UBP3_SCHPO
ID UBP3_SCHPO Reviewed; 512 AA.
AC O94269;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Probable ubiquitin carboxyl-terminal hydrolase 3;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 3;
DE AltName: Full=Ubiquitin thioesterase 3;
DE AltName: Full=Ubiquitin-specific-processing protease 3;
GN Name=ubp3; ORFNames=SPBP8B7.21;
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).
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 -!- SIMILARITY: Belongs to the peptidase C19 family. {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; CU329671; CAA21806.1; -; Genomic_DNA.
DR PIR; T40815; T40815.
DR RefSeq; NP_596528.1; NM_001022449.2.
DR AlphaFoldDB; O94269; -.
DR SMR; O94269; -.
DR BioGRID; 277889; 116.
DR STRING; 4896.SPBP8B7.21.1; -.
DR MEROPS; C19.A57; -.
DR iPTMnet; O94269; -.
DR MaxQB; O94269; -.
DR PaxDb; O94269; -.
DR PRIDE; O94269; -.
DR EnsemblFungi; SPBP8B7.21.1; SPBP8B7.21.1:pep; SPBP8B7.21.
DR GeneID; 2541378; -.
DR KEGG; spo:SPBP8B7.21; -.
DR PomBase; SPBP8B7.21; ubp3.
DR VEuPathDB; FungiDB:SPBP8B7.21; -.
DR eggNOG; KOG1871; Eukaryota.
DR HOGENOM; CLU_008279_7_2_1; -.
DR InParanoid; O94269; -.
DR OMA; PSGKWLR; -.
DR PhylomeDB; O94269; -.
DR PRO; PR:O94269; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0010494; C:cytoplasmic stress granule; EXP:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IGI:PomBase.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; HDA:PomBase.
DR GO; GO:1905538; F:polysome binding; EXP:PomBase.
DR GO; GO:0071629; P:cytoplasm protein quality control by the ubiquitin-proteasome system; IGI:PomBase.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0060628; P:regulation of ER to Golgi vesicle-mediated transport; ISO:PomBase.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 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 3: Inferred from homology;
KW Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..512
FT /note="Probable ubiquitin carboxyl-terminal hydrolase 3"
FT /id="PRO_0000080604"
FT DOMAIN 133..511
FT /note="USP"
FT REGION 64..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 142
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 453
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 512 AA; 58081 MW; 1F97DA2C7720695D CRC64;
MRDLTSATDS ASLESDSSRN QFIINSLLPW YSCSEHEFPH RKARKRRSPK NLDWSVSVQM
PLVTSKTKES EKSPKSWSAI AKKHVQGDSP VKKSHSVPVP SDRSEKKSFN SSLGELIETY
SPSLDAPRPI QPRGFINTGN ICFMNSILQA LMYCVPFYNL LKQINRMVPY NFERTTPLIE
SLTMLSRDFR EYSEKFDLQG DSILPEVVYS ATKGNPRFEM LQTGEQEDAE EFLNLFLDEL
HEEFVRERRH YLLKNDERNP KSDIKISNGI KSGLDSFDDQ SSVEASGWTE VGKNKKPVIA
RSATVERSPI SQIFGGQLRS TLRVPSARDS VLLEPFQPLQ LDIQAEDIHS VIDALEHMTA
PEILPEWHSS KGNVTATKQM YIESLPPVLI LHLKRFFYEA SGGTQKNYKP IAYPARLSIP
QNVFSPSVRG SIHPEYDLNA VVYHHGTSAS GGHYTVDVQQ LDKSGWFRID DTHIHRVPIH
DVENSELSAD PSLSKLGHGD RVAYLLFYTR RS
