WSS1_YEAST
ID WSS1_YEAST Reviewed; 269 AA.
AC P38838; D3DL83;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=DNA-dependent metalloprotease WSS1;
DE EC=3.4.24.- {ECO:0000269|PubMed:24998930};
DE AltName: Full=DNA damage response protein WSS1;
DE AltName: Full=SUMO-dependent isopeptidase WSS1;
DE AltName: Full=Weak suppressor of SMT3 protein 1;
GN Name=WSS1; OrderedLocusNames=YHR134W;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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=11606525; DOI=10.1093/genetics/159.2.453;
RA Biggins S., Bhalla N., Chang A., Smith D.L., Murray A.W.;
RT "Genes involved in sister chromatid separation and segregation in the
RT budding yeast Saccharomyces cerevisiae.";
RL Genetics 159:453-470(2001).
RN [4]
RP FUNCTION.
RX PubMed=11606770; DOI=10.1073/pnas.231366398;
RA Birrell G.W., Giaever G., Chu A.M., Davis R.W., Brown J.M.;
RT "A genome-wide screen in Saccharomyces cerevisiae for genes affecting UV
RT radiation sensitivity.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12608-12613(2001).
RN [5]
RP FUNCTION, AND INTERACTION WITH PSY2 AND TOF1.
RX PubMed=15598824; DOI=10.1093/nar/gkh994;
RA O'Neill B.M., Hanway D., Winzeler E.A., Romesberg F.E.;
RT "Coordinated functions of WSS1, PSY2 and TOF1 in the DNA damage response.";
RL Nucleic Acids Res. 32:6519-6530(2004).
RN [6]
RP FUNCTION.
RX PubMed=18085829; DOI=10.1371/journal.pgen.0030228;
RA Alvaro D., Lisby M., Rothstein R.;
RT "Genome-wide analysis of Rad52 foci reveals diverse mechanisms impacting
RT recombination.";
RL PLoS Genet. 3:E228-E228(2007).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=18336552; DOI=10.1111/j.1574-6968.2008.01113.x;
RA van Heusden G.P.H., Steensma H.Y.;
RT "The Saccharomyces cerevisiae Wss1 protein is only present in mother
RT cells.";
RL FEMS Microbiol. Lett. 282:100-104(2008).
RN [8]
RP FUNCTION, MUTAGENESIS OF HIS-115 AND HIS-119, AND INTERACTION WITH SMT3.
RX PubMed=20516210; DOI=10.1128/mcb.01649-09;
RA Mullen J.R., Chen C.F., Brill S.J.;
RT "Wss1 is a SUMO-dependent isopeptidase that interacts genetically with the
RT Slx5-Slx8 SUMO-targeted ubiquitin ligase.";
RL Mol. Cell. Biol. 30:3737-3748(2010).
RN [9]
RP FUNCTION, ACTIVITY REGULATION, MUTAGENESIS OF GLU-116, INTERACTION WITH
RP CDC48 AND SMT3, DNA-BINDING, DOMAIN, AND DISRUPTION PHENOTYPE.
RX PubMed=24998930; DOI=10.1016/j.cell.2014.04.053;
RA Stingele J., Schwarz M.S., Bloemeke N., Wolf P.G., Jentsch S.;
RT "A DNA-dependent protease involved in DNA-protein crosslink repair.";
RL Cell 158:327-338(2014).
CC -!- FUNCTION: Metalloendopeptidase that acts selectively on DNA-binding
CC proteins. DNA is needed to bring the protease and substrates together
CC to enable proteolysis. Involved in the repair of toxic DNA-protein
CC cross-links (DPCs) such as covalently trapped topoisomerase 1 (TOP1)
CC adducts on DNA lesions or DPCs induced by reactive compounds such as
CC formaldehyde. Involved in DNA damage response and processing of stalled
CC or collapsed replication forks by removing the covalently trapped TOP1
CC from chromatin. DPC proteolysis enables the repair of the lesions via
CC downstream DNA repair pathways. May be recruited to DPCs via the
CC SUMOylation of substrate proteins at damaged DNA sites.
CC {ECO:0000269|PubMed:11606525, ECO:0000269|PubMed:11606770,
CC ECO:0000269|PubMed:15598824, ECO:0000269|PubMed:18085829,
CC ECO:0000269|PubMed:20516210, ECO:0000269|PubMed:24998930}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9H040};
CC -!- ACTIVITY REGULATION: Inactivated by EDTA.
CC {ECO:0000269|PubMed:24998930}.
CC -!- SUBUNIT: Binds to DNA. Interacts with CDC48 and SMT3. Interacts with
CC PSY2 and TOF1. {ECO:0000269|PubMed:15598824,
CC ECO:0000269|PubMed:20516210, ECO:0000269|PubMed:24998930}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18336552}.
CC Note=Present in a single sharp spot near the nuclear membrane, distinct
CC from the spindle pole bodies and nucleolus. In dividing cells, the spot
CC is exclusively present in the mother cell.
CC -!- DOMAIN: The SHP box and the VCP-interaction motif (VIM) are important
CC both together for binding to CDC48. The 2 SUMO interaction motifs (SIM)
CC are each important for binding to SMT3(SUMO).
CC {ECO:0000269|PubMed:24998930}.
CC -!- DISRUPTION PHENOTYPE: Accumulates DPCs and exhibits gross chromosomal
CC rearrangements. {ECO:0000269|PubMed:24998930}.
CC -!- SIMILARITY: Belongs to the peptidase M3 family. WSS1-like
CC metalloprotease (WLM) subfamily. {ECO:0000305}.
CC -!- CAUTION: Was initially reported to be a SUMO-dependent isopeptidase
CC (PubMed:20516210), but this activity could not be confirmed
CC (PubMed:24998930). {ECO:0000305|PubMed:20516210,
CC ECO:0000305|PubMed:24998930}.
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DR EMBL; U10398; AAB68404.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06827.1; -; Genomic_DNA.
DR PIR; S48978; S48978.
DR RefSeq; NP_012002.1; NM_001179264.1.
DR AlphaFoldDB; P38838; -.
DR SMR; P38838; -.
DR BioGRID; 36567; 217.
DR DIP; DIP-1600N; -.
DR IntAct; P38838; 4.
DR MINT; P38838; -.
DR STRING; 4932.YHR134W; -.
DR MEROPS; M80.001; -.
DR PaxDb; P38838; -.
DR PRIDE; P38838; -.
DR TopDownProteomics; P38838; -.
DR EnsemblFungi; YHR134W_mRNA; YHR134W; YHR134W.
DR GeneID; 856536; -.
DR KEGG; sce:YHR134W; -.
DR SGD; S000001176; WSS1.
DR VEuPathDB; FungiDB:YHR134W; -.
DR eggNOG; KOG4842; Eukaryota.
DR HOGENOM; CLU_023057_3_0_1; -.
DR InParanoid; P38838; -.
DR OMA; KWCHSEN; -.
DR BioCyc; YEAST:G3O-31172-MON; -.
DR PRO; PR:P38838; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38838; protein.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:SGD.
DR GO; GO:0008237; F:metallopeptidase activity; IDA:SGD.
DR GO; GO:0032183; F:SUMO binding; IDA:SGD.
DR GO; GO:0061665; F:SUMO ligase activity; IDA:SGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:SGD.
DR GO; GO:0036205; P:histone catabolic process; IMP:SGD.
DR GO; GO:1990466; P:protein autosumoylation; IDA:SGD.
DR GO; GO:0016925; P:protein sumoylation; IDA:SGD.
DR GO; GO:0106300; P:protein-DNA covalent cross-linking repair; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IMP:SGD.
DR GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IMP:SGD.
DR GO; GO:0010224; P:response to UV-B; IMP:SGD.
DR GO; GO:0010225; P:response to UV-C; IMP:SGD.
DR GO; GO:0019985; P:translesion synthesis; IDA:SGD.
DR InterPro; IPR013536; WLM_dom.
DR Pfam; PF08325; WLM; 1.
DR PROSITE; PS51397; WLM; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW DNA damage; Hydrolase; Metal-binding; Metalloprotease; Nucleus; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..269
FT /note="DNA-dependent metalloprotease WSS1"
FT /id="PRO_0000202919"
FT DOMAIN 20..221
FT /note="WLM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00730"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..208
FT /note="Required and sufficient for binding to DNA"
FT MOTIF 152..160
FT /note="SHP box"
FT MOTIF 209..219
FT /note="VCP-interaction motif (VIM)"
FT /evidence="ECO:0000269|PubMed:24998930"
FT MOTIF 247..254
FT /note="SUMO interaction motif 1 (SIM)"
FT /evidence="ECO:0000269|PubMed:24998930"
FT MOTIF 266..269
FT /note="SUMO interaction motif 2 (SIM)"
FT /evidence="ECO:0000269|PubMed:24998930"
FT ACT_SITE 116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT MUTAGEN 115
FT /note="H->A: In wss1-pd; loss of function; when associated
FT with A-119."
FT /evidence="ECO:0000269|PubMed:20516210"
FT MUTAGEN 116
FT /note="E->Q: Loss of function."
FT /evidence="ECO:0000269|PubMed:24998930"
FT MUTAGEN 119
FT /note="H->A: In wss1-pd; loss of function; when associated
FT with A-115."
FT /evidence="ECO:0000269|PubMed:20516210"
SQ SEQUENCE 269 AA; 30627 MW; 09DC0854537F9D02 CRC64;
MKTEGIKSPS AKYHDMAGSQ RIPHKNPHIQ KVAVLQSKPN KEDALNLIKE IAHKVSYLMK
ENHFKVTNLV EFYPRDQRLL GMNVNHGSKI MLRLRCSTDE FQFLPMECIM GTMLHELTHN
LFGPHDKKFY NKLDELIGRQ WVIEQRGLYD TFLGNGQRLG GRANLRSNRY PMTGISTNTG
IVRKRGKGVK LGSLHPEGIS SIDRGNSPRE LAAFAAERRY RDDRWCGETK NNKDQIISDN
ISSSLEVVIL DDDDEVLPGD TLIEVIDLT
