GenomeNet

Database: UniProt
Entry: Q66HM2
LinkDB: Q66HM2
Original site: Q66HM2 
ID   Q66HM2_RAT              Unreviewed;       939 AA.
AC   Q66HM2;
DT   11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2004, sequence version 1.
DT   12-AUG-2020, entry version 147.
DE   RecName: Full=AP-2 complex subunit alpha {ECO:0000256|PIRNR:PIRNR037091};
GN   Name=Ap2a2 {ECO:0000313|EMBL:AAH81786.1,
GN   ECO:0000313|Ensembl:ENSRNOP00000060992, ECO:0000313|RGD:71015};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|EMBL:AAH81786.1};
RN   [1] {ECO:0000313|EMBL:AAH81786.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney {ECO:0000313|EMBL:AAH81786.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000060992, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000060992,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000060992}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000060992};
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
CC   -!- FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor
CC       protein complexes function in protein transport via transport vesicles
CC       in different membrane traffic pathways. Adaptor protein complexes are
CC       vesicle coat components and appear to be involved in cargo selection
CC       and vesicle formation. AP-2 is involved in clathrin-dependent
CC       endocytosis in which cargo proteins are incorporated into vesicles
CC       surrounded by clathrin (clathrin-coated vesicles, CCVs) which are
CC       destined for fusion with the early endosome. The clathrin lattice
CC       serves as a mechanical scaffold but is itself unable to bind directly
CC       to membrane components. Clathrin-associated adaptor protein (AP)
CC       complexes which can bind directly to both the clathrin lattice and to
CC       the lipid and protein components of membranes are considered to be the
CC       major clathrin adaptors contributing the CCV formation. AP-2 also
CC       serves as a cargo receptor to selectively sort the membrane proteins
CC       involved in receptor-mediated endocytosis. AP-2 seems to play a role in
CC       the recycling of synaptic vesicle membranes from the presynaptic
CC       surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-
CC       [LI] endocytosis signal motifs within the cytosolic tails of
CC       transmembrane cargo molecules. AP-2 may also play a role in maintaining
CC       normal post-endocytic trafficking through the ARF6-regulated, non-
CC       clathrin pathway. The AP-2 alpha subunit binds polyphosphoinositide-
CC       containing lipids, positioning AP-2 on the membrane. The AP-2 alpha
CC       subunit acts via its C-terminal appendage domain as a scaffolding
CC       platform for endocytic accessory proteins. The AP-2 alpha and AP-2
CC       sigma subunits are thought to contribute to the recognition of the
CC       [ED]-X-X-X-L-[LI] motif. {ECO:0000256|PIRNR:PIRNR037091}.
CC   -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer composed
CC       of two large adaptins (alpha-type subunit AP2A1 or AP2A2 and beta-type
CC       subunit AP2B1), a medium adaptin (mu-type subunit AP2M1) and a small
CC       adaptin (sigma-type subunit AP2S1). {ECO:0000256|PIRNR:PIRNR037091}.
CC   -!- SUBCELLULAR LOCATION: Membrane, coated pit
CC       {ECO:0000256|PIRNR:PIRNR037091}.
CC   -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC       {ECO:0000256|ARBA:ARBA00006613, ECO:0000256|PIRNR:PIRNR037091}.
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DR   EMBL; AC109542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC081786; AAH81786.1; -; mRNA.
DR   RefSeq; NP_112270.2; NM_031008.2.
DR   IntAct; Q66HM2; 2.
DR   Ensembl; ENSRNOT00000064254; ENSRNOP00000060992; ENSRNOG00000019534.
DR   GeneID; 81637; -.
DR   KEGG; rno:81637; -.
DR   CTD; 161; -.
DR   RGD; 71015; Ap2a2.
DR   GeneTree; ENSGT00950000182838; -.
DR   HOGENOM; CLU_003824_1_0_1; -.
DR   KO; K11824; -.
DR   OMA; TKTTQVG; -.
DR   OrthoDB; 751651at2759; -.
DR   TreeFam; TF300308; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000019534; Expressed in frontal cortex and 21 other tissues.
DR   GO; GO:0030122; C:AP-2 adaptor complex; IEA:Ensembl.
DR   GO; GO:0035615; F:clathrin adaptor activity; IEA:InterPro.
DR   GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR   GO; GO:0072583; P:clathrin-dependent endocytosis; IEA:Ensembl.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
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   Coated pit {ECO:0000256|ARBA:ARBA00023176, ECO:0000256|PIRNR:PIRNR037091};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Endocytosis {ECO:0000256|ARBA:ARBA00022583, ECO:0000256|PIRNR:PIRNR037091};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR037091};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW   ECO:0000256|PIRNR:PIRNR037091};
KW   Proteomics identification {ECO:0000213|PeptideAtlas:Q66HM2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037091}.
FT   DOMAIN          707..820
FT                   /note="Alpha_adaptinC2"
FT                   /evidence="ECO:0000259|SMART:SM00809"
FT   REGION          616..683
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          23..43
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        616..639
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         43
FT                   /note="Phosphatidylinositol lipid headgroup"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037091-1"
FT   BINDING         53
FT                   /note="Phosphatidylinositol lipid headgroup"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037091-1"
FT   BINDING         57
FT                   /note="Phosphatidylinositol lipid headgroup"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037091-1"
FT   BINDING         58
FT                   /note="Phosphatidylinositol lipid headgroup"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037091-1"
FT   BINDING         61
FT                   /note="Phosphatidylinositol lipid headgroup"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037091-1"
SQ   SEQUENCE   939 AA;  104174 MW;  D6A7EB7EE919F566 CRC64;
     MPAVSKGEGM 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 PEDPAVRGRL TECLETILNK AQEPPKSKKV
     QHSNAKNAVL FEAISLIIHH DSEPNLLVRA CNQLGQFLQH RETNLRYLAL ESMCTLASSE
     FSHEAVKTHI ETVINALKTE RDVSVRQRAV DLLYAMCDRS NAQQIVAEML SYLETADYSI
     REEIVLKVAI LAEKYAVDYT WYVDTILNLI RIAGDYVSEE VWYRVIQIVI NRDDVQGYAA
     KTVFEALQAP ACHENLVKVG GYILGEFGNL IAGDPRSSPL IQFNLLHSKF HLCSVPTRAL
     LLSTYIKFVN LFPEVKATIQ DVLRSDSQLK NADVELQQRA VEYLRLSTVA STDILATVLE
     EMPPFPERES SILAKLKKKK GPSTVTDLEE TKRERSIDVN GGPEPVPAST SAASTPSPSA
     DLLGLGAVPP APTGPPPTSG GGLLVDVFSD SASAVAPLAP GSEDNFARFV CKNNGVLFEN
     QLLQIGLKSE FRQNLGRMFI FYGNKTSTQF LNFTPTLICA DDLQTNLNLQ TKPVDPTVDG
     GAQVQQVVNI ECISDFTEAP VLNIQFRYGG TFQNVSVKLP ITLNKFFQPT EMASQDFFQR
     WKQLSNPQQE VQNIFKAKHP MDTEITKAKI IGFGSALLEE VDPNPANFVG AGIIHTKTTQ
     IGCLLRLEPN LQAQMYRLTL RTSKDTVSQR LCELLSEQF
//
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