VPS71_YEAST
ID VPS71_YEAST Reviewed; 280 AA.
AC Q03433; D6VZD4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Vacuolar protein sorting-associated protein 71;
DE AltName: Full=SWR complex protein 6;
GN Name=VPS71; Synonyms=SWC6; OrderedLocusNames=YML041C; ORFNames=YM8054.02C;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 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 [4]
RP FUNCTION, AND INTERACTION WITH ACT1; ARP4; RVB1; RVB2; ARP6; YAF9; VPS72;
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 [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 FUNCTION, AND INTERACTION WITH ACT1; ARP4; RVB1; RVB2; ARP6; YAF9; VPS72;
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 [7]
RP FUNCTION, AND INTERACTION WITH ACT1; ARP4; RVB1; RVB2; ARP6; YAF9; VPS72;
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).
CC -!- FUNCTION: Participates in the catalytic exchange of histone H2A for the
CC H2A variant HZT1, 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 -!- INTERACTION:
CC Q03433; Q12509: ARP6; NbExp=3; IntAct=EBI-27814, EBI-2957;
CC Q03433; P35817: BDF1; NbExp=2; IntAct=EBI-27814, EBI-3493;
CC Q03433; Q12692: HTZ1; NbExp=6; IntAct=EBI-27814, EBI-8080;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z48430; CAA88328.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09858.1; -; Genomic_DNA.
DR PIR; S52479; S52479.
DR RefSeq; NP_013671.1; NM_001182399.1.
DR PDB; 6GEJ; EM; 3.60 A; S=1-280.
DR PDB; 6GEN; EM; 3.60 A; S=1-280.
DR PDBsum; 6GEJ; -.
DR PDBsum; 6GEN; -.
DR AlphaFoldDB; Q03433; -.
DR SMR; Q03433; -.
DR BioGRID; 35128; 721.
DR ComplexPortal; CPX-2122; Swr1 chromatin remodelling complex.
DR DIP; DIP-4074N; -.
DR IntAct; Q03433; 17.
DR MINT; Q03433; -.
DR STRING; 4932.YML041C; -.
DR MaxQB; Q03433; -.
DR PaxDb; Q03433; -.
DR PRIDE; Q03433; -.
DR EnsemblFungi; YML041C_mRNA; YML041C; YML041C.
DR GeneID; 854966; -.
DR KEGG; sce:YML041C; -.
DR SGD; S000004505; VPS71.
DR VEuPathDB; FungiDB:YML041C; -.
DR eggNOG; KOG3362; Eukaryota.
DR GeneTree; ENSGT00390000018426; -.
DR HOGENOM; CLU_099156_0_0_1; -.
DR InParanoid; Q03433; -.
DR OMA; RFMELDT; -.
DR BioCyc; YEAST:G3O-32640-MON; -.
DR PRO; PR:Q03433; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03433; protein.
DR GO; GO:0000785; C:chromatin; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0000812; C:Swr1 complex; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0006623; P:protein targeting to vacuole; HMP:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR InterPro; IPR039723; Vps71/ZNHIT1.
DR InterPro; IPR007529; Znf_HIT.
DR PANTHER; PTHR13093; PTHR13093; 1.
DR PROSITE; PS51083; ZF_HIT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Metal-binding; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..280
FT /note="Vacuolar protein sorting-associated protein 71"
FT /id="PRO_0000173557"
FT ZN_FING 244..277
FT /note="HIT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT REGION 64..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
SQ SEQUENCE 280 AA; 32021 MW; D95B57C72ACB648A CRC64;
MKALVEEIDK KTYNPDIYFT SLDPQARRYT SKKINKQGTI STSRPVKRIN YSLADLEARL
YTSRSEGDGN SISRQDDRNS KNSHSFEERY TQQEILQSDR RFMELNTENF SDLPNVPTLL
SDLTGVPRDR IESTTKPISQ TSDGLSALMG GSSFVKEHSK YGHGWVLKPE TLREIQLSYK
STKLPKPKRK NTNRIVALKK VLSSKRNLHS FLDSALLNLM DKNVIYHNVY NKRYFKVLPL
ITTCSICGGY DSISSCVNCG NKICSVSCFK LHNETRCRNR
