VPS72_YEAST
ID VPS72_YEAST Reviewed; 795 AA.
AC Q03388; D6VTA8;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Vacuolar protein sorting-associated protein 72;
DE AltName: Full=SWR complex protein 2;
GN Name=VPS72; Synonyms=SWC2; OrderedLocusNames=YDR485C;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [5]
RP FUNCTION.
RX PubMed=12134085; DOI=10.1091/mbc.02-01-0005;
RA Bonangelino C.J., Chavez E.M., Bonifacino J.S.;
RT "Genomic screen for vacuolar protein sorting genes in Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 13:2486-2501(2002).
RN [6]
RP FUNCTION, AND INTERACTION WITH ACT1; ARP4; RVB1; RVB2; ARP6; YAF9; VPS71;
RP SWC3; SWC4; SWC5; SWR1 AND HTZ1.
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 [7]
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 [8]
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 [9]
RP FUNCTION, AND INTERACTION WITH ACT1; ARP4; RVB1; RVB2; ARP6; YAF9; VPS71;
RP SWC3; SWC4; SWC5; SWR1 AND HTZ1.
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).
RN [10]
RP FUNCTION, AND INTERACTION WITH ACT1; ARP4; RVB1; RVB2; ARP6; YAF9; VPS71;
RP SWC3; SWC4; SWC5; SWR1 AND HTZ1.
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 [11]
RP INTERACTION WITH HTZ1.
RX PubMed=16299513; DOI=10.1038/nsmb1023;
RA Wu W.-H., Alami S., Luk E., Wu C.-H., Sen S., Mizuguchi G., Wei D., Wu C.;
RT "Swc2 is a widely conserved H2AZ-binding module essential for ATP-dependent
RT histone exchange.";
RL Nat. Struct. Mol. Biol. 12:1064-1071(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, 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 [13]
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).
CC -!- FUNCTION: Participates in the catalytic exchange of histone H2A for the
CC H2A variant HTZ1, an euchromatin-specific factor, leading to chromatin
CC remodeling and changes in transcription of targeted genes. Indirectly
CC involved in vacuolar protein sorting. {ECO:0000269|PubMed:12134085,
CC ECO:0000269|PubMed:14645854, ECO:0000269|PubMed:14690608,
CC ECO:0000269|PubMed:15045029}.
CC -!- SUBUNIT: Belongs to the SWR1 complex at least composed of ACT1, ARP4,
CC RVB1, RVB2, ARP6, YAF9, VPS71, VPS72, SWC3, SWC4, SWC5, SWR1 and HTZ1.
CC Interacts with HTZ1. {ECO:0000269|PubMed:14645854,
CC ECO:0000269|PubMed:14690608, ECO:0000269|PubMed:15045029,
CC ECO:0000269|PubMed:16299513}.
CC -!- INTERACTION:
CC Q03388; Q12692: HTZ1; NbExp=9; IntAct=EBI-38035, EBI-8080;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 358 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the VPS72/YL1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB64928.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAT93172.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U33050; AAB64928.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY693153; AAT93172.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006938; DAA12318.1; -; Genomic_DNA.
DR PIR; S69652; S69652.
DR RefSeq; NP_010773.4; NM_001180793.3.
DR AlphaFoldDB; Q03388; -.
DR BioGRID; 32537; 557.
DR ComplexPortal; CPX-2122; Swr1 chromatin remodelling complex.
DR DIP; DIP-1008N; -.
DR IntAct; Q03388; 15.
DR MINT; Q03388; -.
DR STRING; 4932.YDR485C; -.
DR iPTMnet; Q03388; -.
DR MaxQB; Q03388; -.
DR PaxDb; Q03388; -.
DR PRIDE; Q03388; -.
DR EnsemblFungi; YDR485C_mRNA; YDR485C; YDR485C.
DR GeneID; 852096; -.
DR KEGG; sce:YDR485C; -.
DR SGD; S000002893; VPS72.
DR VEuPathDB; FungiDB:YDR485C; -.
DR eggNOG; KOG2897; Eukaryota.
DR GeneTree; ENSGT00390000017503; -.
DR HOGENOM; CLU_018782_0_0_1; -.
DR InParanoid; Q03388; -.
DR OMA; CQYFDPK; -.
DR BioCyc; YEAST:G3O-30010-MON; -.
DR PRO; PR:Q03388; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03388; protein.
DR GO; GO:0000785; C:chromatin; IDA:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0000812; C:Swr1 complex; IDA:SGD.
DR GO; GO:0042393; F:histone binding; IPI: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; IPR008895; Vps72/YL1.
DR InterPro; IPR013272; Vps72/YL1_C.
DR PANTHER; PTHR13275; PTHR13275; 1.
DR Pfam; PF05764; YL1; 1.
DR Pfam; PF08265; YL1_C; 1.
DR SMART; SM00993; YL1_C; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Coiled coil; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..795
FT /note="Vacuolar protein sorting-associated protein 72"
FT /id="PRO_0000065909"
FT REGION 1..281
FT /note="Interaction with HTZ1"
FT REGION 40..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 28..63
FT /evidence="ECO:0000255"
FT COILED 121..150
FT /evidence="ECO:0000255"
FT COILED 204..281
FT /evidence="ECO:0000255"
FT COMPBIAS 40..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..91
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..160
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 795 AA; 90580 MW; 6D3053EBB610DB95 CRC64;
MSDEGADKSL DTNTEFIIQT RSRRSNAGNK LQKLLEQELR DIESTKRQIS SYKNGNDDEE
DEIGLLFQED EDDEDFEMMA KDDDDEGEEK EDETQSIRKE PSQASSEQAA DDLMFSSSES
EDSSNENDED AEEKEIRRQE LLSRKKRNKR LQKGPVVIKK QKPKPKSGEA IPRSHHTHEQ
LNAETLLLNT RRTSKRSSVM ENTMKVYEKL SKAEKKRKII QERIRKHKEQ ESQHMLTQEE
RLRIAKETEK LNILSLDKFK EQEVWKKENR LALQKRQKQK FQPNETILQF LSTAWLMTPA
MELEDRKYWQ EQLNKRDKKK KKYPRKPKKN LNLGKQDASD DKKRESEESI KNDGDVNSLG
ENSSSVHNQK RIEETSTNDT VEGESSPDAA VSRVNSDELK PTALPDVTLD AIANKQSTVD
EAPNSQPQKN IITNEQKITN VGEPIQNLHN EEIKDEMVSA LESRENTFEN SSPAAQVVSQ
RDNSATPTPS NSTGTEDTIL ISPDTDIKGE PEPCLKTEGI ENLSHNVPQE TKSNTDVSFL
KQVTFTDHPQ VAIIDTEESP SKKDTANVDE SSAENSLSTQ TYEGPEQLTS RNFVTLYDFP
NAPPNLKDFN TNLFGDRWSY TNGLSATQRP QDMKTVFHSI LPSPPQSSVP SPTVDISLDL
SALANFPSFG EYDKKIVHQI NTEINKDLEI KIKTQPPTGV FLANGIRKKC LITNKECQYF
DPRTGVPYSD VEAYKIIQRI QDPISKEEGR SDIKRDETTN EDSDDQVRFK WFGFKNGGIY
LDLSQRPAKG VPEGF
