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   27-MAR-2024, entry version 131.
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 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; 284812.Q9P7V9; -.
DR   MEROPS; C19.A62; -.
DR   iPTMnet; Q9P7V9; -.
DR   MaxQB; Q9P7V9; -.
DR   PaxDb; 4896-SPBC1703-12-1; -.
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; ANFGNTC; -.
DR   PhylomeDB; Q9P7V9; -.
DR   Reactome; R-SPO-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR   PRO; PR:Q9P7V9; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0032153; C:cell division site; HDA:PomBase.
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:0140492; F:metal-dependent deubiquitinase activity; IDA:PomBase.
DR   GO; GO:0006897; P:endocytosis; IMP:PomBase.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02663; Peptidase_C19G; 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; PTHR24006:SF944; RE52890P; 1.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 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
//