ID   UBP5_YEAST              Reviewed;         805 AA.
AC   P39944; D3DM51;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 180.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 5;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 5;
DE   AltName: Full=Ubiquitin thioesterase 5;
DE   AltName: Full=Ubiquitin-specific-processing protease 5;
GN   Name=UBP5; OrderedLocusNames=YER144C;
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].
RX   PubMed=7871889; DOI=10.1002/yea.320101114;
RA   Xiao W., Fontanie T., Tang M.;
RT   "UBP5 encodes a putative yeast ubiquitin-specific protease that is related
RT   to the human Tre-2 oncogene product.";
RL   Yeast 10:1497-1502(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA   Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA   Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA   Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(1997).
RN   [3]
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   [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).
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   -!- MISCELLANEOUS: Present with 300 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; U10082; AAC48928.1; -; Genomic_DNA.
DR   EMBL; U18917; AAB64671.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07805.1; -; Genomic_DNA.
DR   PIR; S50277; S50277.
DR   RefSeq; NP_011071.3; NM_001179034.3.
DR   AlphaFoldDB; P39944; -.
DR   SMR; P39944; -.
DR   BioGRID; 36893; 87.
DR   DIP; DIP-1716N; -.
DR   IntAct; P39944; 7.
DR   MINT; P39944; -.
DR   STRING; 4932.YER144C; -.
DR   MEROPS; C19.006; -.
DR   GlyGen; P39944; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; P39944; -.
DR   MaxQB; P39944; -.
DR   PaxDb; 4932-YER144C; -.
DR   PeptideAtlas; P39944; -.
DR   EnsemblFungi; YER144C_mRNA; YER144C; YER144C.
DR   GeneID; 856887; -.
DR   KEGG; sce:YER144C; -.
DR   AGR; SGD:S000000946; -.
DR   SGD; S000000946; UBP5.
DR   VEuPathDB; FungiDB:YER144C; -.
DR   eggNOG; KOG1868; Eukaryota.
DR   GeneTree; ENSGT00940000173629; -.
DR   HOGENOM; CLU_005922_1_0_1; -.
DR   InParanoid; P39944; -.
DR   OMA; PFVHTYE; -.
DR   OrthoDB; 227085at2759; -.
DR   BioCyc; YEAST:G3O-30305-MONOMER; -.
DR   BioGRID-ORCS; 856887; 5 hits in 10 CRISPR screens.
DR   PRO; PR:P39944; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P39944; Protein.
DR   GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR   GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; TAS:SGD.
DR   GO; GO:0016579; P:protein deubiquitination; TAS:SGD.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02674; Peptidase_C19R; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF95; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 4-RELATED; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR   PROSITE; PS50206; RHODANESE_3; 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   Hydrolase; Protease; Reference proteome; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN           1..805
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 5"
FT                   /id="PRO_0000080590"
FT   DOMAIN          159..283
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   DOMAIN          446..804
FT                   /note="USP"
FT   REGION          359..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        455
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   ACT_SITE        761
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
SQ   SEQUENCE   805 AA;  92261 MW;  884054A66370DFF7 CRC64;
     MGSEQALSEV VESAKERFGR LRHLVQKFLD DDDVPQECLP LLQECAEIWS SYVDACQDIT
     MQAPKEDANR LSKGFLRLNE TAFLYYMIVY TLLEDTLPRL KEFSSNKDQN VRNLYGERIQ
     LLHNDPNIER IRNVIENYPK FIQLQTIEPG KLSSMLHFHG DALLLIDVRP RSEFVRAHIK
     CKNIICIDPA SFKDSFTDQQ IESVSLITSP HSDITFFSNR DKFKFIILYT DTQLHNNFQQ
     RQTRILAKIL SQNSVIKPLS GTKILILENG FSNWVKLGGA YQSSVSETAH LTSSSSTPAF
     GSPQVPTGLF NQKSLSPNKD KSMPMVSMNT QPLLTTVQRP QLPLYYSDLP IIPQPSPNRN
     SPTVQKFSPH PPTTLSKLNT PSTIQNKANT VERISPDIRA AQAHAYLPPA SNVFSPRIPP
     LPQQNLSSSR QTILNNSQVL DLDLIVGLEN IGNCCYMNCI LQCLVGTHDL VRMFLDNTYL
     NFINFDSSRG SKGLLAKNFA ILVNNMHRHG AFTPPNVRTI PVQTIQFKKI CGHINPMYSD
     SMQQDCQEFC QFLLDGLHED LNQNGSKKHL KQLSDEEERM REKMSIRKAS ALEWERFLLT
     DFSAIIDLFQ GQYASRLQCQ VCEHTSTTYQ TFSVLSVPVP RVKTCNILDC FREFTKCERL
     GVDEQWSCPK CLKKQPSTKQ LKITRLPKKL IINLKRFDNQ MNKNNVFVQY PYSLDLTPYW
     ARDFNHEAIV NEDIPTRGQV PPFRYRLYGV ACHSGSLYGG HYTSYVYKGP KKGWYFFDDS
     LYRPITFSTE FITPSAYVLF YERIF
//