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ARP6_YEAST
ID   ARP6_YEAST              Reviewed;         438 AA.
AC   Q12509; D6VY85;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 169.
DE   RecName: Full=Actin-like protein ARP6;
GN   Name=ARP6; OrderedLocusNames=YLR085C; ORFNames=L2393, L9449.13;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   NOMENCLATURE.
RX   PubMed=9290209;
RX   DOI=10.1002/(sici)1097-0061(19970915)13:11<1053::aid-yea164>3.0.co;2-4;
RA   Poch O., Winsor B.;
RT   "Who's who among the Saccharomyces cerevisiae actin-related proteins? A
RT   classification and nomenclature proposal for a large family.";
RL   Yeast 13:1053-1058(1997).
RN   [4]
RP   IDENTIFICATION IN THE SWR1 COMPLEX, FUNCTION OF THE SWR1 COMPLEX, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=14690608; DOI=10.1016/s1097-2765(03)00497-0;
RA   Krogan N.J., Keogh M.-C., Datta N., Sawa C., Ryan O.W., Ding H., Haw R.A.,
RA   Pootoolal J., Tong A., Canadien V., Richards D.P., Wu X., Emili A.,
RA   Hughes T.R., Buratowski S., Greenblatt J.F.;
RT   "A Snf2 family ATPase complex required for recruitment of the histone H2A
RT   variant Htz1.";
RL   Mol. Cell 12:1565-1576(2003).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   IDENTIFICATION IN THE SWR1 COMPLEX, FUNCTION OF THE SWR1 COMPLEX, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15045029; DOI=10.1371/journal.pbio.0020131;
RA   Kobor M.S., Venkatasubrahmanyam S., Meneghini M.D., Gin J.W.,
RA   Jennings J.L., Link A.J., Madhani H.D., Rine J.;
RT   "A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p
RT   deposits histone variant H2A.Z into euchromatin.";
RL   PLoS Biol. 2:587-599(2004).
RN   [8]
RP   IDENTIFICATION IN THE SWR1 COMPLEX, FUNCTION OF THE SWR1 COMPLEX, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=14645854; DOI=10.1126/science.1090701;
RA   Mizuguchi G., Shen X., Landry J., Wu W.-H., Sen S., Wu C.;
RT   "ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin
RT   remodeling complex.";
RL   Science 303:343-348(2004).
CC   -!- FUNCTION: Component of the SWR1 complex which mediates the ATP-
CC       dependent exchange of histone H2A for the H2A variant HZT1 leading to
CC       transcriptional regulation of selected genes by chromatin remodeling.
CC       Involved in chromosome stability. {ECO:0000269|PubMed:14645854,
CC       ECO:0000269|PubMed:14690608, ECO:0000269|PubMed:15045029}.
CC   -!- SUBUNIT: Component of the SWR1 chromatin remodeling complex composed of
CC       at least ACT1, ARP4, RVB1, RVB2, ARP6, YAF9, VPS71, VPS72, SWC3, SWC4,
CC       SWC5, SWC7 and SWR1, and perhaps BDF1. {ECO:0000269|PubMed:14645854,
CC       ECO:0000269|PubMed:14690608, ECO:0000269|PubMed:15045029}.
CC   -!- INTERACTION:
CC       Q12509; Q03433: VPS71; NbExp=3; IntAct=EBI-2957, EBI-27814;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 238 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the actin family. ARP6 subfamily. {ECO:0000305}.
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DR   EMBL; U53880; AAB67589.1; -; Genomic_DNA.
DR   EMBL; Z73257; CAA97645.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09401.1; -; Genomic_DNA.
DR   PIR; S64917; S64917.
DR   RefSeq; NP_013186.1; NM_001181972.1.
DR   PDB; 6GEJ; EM; 3.60 A; R=1-438.
DR   PDB; 6GEN; EM; 3.60 A; R=1-438.
DR   PDBsum; 6GEJ; -.
DR   PDBsum; 6GEN; -.
DR   AlphaFoldDB; Q12509; -.
DR   SMR; Q12509; -.
DR   BioGRID; 31358; 762.
DR   ComplexPortal; CPX-2122; Swr1 chromatin remodelling complex.
DR   DIP; DIP-5169N; -.
DR   IntAct; Q12509; 14.
DR   MINT; Q12509; -.
DR   STRING; 4932.YLR085C; -.
DR   MaxQB; Q12509; -.
DR   PaxDb; Q12509; -.
DR   PRIDE; Q12509; -.
DR   EnsemblFungi; YLR085C_mRNA; YLR085C; YLR085C.
DR   GeneID; 850774; -.
DR   KEGG; sce:YLR085C; -.
DR   SGD; S000004075; ARP6.
DR   VEuPathDB; FungiDB:YLR085C; -.
DR   eggNOG; KOG0680; Eukaryota.
DR   GeneTree; ENSGT00720000108833; -.
DR   HOGENOM; CLU_027965_1_1_1; -.
DR   InParanoid; Q12509; -.
DR   OMA; FFEEYEC; -.
DR   BioCyc; YEAST:G3O-32236-MON; -.
DR   PRO; PR:Q12509; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q12509; protein.
DR   GO; GO:0000785; C:chromatin; IDA:ComplexPortal.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0034399; C:nuclear periphery; IDA:SGD.
DR   GO; GO:0000812; C:Swr1 complex; IDA:SGD.
DR   GO; GO:0031491; F:nucleosome binding; IMP:SGD.
DR   GO; GO:0006338; P:chromatin remodeling; IDA:SGD.
DR   GO; GO:0043486; P:histone exchange; IMP:SGD.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR030054; Arp6.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; PTHR11937; 1.
DR   PANTHER; PTHR11937:SF47; PTHR11937:SF47; 1.
DR   Pfam; PF00022; Actin; 1.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Chromatin regulator; Cytoplasm; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..438
FT                   /note="Actin-like protein ARP6"
FT                   /id="PRO_0000089121"
FT   REGION          158..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   438 AA;  50044 MW;  92D201F62D04232B CRC64;
     METPPIVIDN GSYEIKFGPS TNKKPFRALN ALAKDKFGTS YLSNHIKNIK DISSITFRRP
     HELGQLTLWE LESCIWDYCL FNPSEFDGFD LKEGKGHHLV ASESCMTLPE LSKHADQVIF
     EEYEFDSLFK SPVAVFVPFT KSYKGEMRTI SGKDEDIDIV RGNSDSTNST SSESKNAQDS
     GSDYHDFQLV IDSGFNCTWI IPVLKGIPYY KAVKKLDIGG RFLTGLLKET LSFRHYNMMD
     ETILVNNIKE QCLFVSPVSY FDSFKTKDKH ALEYVLPDFQ TSFLGYVRNP RKENVPLPED
     AQIITLTDEL FTIPETFFHP EISQITKPGI VEAILESLSM LPEIVRPLMV GNIVCTGGNF
     NLPNFAQRLA AELQRQLPTD WTCHVSVPEG DCALFGWEVM SQFAKTDSYR KARVTREEYY
     EHGPDWCTKH RFGYQNWI
 
 
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