MU105_SCHPO
ID MU105_SCHPO Reviewed; 244 AA.
AC O13979;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase mug105;
DE EC=3.4.19.12 {ECO:0000269|PubMed:29476094};
DE AltName: Full=Lys-48-selective deubiquitinase mug105;
DE Short=DUB;
DE AltName: Full=Meiotically up-regulated gene 105 protein;
GN Name=mug105; ORFNames=SPAC25H1.04;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION IN MEIOSIS.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=22146723; DOI=10.1271/bbb.110558;
RA Ikebe C., Konishi M., Hirata D., Matsusaka T., Toda T.;
RT "Systematic localization study on novel proteins encoded by meiotically up-
RT regulated ORFs in fission yeast.";
RL Biosci. Biotechnol. Biochem. 75:2364-2370(2011).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF CYS-42.
RX PubMed=29576528; DOI=10.1016/j.molcel.2018.02.024;
RA Haahr P., Borgermann N., Guo X., Typas D., Achuthankutty D., Hoffmann S.,
RA Shearer R., Sixma T.K., Mailand N.;
RT "ZUFSP deubiquitylates K63-linked polyubiquitin chains to promote genome
RT stability.";
RL Mol. Cell 70:165-174(2018).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=29476094; DOI=10.1038/s41467-018-03148-5;
RA Hermanns T., Pichlo C., Woiwode I., Klopffleisch K., Witting K.F., Ovaa H.,
RA Baumann U., Hofmann K.;
RT "A family of unconventional deubiquitinases with modular chain specificity
RT determinants.";
RL Nat. Commun. 9:799-799(2018).
CC -!- FUNCTION: Deubiquitinase with endodeubiquitinase activity that
CC preferentially cleaves 'Lys-48'-linked polyubiquitin chains
CC (PubMed:29576528, PubMed:29476094). Shows only weak activity against
CC 'Lys-63' and 'Lys-11'-linked chains (PubMed:29476094). Has a role in
CC meiosis (PubMed:16303567). {ECO:0000269|PubMed:16303567,
CC ECO:0000269|PubMed:29476094, ECO:0000269|PubMed:29576528}.
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:29476094};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12.2 uM for Arg-Leu-Arg-Gly-Gly-AMC {ECO:0000269|PubMed:29476094};
CC Note=kcat is 7.2 sec(-1) with Arg-Leu-Arg-Gly-Gly-AMC as substrate.
CC {ECO:0000269|PubMed:29476094};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22146723}.
CC -!- SIMILARITY: Belongs to the peptidase C78 family. ZUFSP subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB11605.1; -; Genomic_DNA.
DR PIR; T38384; T38384.
DR RefSeq; NP_593808.1; NM_001019237.2.
DR PDB; 7OIY; X-ray; 2.05 A; A/B=1-244.
DR PDBsum; 7OIY; -.
DR AlphaFoldDB; O13979; -.
DR SMR; O13979; -.
DR BioGRID; 279170; 1.
DR STRING; 4896.SPAC25H1.04.1; -.
DR MEROPS; C78.004; -.
DR MaxQB; O13979; -.
DR PaxDb; O13979; -.
DR PRIDE; O13979; -.
DR EnsemblFungi; SPAC25H1.04.1; SPAC25H1.04.1:pep; SPAC25H1.04.
DR GeneID; 2542717; -.
DR KEGG; spo:SPAC25H1.04; -.
DR PomBase; SPAC25H1.04; mug105.
DR VEuPathDB; FungiDB:SPAC25H1.04; -.
DR eggNOG; KOG4696; Eukaryota.
DR HOGENOM; CLU_099553_0_0_1; -.
DR InParanoid; O13979; -.
DR OMA; QFQGHSI; -.
DR PhylomeDB; O13979; -.
DR PRO; PR:O13979; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:1990380; F:Lys48-specific deubiquitinase activity; IDA:PomBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR InterPro; IPR012462; Peptidase_C78_UfSP1/2.
DR Pfam; PF07910; Peptidase_C78; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Meiosis; Reference proteome.
FT CHAIN 1..244
FT /note="Ubiquitin carboxyl-terminal hydrolase mug105"
FT /id="PRO_0000278504"
FT ACT_SITE 42
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
FT ACT_SITE 183
FT /evidence="ECO:0000250|UniProtKB:Q99K23"
FT SITE 161
FT /note="Involved in the stabilization of negative charge on
FT the oxyanion by the formation of the oxyanion hole"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
FT MUTAGEN 42
FT /note="C->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:29576528"
SQ SEQUENCE 244 AA; 28084 MW; DE1A62DBE55BC1C7 CRC64;
MSKCLQQLKR QLQHFGIDGC SLADGDIDYF FTVTGIDRGW GCGWRNIQML ISWLQYTNPN
WFKRNFSSGN YEINSLQSLL LSAWMKGIDA EGYAQLGDNL HGKWIGATEV YSLFTGLFVN
VALVDFDFRS EASASNALFL YVKKHFESSN DTSNVSPCYL QFQGHSIIII GFCSSLETLV
VLDPDRYQSV QKKFVNIADF NHCYMRKKRS LKFSQFQLVH FKQNIFLNDF SSKLEVRSTR
ISDF
