UBP7_YEAST
ID UBP7_YEAST Reviewed; 1071 AA.
AC P40453; D6VVD1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 7;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 7;
DE AltName: Full=Ubiquitin thioesterase 7;
DE AltName: Full=Ubiquitin-specific-processing protease 7;
GN Name=UBP7; OrderedLocusNames=YIL156W;
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=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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 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 [4]
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 [5]
RP FUNCTION, AND INTERACTION WITH HSE1.
RX PubMed=17079730; DOI=10.1091/mbc.e06-06-0557;
RA Ren J., Kee Y., Huibregtse J.M., Piper R.C.;
RT "Hse1, a component of the yeast Hrs-STAM ubiquitin-sorting complex,
RT associates with ubiquitin peptidases and a ligase to control sorting
RT efficiency into multivesicular bodies.";
RL Mol. Biol. Cell 18:324-335(2007).
RN [6]
RP IDENTIFICATION BY 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 [7]
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: Involved in the sorting of ubiquitinated cargo proteins at
CC the multivesicular body (MVB). {ECO:0000269|PubMed:17079730}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12;
CC -!- INTERACTION:
CC P40453; P38822: BZZ1; NbExp=3; IntAct=EBI-19857, EBI-3889;
CC P40453; Q05080: HOF1; NbExp=2; IntAct=EBI-19857, EBI-5412;
CC P40453; P38753: HSE1; NbExp=4; IntAct=EBI-19857, EBI-1382;
CC P40453; P43603: LSB3; NbExp=2; IntAct=EBI-19857, EBI-22980;
CC P40453; P36006: MYO3; NbExp=3; IntAct=EBI-19857, EBI-11670;
CC P40453; Q04439: MYO5; NbExp=4; IntAct=EBI-19857, EBI-11687;
CC P40453; P80667: PEX13; NbExp=2; IntAct=EBI-19857, EBI-13206;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 606 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; Z38059; CAA86122.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08397.1; -; Genomic_DNA.
DR PIR; S48378; S48378.
DR RefSeq; NP_012110.1; NM_001179504.1.
DR AlphaFoldDB; P40453; -.
DR SMR; P40453; -.
DR BioGRID; 34836; 83.
DR DIP; DIP-6272N; -.
DR IntAct; P40453; 14.
DR MINT; P40453; -.
DR STRING; 4932.YIL156W; -.
DR MEROPS; C19.101; -.
DR iPTMnet; P40453; -.
DR MaxQB; P40453; -.
DR PaxDb; P40453; -.
DR PRIDE; P40453; -.
DR EnsemblFungi; YIL156W_mRNA; YIL156W; YIL156W.
DR GeneID; 854650; -.
DR KEGG; sce:YIL156W; -.
DR SGD; S000001418; UBP7.
DR VEuPathDB; FungiDB:YIL156W; -.
DR eggNOG; KOG1868; Eukaryota.
DR GeneTree; ENSGT00940000172369; -.
DR HOGENOM; CLU_004122_0_0_1; -.
DR InParanoid; P40453; -.
DR OMA; NAWDCPK; -.
DR BioCyc; YEAST:G3O-31404-MON; -.
DR Reactome; R-SCE-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR PRO; PR:P40453; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40453; protein.
DR GO; GO:0005737; C:cytoplasm; IC:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:SGD.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; IDA:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..1071
FT /note="Ubiquitin carboxyl-terminal hydrolase 7"
FT /id="PRO_0000080592"
FT DOMAIN 609..1069
FT /note="USP"
FT REGION 467..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..532
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 618
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 1014
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 1071 AA; 123134 MW; 82683A01063CEC74 CRC64;
MLDDDKGTAM HPHITPFTPE YSNELLRRVQ DLYHEDIKHY YPQLKLEKLL DLLEHTEYLF
ELYLDSIHHD RPNDALTAFI IGCYYVFLII PQSLQFQTRN KSYSIYTDLK KMYENEMNMT
NVVLMVKKEI GVVLDESVKH GAGIEHRITK KRAFSVPADD LSGQVASLSL DTAAPQDHGL
KGTFTEDDAE QSSPVWTAPN LEPNDQLKLA LLPEVIPTPA FREPERKTSV PVRPSVLLED
VPSIYHEDDT SFASLNPPFR EITADRSVTH RKDSYHSVYM VDSGNLKEDN DDLFNVENDG
FIQSLDILQK QSIITAPELF SILSNRVERE KVLLIDLRIP QRSAINHIVA PNLVNVDPNL
LWDKQTNTPI YKDDILEHLL KENENFINRN KFDYIVYYTD VKTFMTINFD YAFIFFYLML
TSQKTPLTTV PTTLLGGYEK WKKTLHSYAQ EYHISIEDYL YRPYSQKARL QQEQQQQQQQ
PDSQDSFSAK ESSTKVPEPP SWKPPDLPIR LRKRPPPPPP VSMPTTPEIP PPLPPKIMVH
SQVSSISRKP PIPAKQHVKK EQLNSNEIIQ RKRQHQHQHY DQQILQPQRA YNIPTIERSP
NVYVSLSITG LRNLGNTCYI NSMIQCLFAA KTFRTLFISS KYKSYLQPIR SNGSHYSPKL
SNSLSMLFNK MYLNGGCSVV PTGFLKVINQ LRPDLKIPDD QQDTQEFLMI LLDRLHDELS
DQQHVANDYP NLLLYNADAL KVSNNEYKHW FDKNVIGNGI SPIDDIFQGQ MENSLQCKRC
GYTTFNYSTF YVLSLAIPRR SMKLSKLGRS TEKRVKLEDC INMFTSDEVL SGENAWDCPR
CGPTASVSTS VSALENEPSI VKSKKKKSRF FTLHTGTKRR HLDFFGDGIT EGHNSNNNNT
TIFERERSRS PFRMLGGSGK RSSSSTPFST GGNDSNNSSD YKNKKLTTVK TINFVTLPKI
LVIHLSRFYY DLTKKNNTVV TYPLILNIIL KNNDTMKYKL FGVVNHTGTL ISGHYTSLVN
KDLEHNVNIG RSKWYYFDDE VVKADRKHGS DKNLKISSSD VYVLFYERVY D
