YP191_YEAST
ID YP191_YEAST Reviewed; 360 AA.
AC Q08930; D6W3H7;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase MIY1 {ECO:0000303|PubMed:27292798};
DE EC=3.4.19.12 {ECO:0000269|PubMed:27292798};
DE AltName: Full=Deubiquitinating enzyme MIY1 {ECO:0000303|PubMed:27292798};
GN OrderedLocusNames=YPL191C;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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, CATALYTIC ACTIVITY, AND GENE FAMILY.
RX PubMed=27292798; DOI=10.1016/j.molcel.2016.05.009;
RA Abdul Rehman S.A., Kristariyanto Y.A., Choi S.Y., Nkosi P.J., Weidlich S.,
RA Labib K., Hofmann K., Kulathu Y.;
RT "MINDY-1 is a member of an evolutionarily conserved and structurally
RT distinct new family of deubiquitinating enzymes.";
RL Mol. Cell 63:146-155(2016).
CC -!- FUNCTION: Hydrolase that can specifically remove 'Lys-48'-linked
CC conjugated ubiquitin from proteins. Has endodeubiquitinase activity.
CC {ECO:0000269|PubMed:27292798}.
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; Evidence={ECO:0000269|PubMed:27292798};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2050 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MINDY deubiquitinase family. FAM63
CC subfamily. {ECO:0000305}.
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; Z73547; CAA97904.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11243.1; -; Genomic_DNA.
DR PIR; S65210; S65210.
DR RefSeq; NP_015133.1; NM_001184005.1.
DR AlphaFoldDB; Q08930; -.
DR SMR; Q08930; -.
DR BioGRID; 35992; 68.
DR DIP; DIP-2779N; -.
DR IntAct; Q08930; 1.
DR MINT; Q08930; -.
DR STRING; 4932.YPL191C; -.
DR iPTMnet; Q08930; -.
DR PaxDb; Q08930; -.
DR PRIDE; Q08930; -.
DR EnsemblFungi; YPL191C_mRNA; YPL191C; YPL191C.
DR GeneID; 855910; -.
DR KEGG; sce:YPL191C; -.
DR SGD; S000006112; YPL191C.
DR VEuPathDB; FungiDB:YPL191C; -.
DR eggNOG; KOG2427; Eukaryota.
DR GeneTree; ENSGT00390000016607; -.
DR HOGENOM; CLU_022566_0_0_1; -.
DR InParanoid; Q08930; -.
DR OMA; NHEVPLG; -.
DR BioCyc; YEAST:G3O-34084-MON; -.
DR PRO; PR:Q08930; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q08930; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0016807; F:cysteine-type carboxypeptidase activity; IDA:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:1990380; F:Lys48-specific deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; IDA:SGD.
DR InterPro; IPR007518; MINDY.
DR InterPro; IPR033979; MINDY_domain.
DR PANTHER; PTHR18063; PTHR18063; 1.
DR Pfam; PF04424; MINDY_DUB; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..360
FT /note="Ubiquitin carboxyl-terminal hydrolase MIY1"
FT /id="PRO_0000238658"
FT REGION 317..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 28
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT ACT_SITE 216
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT SITE 296
FT /note="Ubiquitin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT SITE 299..300
FT /note="Ubiquitin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT SITE 303
FT /note="Ubiquitin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q8N5J2"
SQ SEQUENCE 360 AA; 41032 MW; 6C345663C0B69491 CRC64;
MDLSFTTKSV KINGQNHRIL LQNENGPCAL LALANILILS PDHTRFSNEL IRLVNKGSQI
SLKELIEVLA DIALQVTDKP STDISELLSL LPRLHEGLNI NPEFNGSFEN TKEMSIFRLF
NVDVVHGWVI NSFINENIDE KLSHYSYESA QRILTQAADI NCGISQDENS DEVLRDAMHL
GLFLNESPTQ LTAFGLLRLR EKLLHNKFSI LFRNDHFSTL FKYEDRLYTL VTDFGYKNCK
DIVWQSLDSV DGSCDAFFAG NFSAAEVNGQ QLSTDIERDF GTGNLLLEEI QQIENDKELA
KQLQEQEQER VTKFEAKRKI HSHKKNSEIH APVKKDKFKR RSSLLNAKAS EKEKSECVVM
