ARP5_YEAST
ID ARP5_YEAST Reviewed; 755 AA.
AC P53946; D6W1C0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Actin-related protein 5;
DE AltName: Full=Actin-like protein ARP5;
GN Name=ARP5; OrderedLocusNames=YNL059C; ORFNames=N2430, YNL2430C;
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 [GENOMIC DNA].
RC STRAIN=S288c / FY1676;
RX PubMed=8533472; DOI=10.1002/yea.320111008;
RA Bergez P., Doignon F., Crouzet M.;
RT "The sequence of a 44 420 bp fragment located on the left arm of chromosome
RT XIV from Saccharomyces cerevisiae.";
RL Yeast 11:967-974(1995).
RN [2]
RP ERRATUM OF PUBMED:8533472.
RX PubMed=8904343;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<297::aid-yea940>3.0.co;2-d;
RA Bergez P., Doignon F., Crouzet M.;
RL Yeast 12:297-297(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
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 [5]
RP GENE NAME.
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 [6]
RP IDENTIFICATION IN THE INO80 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12887900; DOI=10.1016/s1097-2765(03)00264-8;
RA Shen X., Ranallo R., Choi E., Wu C.;
RT "Involvement of actin-related proteins in ATP-dependent chromatin
RT remodeling.";
RL Mol. Cell 12:147-155(2003).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND SER-383, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [10]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-12, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Probably involved in transcription regulation via its
CC interaction with the INO80 complex, a chromatin remodeling complex.
CC -!- SUBUNIT: Component of the chromatin-remodeling INO80 complex, at least
CC composed of ARP4, ARP5, ARP8, RVB1, RVB2, TAF14, NHP10, IES1, IES3,
CC IES4, IES6, ACT1, IES2, IES5 and INO80. {ECO:0000269|PubMed:12887900}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 2170 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; U12141; AAA99652.1; -; Genomic_DNA.
DR EMBL; Z71335; CAA95933.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10486.1; -; Genomic_DNA.
DR PIR; S58718; S58718.
DR RefSeq; NP_014339.1; NM_001182898.1.
DR AlphaFoldDB; P53946; -.
DR SMR; P53946; -.
DR BioGRID; 35763; 53.
DR ComplexPortal; CPX-863; INO80 chromatin remodeling complex.
DR IntAct; P53946; 26.
DR MINT; P53946; -.
DR STRING; 4932.YNL059C; -.
DR iPTMnet; P53946; -.
DR MaxQB; P53946; -.
DR PaxDb; P53946; -.
DR PRIDE; P53946; -.
DR EnsemblFungi; YNL059C_mRNA; YNL059C; YNL059C.
DR GeneID; 855665; -.
DR KEGG; sce:YNL059C; -.
DR SGD; S000005004; ARP5.
DR VEuPathDB; FungiDB:YNL059C; -.
DR eggNOG; KOG0681; Eukaryota.
DR GeneTree; ENSGT00720000108866; -.
DR HOGENOM; CLU_008246_1_0_1; -.
DR InParanoid; P53946; -.
DR OMA; TNWNHQE; -.
DR BioCyc; YEAST:G3O-33090-MON; -.
DR PRO; PR:P53946; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53946; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031011; C:Ino80 complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IDA:SGD.
DR GO; GO:0006281; P:DNA repair; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR027664; Arp5.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR PANTHER; PTHR11937:SF16; PTHR11937:SF16; 1.
DR Pfam; PF00022; Actin; 2.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 1: Evidence at protein level;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..755
FT /note="Actin-related protein 5"
FT /id="PRO_0000089104"
FT REGION 418..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 24
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 12
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 755 AA; 87560 MW; D8748B9096B32B53 CRC64;
MSSRDASLTP LKAVVIDDPP LRQTPEPFDE QSAYNPQSPI AIDFGSSKLR AGFVNHATPT
HIFPNALTKF RDRKLNKNFT FVGNDTLLDQ AVRSQSRSPF DGPFVTNWNL TEEILDYTFH
HLGVVPDNGI PNPILLTERL ATVQSQRTNW YQILFETYNV PGVTFGIDSL FSFYNYNPSG
NKTGLVISCG HEDTNVIPVV DGAGILTDAK RINWGGHQAV DYLNDLMALK YPYFPTKMSY
LQYETMYKDY CYVSRNYDED IEKILTLENL DTNDVVVEAP FTEVLQPQKT EEELRIQAEK
RKETGKRLQE QARLKRMEKL VQKQEEFEYF SKVRDQLIDE PKKKVLSVLQ NAGFDDERDF
KKYLHSLEQS LKKAQMVEAE DDSHLDEMNE DKTAQKFDLL DIADEDLNED QIKEKRKQRF
LKASQDARQK AKEEKERVAK EEEEKKLKEQ QWRETDLNGW IKDKRLKLNK LIKRRKEKLK
LRDEMKDRKS QVSQNRMKNL ASLAEDNVKQ GAKRNRHQAT IDNDPNDTFG ANDEDWLIYT
DITQNPEAFE EALEYEYKDI VELERLLLEH DPNFTEEDTL EAQYDWRNSI LHLFLRGPRP
HDSENIHEQH QMHLNVERIR VPEVIFQPTM GGQDQAGICE LSETILLKKF GSQPGKLSQT
SIDMVNNVLI TGGNAKVPGL KERIVKEFTG FLPTGTNITV NMSSDPSLDA WKGMAALARN
EEQYRKTVIS KKEYEEYGPE YIKEHKLGNT KYFED
