 A; A=701-938.
PDB; 1KYD; X-ray; 2.00 A; A=701-938.
PDB; 1KYF; X-ray; 1.22 A; A=701-938.
PDB; 1KYU; X-ray; 1.80 A; A=701-938.
PDB; 1QTP; X-ray; 1.60 A; A=701-938.
PDB; 1QTS; X-ray; 1.40 A; A=701-938.
PDB; 1W80; X-ray; 1.90 A; A=695-938.
PDB; 2JKR; X-ray; 2.98 A; A/L=1-620.
PDB; 2JKT; X-ray; 3.40 A; A/L=1-620.
PDB; 2VJ0; X-ray; 1.60 A; A=695-938.
PDB; 3HS8; X-ray; 1.90 A; A=702-938.
PDBsum; 1B9K; -.
PDBsum; 1KY6; -.
PDBsum; 1KY7; -.
PDBsum; 1KYD; -.
PDBsum; 1KYF; -.
PDBsum; 1KYU; -.
PDBsum; 1QTP; -.
PDBsum; 1QTS; -.
PDBsum; 1W80; -.
PDBsum; 2JKR; -.
PDBsum; 2JKT; -.
PDBsum; 2VJ0; -.
PDBsum; 3HS8; -.
ProteinModelPortal; P17427; -.
SMR; P17427; -.
BioGrid; 198130; 12.
DIP; DIP-32160N; -.
IntAct; P17427; 17.
MINT; MINT-101068; -.
STRING; 10090.ENSMUSP00000003038; -.
iPTMnet; P17427; -.
PhosphoSitePlus; P17427; -.
SwissPalm; P17427; -.
EPD; P17427; -.
MaxQB; P17427; -.
PaxDb; P17427; -.
PeptideAtlas; P17427; -.
PRIDE; P17427; -.
Ensembl; ENSMUST00000003038; ENSMUSP00000003038; ENSMUSG00000002957.
GeneID; 11772; -.
KEGG; mmu:11772; -.
UCSC; uc009kls.2; mouse.
CTD; 161; -.
MGI; MGI:101920; Ap2a2.
eggNOG; KOG1077; Eukaryota.
eggNOG; ENOG410XNQE; LUCA.
GeneTree; ENSGT00550000074757; -.
HOVERGEN; HBG050518; -.
InParanoid; P17427; -.
KO; K11824; -.
OMA; FMNLALH; -.
OrthoDB; EOG091G01JZ; -.
TreeFam; TF300308; -.
Reactome; R-MMU-177504; Retrograde neurotrophin signalling.
Reactome; R-MMU-2132295; MHC class II antigen presentation.
Reactome; R-MMU-416993; Trafficking of GluR2-containing AMPA receptors.
Reactome; R-MMU-437239; Recycling pathway of L1.
Reactome; R-MMU-5099900; WNT5A-dependent internalization of FZD4.
Reactome; R-MMU-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
Reactome; R-MMU-8866427; VLDLR internalisation and degradation.
Reactome; R-MMU-8964038; LDL clearance.
ChiTaRS; Ap2a2; mouse.
EvolutionaryTrace; P17427; -.
PMAP-CutDB; P17427; -.
PRO; PR:P17427; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000002957; -.
CleanEx; MM_AP2A2; -.
ExpressionAtlas; P17427; baseline and differential.
Genevisible; P17427; MM.
GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:BHF-UCL.
GO; GO:0030117; C:membrane coat; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0030141; C:secretory granule; TAS:MGI.
GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; NAS:BHF-UCL.
GO; GO:0016192; P:vesicle-mediated transport; TAS:MGI.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR017104; AP2_complex_asu.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
InterPro; IPR003164; Clathrin_a-adaptin_app_sub_C.
InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
InterPro; IPR013041; Coatomer/clathrin_app_Ig-like.
Pfam; PF01602; Adaptin_N; 1.
Pfam; PF02296; Alpha_adaptin_C; 1.
Pfam; PF02883; Alpha_adaptinC2; 1.
PIRSF; PIRSF037091; AP2_complex_alpha; 1.
SMART; SM00809; Alpha_adaptinC2; 1.
SUPFAM; SSF48371; SSF48371; 1.
SUPFAM; SSF49348; SSF49348; 1.
SUPFAM; SSF55711; SSF55711; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Coated pit; Complete proteome;
Endocytosis; Lipid-binding; Membrane; Protein transport;
Reference proteome; Transport.
CHAIN 1 938 AP-2 complex subunit alpha-2.
/FTId=PRO_0000193733.
REGION 5 80 Lipid-binding.
BINDING 43 43 Phosphatidylinositol lipid headgroup.
BINDING 53 53 Phosphatidylinositol lipid headgroup.
BINDING 57 57 Phosphatidylinositol lipid headgroup.
BINDING 58 58 Phosphatidylinositol lipid headgroup.
BINDING 61 61 Phosphatidylinositol lipid headgroup.
MUTAGEN 21 21 R->E: Reduces interaction with CD4
endocytosis signal motif; when associated
with AP2S1 S-15.
{ECO:0000269|PubMed:19140243}.
MUTAGEN 31 31 K->Q: Reduces phosphatidylinositol
binding. {ECO:0000269|PubMed:10459011}.
MUTAGEN 32 32 R->Q: Reduces phosphatidylinositol
binding. {ECO:0000269|PubMed:10459011}.
MUTAGEN 35 35 K->Q: Reduces phosphatidylinositol
binding. {ECO:0000269|PubMed:10459011}.
MUTAGEN 45 45 K->Q: Reduces phosphatidylinositol
binding. {ECO:0000269|PubMed:10459011}.
MUTAGEN 55 55 K->Q: Strongly reduces
phosphatidylinositol binding. Abolishes
phosphatidylinositol binding; when
associated with Q-56 and Q-57.
{ECO:0000269|PubMed:10459011}.
MUTAGEN 56 56 K->E: Strongly reduces
phosphatidylinositol binding.
{ECO:0000269|PubMed:10459011}.
MUTAGEN 56 56 K->Q: Strongly reduces
phosphatidylinositol binding. Abolishes
phosphatidylinositol binding; when
associated with Q-55 and Q-57.
{ECO:0000269|PubMed:10459011}.
MUTAGEN 57 57 K->Q: Strongly reduces
phosphatidylinositol binding. Abolishes
phosphatidylinositol binding; when
associated with Q-55 and Q-56.
{ECO:0000269|PubMed:10459011}.
MUTAGEN 61 61 K->Q: Reduces phosphatidylinositol
binding. {ECO:0000269|PubMed:10459011}.
MUTAGEN 727 727 K->A: No effect on DENND1A-,DENND1B- nor
DENND1C-binding.
MUTAGEN 782 782 Q->A: Reduces DENND1A- and DENND1C-
binding. {ECO:0000269|PubMed:20154091}.
MUTAGEN 837 837 F->A: Reduces SNAP91, AMPH and BIN1
binding. Abolishes AMPH and SNAP91
binding; when associated with A-916.
Abolishes EPN1 and EPS15 binding; when
associated with A-905.
{ECO:0000269|PubMed:10380931,
ECO:0000269|PubMed:10430869}.
MUTAGEN 840 840 W->A: Abolishes AMPH, BIN1, EPS15, EPN1,
auxilin and SNAP91 binding. Abolishes
interaction with DGKD.
{ECO:0000269|PubMed:10380931,
ECO:0000269|PubMed:17880279}.
MUTAGEN 849 849 E->A: No effect.
{ECO:0000269|PubMed:10380931}.
MUTAGEN 905 905 R->A: Strongly reduces AMPH, SNAP91,
auxilin and BIN1 binding. Abolishes EPN1
and EPS15 binding; when associated with
A-837. {ECO:0000269|PubMed:10380931,
ECO:0000269|PubMed:10430869}.
MUTAGEN 907 907 E->A: Strongly reduces AMPH, SNAP91 and
BIN1 binding. Slightly reduces EPS15 and
auxilin binding.
{ECO:0000269|PubMed:10380931}.
MUTAGEN 916 916 R->A: Strongly reduces AMPH and SNAP91
binding. Abolishes DENND1B-binding; no
effect on DENND1A-, nor DENND1C-binding.
Abolishes AMPH and SNAP91 binding; when
associated with A-837.
{ECO:0000269|PubMed:10430869,
ECO:0000269|PubMed:20154091}.
MUTAGEN 920 920 R->A: Abolishes AMPH and BIN1 binding.
Reduces EPS15, SNAP91 and auxilin
binding. {ECO:0000269|PubMed:10380931}.
CONFLICT 858 859 HP -> LE (in Ref. 4; AAH10597).
{ECO:0000305}.
CONFLICT 889 890 GA -> VL (in Ref. 1; CAA33097 and 5;
AAB62703). {ECO:0000305}.
HELIX 11 22 {ECO:0000244|PDB:2JKR}.
HELIX 28 40 {ECO:0000244|PDB:2JKR}.
TURN 41 43 {ECO:0000244|PDB:2JKR}.
STRAND 44 48 {ECO:0000244|PDB:2JKR}.
HELIX 52 66 {ECO:0000244|PDB:2JKR}.
TURN 67 69 {ECO:0000244|PDB:2JKR}.
HELIX 76 82 {ECO:0000244|PDB:2JKR}.
HELIX 88 100 {ECO:0000244|PDB:2JKR}.
HELIX 106 121 {ECO:0000244|PDB:2JKR}.
HELIX 125 138 {ECO:0000244|PDB:2JKR}.
HELIX 141 147 {ECO:0000244|PDB:2JKR}.
HELIX 150 156 {ECO:0000244|PDB:2JKR}.
HELIX 162 178 {ECO:0000244|PDB:2JKR}.
HELIX 180 182 {ECO:0000244|PDB:2JKR}.
HELIX 188 193 {ECO:0000244|PDB:2JKR}.
HELIX 194 197 {ECO:0000244|PDB:2JKR}.
HELIX 201 214 {ECO:0000244|PDB:2JKR}.
TURN 215 217 {ECO:0000244|PDB:2JKR}.
HELIX 219 222 {ECO:0000244|PDB:2JKR}.
HELIX 225 238 {ECO:0000244|PDB:2JKR}.
STRAND 241 244 {ECO:0000244|PDB:2JKR}.
TURN 245 247 {ECO:0000244|PDB:2JKR}.
STRAND 252 254 {ECO:0000244|PDB:2JKR}.
HELIX 255 265 {ECO:0000244|PDB:2JKR}.
HELIX 273 291 {ECO:0000244|PDB:2JKR}.
HELIX 299 319 {ECO:0000244|PDB:2JKR}.
HELIX 323 338 {ECO:0000244|PDB:2JKR}.
HELIX 343 355 {ECO:0000244|PDB:2JKR}.
STRAND 359 361 {ECO:0000244|PDB:2JKR}.
HELIX 364 368 {ECO:0000244|PDB:2JKR}.
HELIX 369 378 {ECO:0000244|PDB:2JKR}.
HELIX 382 393 {ECO:0000244|PDB:2JKR}.
TURN 398 400 {ECO:0000244|PDB:2JKR}.
HELIX 401 413 {ECO:0000244|PDB:2JKR}.
HELIX 417 434 {ECO:0000244|PDB:2JKR}.
HELIX 438 450 {ECO:0000244|PDB:2JKR}.
HELIX 453 455 {ECO:0000244|PDB:2JKR}.
HELIX 458 470 {ECO:0000244|PDB:2JKR}.
HELIX 475 485 {ECO:0000244|PDB:2JKR}.
STRAND 488 490 {ECO:0000244|PDB:2JKR}.
HELIX 493 505 {ECO:0000244|PDB:2JKR}.
HELIX 508 510 {ECO:0000244|PDB:2JKR}.
HELIX 514 516 {ECO:0000244|PDB:2JKR}.
HELIX 518 529 {ECO:0000244|PDB:2JKR}.
HELIX 534 550 {ECO:0000244|PDB:2JKR}.
TURN 552 554 {ECO:0000244|PDB:2JKR}.
HELIX 555 562 {ECO:0000244|PDB:2JKR}.
HELIX 565 568 {ECO:0000244|PDB:2JKR}.
HELIX 573 588 {ECO:0000244|PDB:2JKR}.
HELIX 591 597 {ECO:0000244|PDB:2JKR}.
STRAND 610 613 {ECO:0000244|PDB:2JKR}.
STRAND 617 620 {ECO:0000244|PDB:2JKR}.
TURN 701 704 {ECO:0000244|PDB:1QTS}.
HELIX 705 708 {ECO:0000244|PDB:1KYF}.
STRAND 714 718 {ECO:0000244|PDB:1KYF}.
STRAND 720 731 {ECO:0000244|PDB:1KYF}.
STRAND 734 743 {ECO:0000244|PDB:1KYF}.
STRAND 745 747 {ECO:0000244|PDB:1KYF}.
STRAND 749 757 {ECO:0000244|PDB:1KYF}.
HELIX 760 765 {ECO:0000244|PDB:1KYF}.
STRAND 766 770 {ECO:0000244|PDB:1KYF}.
STRAND 782 791 {ECO:0000244|PDB:1KYF}.
STRAND 800 807 {ECO:0000244|PDB:1KYF}.
STRAND 810 817 {ECO:0000244|PDB:1KYF}.
HELIX 822 825 {ECO:0000244|PDB:1KYF}.
STRAND 826 828 {ECO:0000244|PDB:1KYF}.
HELIX 833 840 {ECO:0000244|PDB:1KYF}.
HELIX 846 848 {ECO:0000244|PDB:1KYF}.
STRAND 849 855 {ECO:0000244|PDB:1KYF}.
HELIX 862 872 {ECO:0000244|PDB:1KYF}.
STRAND 874 877 {ECO:0000244|PDB:1KYF}.
STRAND 879 883 {ECO:0000244|PDB:1KYF}.
STRAND 886 894 {ECO:0000244|PDB:1KYF}.
STRAND 899 909 {ECO:0000244|PDB:1KYF}.
TURN 910 913 {ECO:0000244|PDB:1KYF}.
STRAND 914 923 {ECO:0000244|PDB:1KYF}.
HELIX 924 935 {ECO:0000244|PDB:1KYF}.
SEQUENCE 938 AA; 104017 MW; 183FE8DFE199DBCA CRC64;
MPAVSKGDGM RGLAVFISDI RNCKSKEAEI KRINKELANI RSKFKGDKAL DGYSKKKYVC
KLLFIFLLGH DIDFGHMEAV NLLSSNRYTE KQIGYLFISV LVNSNSELIR LINNAIKNDL
ASRNPTFMGL ALHCIANVGS REMAEAFAGE IPKILVAGDT MDSVKQSAAL CLLRLYRTSP
DLVPMGDWTS RVVHLLNDQH LGVVTAATSL ITTLAQKNPE EFKTSVSLAV SRLSRIVTSA
STDLQDYTYY FVPAPWLSVK LLRLLQCYPP PDPAVRGRLT ECLETILNKA QEPPKSKKVQ
HSNAKNAVLF EAISLIIHHD SEPNLLVRAC NQLGQFLQHR ETNLRYLALE SMCTLASSEF
SHEAVKTHIE TVINALKTER DVSVRQRAVD LLYAMCDRSN AQQIVAEMLS YLETADYSIR
EEIVLKVAIL AEKYAVDYTW YVDTILNLIR IAGDYVSEEV WYRVIQIVIN RDDVQGYAAK
TVFEALQAPA CHENLVKVGG YILGEFGNLI AGDPRSSPLI QFNLLHSKFH LCSVPTRALL
LSTYIKFVNL FPEVKATIQD VLRSDSQLKN ADVELQQRAV EYLRLSTVAS TDILATVLEE
MPPFPERESS ILAKLKKKKG PSTVTDLEET KRERSIDVNG GPEPVPASTS AASTPSPSAD
LLGLGAVPPA PTGPPPSSGG GLLVDVFSDS ASAVAPLAPG SEDNFARFVC KNNGVLFENQ
LLQIGLKSEF RQNLGRMFIF YGNKTSTQFL NFTPTLICAD DLQTNLNLQT KPVDPTVDGG
AQVQQVVNIE CISDFTEAPV LNIQFRYGGT FQNVSVKLPI TLNKFFQPTE MASQDFFQRW
KQLSNPQQEV QNIFKAKHPM DTEITKAKII GFGSALLEEV DPNPANFVGA GIIHTKTTQI
GCLLRLEPNL QAQMYRLTLR TSKDTVSQRL CELLSEQF


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