UBP10_SCHPO
ID UBP10_SCHPO Reviewed; 502 AA.
AC Q9USR2;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Probable mRNA-splicing protein ubp10;
DE AltName: Full=Probable inactive ubiquitin-specific-processing protease 10;
GN Name=ubp10; ORFNames=SPBC577.07;
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).
CC -!- FUNCTION: May play a role in mRNA splicing. It is unsure if the protein
CC really exhibits hydrolase activity. Could be a competitor of ubiquitin
CC C-terminal hydrolases (UCHs) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; CU329671; CAB54815.1; -; Genomic_DNA.
DR PIR; T40551; T40551.
DR RefSeq; NP_595305.1; NM_001021212.2.
DR AlphaFoldDB; Q9USR2; -.
DR SMR; Q9USR2; -.
DR BioGRID; 277381; 3.
DR STRING; 4896.SPBC577.07.1; -.
DR MEROPS; C19.972; -.
DR MaxQB; Q9USR2; -.
DR PaxDb; Q9USR2; -.
DR EnsemblFungi; SPBC577.07.1; SPBC577.07.1:pep; SPBC577.07.
DR GeneID; 2540864; -.
DR KEGG; spo:SPBC577.07; -.
DR PomBase; SPBC577.07; ubp10.
DR VEuPathDB; FungiDB:SPBC577.07; -.
DR eggNOG; KOG2026; Eukaryota.
DR HOGENOM; CLU_016848_2_1_1; -.
DR InParanoid; Q9USR2; -.
DR OMA; HVYINLE; -.
DR PhylomeDB; Q9USR2; -.
DR PRO; PR:Q9USR2; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; ISS:PomBase.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISM:PomBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISO:PomBase.
DR GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0000245; P:spliceosomal complex assembly; IEA:InterPro.
DR CDD; cd02669; Peptidase_C19M; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR033809; USP39.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646:SF16; PTHR21646:SF16; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Metal-binding; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Ribonucleoprotein; Spliceosome; Zinc; Zinc-finger.
FT CHAIN 1..502
FT /note="Probable mRNA-splicing protein ubp10"
FT /id="PRO_0000351443"
FT DOMAIN 178..501
FT /note="USP"
FT ZN_FING 56..153
FT /note="UBP-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
SQ SEQUENCE 502 AA; 58885 MW; 491CED10CC66E8B7 CRC64;
MSENKDKNNI LKRHIEEDNN IDNGKRKKLE LGKDMEDVHD IASKEMEEHE TTPIISQNLY
LDTINRKLLD FDFEKVCSVS LTNLSVYACL VCGRYFQGRG PSSHAYFHAL TENHHVFVNC
STLKFYVLPE SYQVESSALQ DIAYVMRPTF TKLEVQRLDH TPQLSYDLML KPYVPGFVGM
NNIKNNDYFN VVIHMLAHVK PFRNYFLLKN FDNCPQLVQR LAILIRKLWN HKAFKSHVSP
QELIQEVTVL SHKKYSINEQ KDPVEFLSWF LNTLHNCLGG KKSTIAKPTS IVHYSFQGFV
RIESQKIRQH AEKGEQVVFT GDRVIQTNVV PFLYLTLDLP PKPIFQDEFE GNIIPQVELK
EILNKYNGVH TQELAGMRRR FHLMTAPPYF IFHIKRFMKN NYFTERNQTI VTFPLDDFDM
SPFIDDSFIQ SNPKISTKYN LVANIIHESV THAEEEFHNF RIQIRNPSTN KWYQIQDLYV
EEISSDMIRL GESFIQLWER SS
