UBP9_SCHPO
ID UBP9_SCHPO Reviewed; 585 AA.
AC Q9P7V9;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Probable ubiquitin carboxyl-terminal hydrolase 9;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 9;
DE AltName: Full=Ubiquitin thioesterase 9;
DE AltName: Full=Ubiquitin-specific-processing protease 9;
GN Name=ubp9; ORFNames=SPBC1703.12;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505 AND SER-549, 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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BUN107 AND BUN62.
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).
CC -!- FUNCTION: Ubiquitin C-terminal hydrolase involved in regulating actin
CC dynamics and/or endocytosis at cell tips and septa.
CC {ECO:0000269|PubMed:20838651}.
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 bun107 and bun62.
CC {ECO:0000269|PubMed:20838651}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20838651}. Cytoplasm
CC {ECO:0000269|PubMed:20838651}. Cell septum
CC {ECO:0000269|PubMed:20838651}. Cell tip {ECO:0000269|PubMed:20838651}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; CU329671; CAB66456.1; -; Genomic_DNA.
DR PIR; T50325; T50325.
DR RefSeq; NP_596207.1; NM_001022126.2.
DR AlphaFoldDB; Q9P7V9; -.
DR SMR; Q9P7V9; -.
DR BioGRID; 276657; 12.
DR STRING; 4896.SPBC1703.12.1; -.
DR MEROPS; C19.A62; -.
DR iPTMnet; Q9P7V9; -.
DR MaxQB; Q9P7V9; -.
DR PaxDb; Q9P7V9; -.
DR PRIDE; Q9P7V9; -.
DR EnsemblFungi; SPBC1703.12.1; SPBC1703.12.1:pep; SPBC1703.12.
DR GeneID; 2540120; -.
DR KEGG; spo:SPBC1703.12; -.
DR PomBase; SPBC1703.12; ubp9.
DR VEuPathDB; FungiDB:SPBC1703.12; -.
DR eggNOG; KOG1864; Eukaryota.
DR HOGENOM; CLU_008279_12_2_1; -.
DR InParanoid; Q9P7V9; -.
DR OMA; NKYFCDV; -.
DR PhylomeDB; Q9P7V9; -.
DR Reactome; R-SPO-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR PRO; PR:Q9P7V9; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0030428; C:cell septum; IEA:UniProtKB-SubCell.
DR GO; GO:0051286; C:cell tip; HDA: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; ISM:PomBase.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IDA:PomBase.
DR GO; GO:0006897; P:endocytosis; IMP:PomBase.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
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; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Nucleus; Phosphoprotein; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..585
FT /note="Probable ubiquitin carboxyl-terminal hydrolase 9"
FT /id="PRO_0000080610"
FT DOMAIN 41..424
FT /note="USP"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 50
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 375
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 585 AA; 66788 MW; DA4C7951C62E38B9 CRC64;
MSLLRWMGMN SPGSTDRRKS TWEAELPKPS IRPETLTDRF YGLTNYGNTC YVSSVLVSLY
HLKPFRDSLN SYPLPSAPPN FKSVCTKTNH PESSSSRHSK KKSMENRKSS LYGSNGINSC
GCVDISNVGS ESGTKHQIVV GESNCSAYGM KENIYTCLKD LYCSVSCCDC RYGICSPERF
IQVLRRDNEA FRSTQQQDAH EFFNFLLNSV TETLDEYYGN HSDVMHPKWV HSLFEGTLTS
ETKCLTCENI TSRDESFLDL SIDIENHTSV TSCLRSFSAS EMLSSKNKFH CDVCKSLQEA
EKRMKIKKLP KILSLHLKRF KYNETQEGHD KLFYTIVFTN EMRLFTTTED AENAERMYYL
SSVIVHVGGG PHRGHYVSIV RTKTYGWVLF DDENVTPVNE NYLQRFFGDQ PGQATAYVLF
YTAADEEDDD VSEVDTKESI KPMSIPSQLK QESVEVSNLS STPRSNSTIT YPDMDPMVAS
FSSQYSHKTL DRDINSRSYF DREPSLDAER FHSRSVDASP KAVRRESRSF FPSLTRKRSK
FFGSSQSNSP KDSPLRDTHK SSDEHSESKH SHTLPWQFSR SRSKR
