UBP21_SCHPO
ID UBP21_SCHPO Reviewed; 1129 AA.
AC Q9UTT1;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 21;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 21;
DE AltName: Full=Ubiquitin thioesterase 21;
DE AltName: Full=Ubiquitin-specific-processing protease 21;
GN Name=ubp21; Synonyms=ubp15, ubpd; ORFNames=SPBC713.02c;
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 [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=11919719; DOI=10.1007/s00438-002-0639-8;
RA Richert K., Schmidt H., Gross T., Kaeufer N.F.;
RT "The deubiquitinating enzyme Ubp21p of fission yeast stabilizes a mutant
RT form of protein kinase Prp4p.";
RL Mol. Genet. Genomics 267:88-95(2002).
RN [2]
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).
CC -!- FUNCTION: Involved in regulating the steady-state levels of proteins
CC including prp4. {ECO:0000269|PubMed:11919719}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11919719}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; AF187961; AAF01440.1; -; Genomic_DNA.
DR EMBL; CU329671; CAC22603.1; -; Genomic_DNA.
DR RefSeq; NP_595341.1; NM_001021249.2.
DR AlphaFoldDB; Q9UTT1; -.
DR SMR; Q9UTT1; -.
DR BioGRID; 277646; 14.
DR IntAct; Q9UTT1; 1.
DR STRING; 4896.SPBC713.02c.1; -.
DR MEROPS; C19.A59; -.
DR iPTMnet; Q9UTT1; -.
DR MaxQB; Q9UTT1; -.
DR PaxDb; Q9UTT1; -.
DR PRIDE; Q9UTT1; -.
DR EnsemblFungi; SPBC713.02c.1; SPBC713.02c.1:pep; SPBC713.02c.
DR GeneID; 2541131; -.
DR KEGG; spo:SPBC713.02c; -.
DR PomBase; SPBC713.02c; -.
DR VEuPathDB; FungiDB:SPBC713.02c; -.
DR eggNOG; KOG1863; Eukaryota.
DR HOGENOM; CLU_003532_2_1_1; -.
DR InParanoid; Q9UTT1; -.
DR OMA; KMKGTCL; -.
DR PhylomeDB; Q9UTT1; -.
DR PRO; PR:Q9UTT1; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0101005; F:deubiquitinase activity; IDA:PomBase.
DR GO; GO:0004175; F:endopeptidase activity; IDA:PomBase.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IDA:PomBase.
DR GO; GO:1904332; P:negative regulation of error-prone translesion synthesis; 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:0070536; P:protein K63-linked deubiquitination; IDA:PomBase.
DR GO; GO:0031647; P:regulation of protein stability; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 2.60.210.10; -; 1.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR024729; USP7_ICP0-binding_dom.
DR InterPro; IPR029346; USP_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00917; MATH; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF14533; USP7_C2; 1.
DR Pfam; PF12436; USP7_ICP0_bdg; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50144; MATH; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase; Nucleus; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..1129
FT /note="Ubiquitin carboxyl-terminal hydrolase 21"
FT /id="PRO_0000080614"
FT DOMAIN 51..204
FT /note="MATH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT DOMAIN 230..545
FT /note="USP"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 239
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 481
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT CONFLICT 42
FT /note="H -> D (in Ref. 1; AAF01440)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1129 AA; 130832 MW; 536681DD9E78EBF8 CRC64;
MVLSNVDAEE VNMDSSMELE ESSQEPLRAD NYEEIYNSLV HHEPDLEEAA HASYSWVVKN
FSTLEDKTYS PLFKAGHTTW RIVLFPKGCN QTEYASVFLE YLPQCKVEAI RKYEAELAAG
KTPTIDPEIV NDETYSCCAQ FALSLSNVQD PTVMQINTSH HRFRSEVKDW GFTRFVDLRK
IAVPTPEFPV PFLENDEICI SVTVRVLQDP TGVLWHSFVN YNSKKETGYV GLKNQGATCY
MNSLLQSLFF TNIFRKTVYK IPTDNDDSRD SVAYALQRVF YNLEKQREPV STTELTRSFG
WNSFDSFMQH DIQEFNRVLQ DNLEKKMKGT EVENALNDIF VGKMKSYVKC IDVNYESSRV
EDFWDIQLNV KGMDTLEDSF RDAIQVETLT GDNKYYAEGH GLQDAHKGII FESLPNVLQL
QLKRFDYDML RDMMVKINDR HEFPLEIDLE PYLSETADKS ESHVYVLHGV LVHGGDLHGG
HYYALIKPEK DSNWFKFDDD RVTRATIKEV LEDNYGGEPA GRAKGYNGNP FKRFMNAYML
VYFRKSRLDH ILSPVTAEDV PFHVRNTLDE EHRVVERKLL EREEQQIYRR VRVLTTDGFK
KYHGFDMTDF SASDDDPVLI TTKIKRNANI WDLQKHLAGL LNRDTSGIRI WLMTNRQNRT
VRVDLPLDKK TILVDQICDM HIRKDMDMRV YVEFLSEHNQ LLADFGATDD NDFDTYIFLK
IFDYETQQIS GLADLHVSKN SPISSLSEWI REHLKWSSDV PITYYEEIKT GMVDVLDPNA
SFEKSEIQVG DIICFEKKLV HDSSSDTSHP YKSALDLYDF MAHRVVITFE PRYSDDTNNG
VFDLVLTTHT NYTDMARAVA NKLNVDPNYL QFTMAHLPSR TPRSVIRNPS KFTLQNAIPS
TYSHNQNVVM FYEVLDITLS ELERKQLIRV HFLSNGISHE TQMEFYVDKE GTVEDILRQV
TQKVPLNAED ASRLRLYEVY NHRILKSHLP TDGIYDLNEF STAYVEVTPK EEQMQLKTDD
AVSIVVQHFF KDLSRLHDIP FYFVLLRGET LKDLKKRLQK RLGYNDTQFS KVKLAVLQAQ
SFGKPYYLTD DDEVLYGELE PQSHILGLDH PPANGSAQYH GMDQAIRMK
