UBP4_SCHPO
ID UBP4_SCHPO Reviewed; 593 AA.
AC O60139;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Probable ubiquitin carboxyl-terminal hydrolase 4;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 4;
DE AltName: Full=Ubiquitin thioesterase 4;
DE AltName: Full=Ubiquitin-specific-processing protease 4;
GN Name=ubp4; ORFNames=SPBC18H10.08c;
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338 AND SER-343, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [4]
RP INTERACTION WITH SFP47, AND SUBCELLULAR LOCATION.
RX PubMed=20838651; DOI=10.1371/journal.pbio.1000471;
RA Kouranti I., McLean J.R., Feoktistova A., Liang P., Johnson A.E.,
RA Roberts-Galbraith R.H., Gould K.L.;
RT "A global census of fission yeast deubiquitinating enzyme localization and
RT interaction networks reveals distinct compartmentalization profiles and
RT overlapping functions in endocytosis and polarity.";
RL PLoS Biol. 8:708-716(2010).
RN [5]
RP REVISION OF GENE MODEL.
RX PubMed=21270388; DOI=10.1534/genetics.110.123497;
RA Bitton D.A., Wood V., Scutt P.J., Grallert A., Yates T., Smith D.L.,
RA Hagan I.M., Miller C.J.;
RT "Augmented annotation of the Schizosaccharomyces pombe genome reveals
RT additional genes required for growth and viability.";
RL Genetics 187:1207-1217(2011).
CC -!- FUNCTION: Has an ATP-independent isopeptidase activity, cleaving at the
CC C-terminus of the ubiquitin moiety. Acts late in the proteolytic
CC pathway in conjunction with the 26S proteasome. Plays a role in
CC avoiding DNA overreplication (By similarity). {ECO:0000250}.
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 -!- SUBUNIT: Interacts with sfp47. {ECO:0000269|PubMed:20838651}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA18405.2; -; Genomic_DNA.
DR PIR; T39772; T39772.
DR RefSeq; NP_595732.2; NM_001021630.2.
DR AlphaFoldDB; O60139; -.
DR SMR; O60139; -.
DR BioGRID; 277355; 91.
DR STRING; 4896.SPBC18H10.08c.1; -.
DR MEROPS; C19.A58; -.
DR iPTMnet; O60139; -.
DR MaxQB; O60139; -.
DR PaxDb; O60139; -.
DR EnsemblFungi; SPBC18H10.08c.1; SPBC18H10.08c.1:pep; SPBC18H10.08c.
DR PomBase; SPBC18H10.08c; ubp4.
DR VEuPathDB; FungiDB:SPBC18H10.08c; -.
DR eggNOG; KOG1868; Eukaryota.
DR HOGENOM; CLU_474207_0_0_1; -.
DR InParanoid; O60139; -.
DR OMA; LAYEIPC; -.
DR Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR PRO; PR:O60139; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005768; C:endosome; HDA:PomBase.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IDA:PomBase.
DR GO; GO:0035871; P:protein K11-linked deubiquitination; IDA:PomBase.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; IDA:PomBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
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 1: Evidence at protein level;
KW Cytoplasm; Endosome; Hydrolase; Phosphoprotein; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..593
FT /note="Probable ubiquitin carboxyl-terminal hydrolase 4"
FT /id="PRO_0000080605"
FT DOMAIN 227..573
FT /note="USP"
FT ACT_SITE 236
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 530
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 593 AA; 67747 MW; 16801C84BB258B61 CRC64;
MSDDYFDRLF ELAFVYINED ETIQSCSFRG QRWLEEAQTL EQKNSLLKAY YYYLKALKLA
YEIPCRFEIS VKSTHYGEFK QFQKLAIQAV SKAFTIKSKL AVKHYLPVIQ ISDALSLSKK
SSLKVLFLNF YSQESSKGYV FSKHTIAIPI SCLQSMDSSK IYDFLKSAPF HPSMVICYSL
ERYFEDVSLA YKLYSMLRSL KLDPHFMELA NPKKVDSSLS YENYQPIGLT NLGNTCYMNC
VLQCLFACKD LTIPMLQGRG LLQNINTKNP LGTGGKITSA FFSLLQSVLL NHGQRSISPR
NFLEIVQSLN RDFSIDGQCD AQEFLNFFLD KLHEDLNSNA SRSPIAPLTE DQLSAREELP
LSHFSHIEWN LHLRSNKSIV VNNFVGQLCS RTQCMTCGRT STTFAPFTSL AIPIDDVSHV
VSLQECLLKF SAPELLQGHD GWHCPVCKVQ RSAKKVIMIS KLPEYLIIQI QRFKISVMGR
KKIDTPLGLS LQIPSKMLVP PSFQSGIGYI PSNYNLFAFI CHYGQLENGH YISDVLFNNE
WCHIDDSIVR TVGGITDLRE DFSSSYILFY KRSSLLEEFE DKCPKMTLKR NVK
