SENP_CAEEL
ID SENP_CAEEL Reviewed; 697 AA.
AC Q09353; Q8IU18;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Sentrin-specific protease;
DE EC=3.4.22.-;
DE AltName: Full=SUMO protease;
DE Short=SuPr;
DE AltName: Full=Ubiquitin-like protease;
GN Name=ulp-1; ORFNames=T10F2.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2;
RA Tsubaki A., Inoue H., Takahashi K.;
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION.
RX PubMed=15107848; DOI=10.1038/ng1336;
RA Zhang H., Smolen G.A., Palmer R., Christoforou A., van den Heuvel S.,
RA Haber D.A.;
RT "SUMO modification is required for in vivo Hox gene regulation by the
RT Caenorhabditis elegans Polycomb group protein SOP-2.";
RL Nat. Genet. 36:507-511(2004).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=25475837; DOI=10.1038/ncomms6485;
RA Pelisch F., Sonneville R., Pourkarimi E., Agostinho A., Blow J.J.,
RA Gartner A., Hay R.T.;
RT "Dynamic SUMO modification regulates mitotic chromosome assembly and cell
RT cycle progression in Caenorhabditis elegans.";
RL Nat. Commun. 5:5485-5485(2014).
CC -!- FUNCTION: Protease that deconjugates smo-1 from targeted proteins and
CC may catalyze the processing of smo-1 to its mature form.
CC {ECO:0000269|PubMed:15107848, ECO:0000269|PubMed:25475837}.
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:25475837}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes increased presence
CC of smo-1 conjugates during the first embryonic mitotic division.
CC {ECO:0000269|PubMed:25475837}.
CC -!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
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DR EMBL; AB095020; BAC22612.1; -; mRNA.
DR EMBL; FO081619; CCD72868.1; -; Genomic_DNA.
DR RefSeq; NP_498095.3; NM_065694.6.
DR AlphaFoldDB; Q09353; -.
DR SMR; Q09353; -.
DR BioGRID; 40935; 7.
DR STRING; 6239.T10F2.3; -.
DR MEROPS; C48.A15; -.
DR iPTMnet; Q09353; -.
DR EPD; Q09353; -.
DR PaxDb; Q09353; -.
DR PeptideAtlas; Q09353; -.
DR EnsemblMetazoa; T10F2.3.1; T10F2.3.1; WBGene00006736.
DR GeneID; 175704; -.
DR KEGG; cel:CELE_T10F2.3; -.
DR UCSC; T10F2.3; c. elegans.
DR CTD; 175704; -.
DR WormBase; T10F2.3; CE33694; WBGene00006736; ulp-1.
DR eggNOG; KOG0778; Eukaryota.
DR GeneTree; ENSGT00940000167730; -.
DR HOGENOM; CLU_415183_0_0_1; -.
DR InParanoid; Q09353; -.
DR OMA; PRFTQKN; -.
DR OrthoDB; 905030at2759; -.
DR Reactome; R-CEL-3065679; SUMO is proteolytically processed.
DR Reactome; R-CEL-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q09353; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006736; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016929; F:deSUMOylase activity; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:1904333; P:positive regulation of error-prone translesion synthesis; IMP:WormBase.
DR GO; GO:0016926; P:protein desumoylation; IMP:WormBase.
DR GO; GO:0032880; P:regulation of protein localization; IMP:WormBase.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR003653; Peptidase_C48_C.
DR Pfam; PF02902; Peptidase_C48; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50600; ULP_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Nucleus; Protease; Reference proteome; Thiol protease.
FT CHAIN 1..697
FT /note="Sentrin-specific protease"
FT /id="PRO_0000101730"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..664
FT /note="Protease"
FT MOTIF 15..19
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 462..467
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 585
FT /evidence="ECO:0000250"
FT ACT_SITE 602
FT /evidence="ECO:0000250"
FT ACT_SITE 653
FT /evidence="ECO:0000250"
SQ SEQUENCE 697 AA; 79647 MW; E825B031779E3B04 CRC64;
MSRRSDLSDK DSQSRKRHWL TDQAVTNEEK EQSPTKRTRK TKSQGLGGLF NTFFGMFVSS
NSGEKEKTEV SGEVQVQEDD EIIVEGTTRR VAENKKYMIF LNEDAPVRAN AGSEENEVII
EKHVQKNVEI RNDEEKQEVQ GDLVLTLSSS PKSPKNLEKS FEVQQDDEEP DVLFEKVVKT
PNKQLQEARR FQNELIFLND NPDTPDDVSV ISDSRSKEFI SPTPDDSVSR PITPSLSSLS
NYTSNNVRDY WRRNSAKKPE VLRRVPVRHQ FKHSTSVRKM NTIIDLKKIK NHLSSRDRLL
QGVVASGQYE AKAISGIVEK KPKKMQRTSS TDILARAKNK IAELGGSRSN TPSLLSREPS
IIIDSEESTS SSYRQHARSN SSESDSYRKL NDILSQINSL GIGSAYRGPQ RYQNSYQLSK
QKEDKLLEEA RIREGHRSQT RGDRLEDVRK RLELQGIAIR PKVEKKKVDD FMALPDAADA
LVERAWSGGN PNEQFVDAFS IQICKKDLAT LSGLHWLNDE IINFYLQLIC DRSNGDSKYP
KIYAFNTFFY SNIVSKGYAS VKRWTRKVDI FAFDIVLVPV HLGMHWCMAV IDMGEKKIEF
YDSLYDGNTA VLPALRGYLE AESLDKKKTA MNFSGWTIQQ MTDIPRQQNG SDCGVFSCQF
GEWASRRTTP RFTQKNMPYY RKRMVYEIVS KKLLATI
