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   27-MAR-2024, entry version 141.
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; 284812.O60139; -.
DR   MEROPS; C19.A58; -.
DR   iPTMnet; O60139; -.
DR   MaxQB; O60139; -.
DR   PaxDb; 4896-SPBC18H10-08c-1; -.
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; CRFEISV; -.
DR   Reactome; R-SPO-5656169; Termination of translesion DNA synthesis.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02674; Peptidase_C19R; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
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   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF104; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 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
//