Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Sentrin-specific protease

Gene

ulp-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Protease that deconjugates smo-1 from targeted proteins and may catalyze the processing of smo-1 to its mature form.2 Publications

Catalytic activityi

Hydrolysis of the alpha-linked peptide bond in the sequence Gly-Gly-|-Ala-Thr-Tyr at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptide, Smt3, leading to the mature form of the protein. A second reaction involves the cleavage of an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei585By similarity1
Active sitei602By similarity1
Active sitei653By similarity1

GO - Molecular functioni

GO - Biological processi

  • embryo development ending in birth or egg hatching Source: WormBase
  • positive regulation of error-prone translesion synthesis Source: WormBase
  • protein desumoylation Source: WormBase
  • regulation of protein localization Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

ReactomeiR-CEL-3065679. SUMO is proteolytically processed.

Protein family/group databases

MEROPSiC48.A15.

Names & Taxonomyi

Protein namesi
Recommended name:
Sentrin-specific protease (EC:3.4.22.68)
Alternative name(s):
SUMO protease
Short name:
SuPr
Ubiquitin-like protease
Gene namesi
Name:ulp-1
ORF Names:T10F2.3
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome III

Organism-specific databases

WormBaseiT10F2.3; CE33694; WBGene00006736; ulp-1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

RNAi-mediated knockdown causes increased presence of smo-1 conjugates during the first embryonic mitotic division.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001017301 – 697Sentrin-specific proteaseAdd BLAST697

Proteomic databases

EPDiQ09353.
PaxDbiQ09353.
PeptideAtlasiQ09353.
PRIDEiQ09353.

PTM databases

iPTMnetiQ09353.

Expressioni

Gene expression databases

BgeeiWBGene00006736.

Interactioni

Protein-protein interaction databases

BioGridi40935. 2 interactors.
STRINGi6239.T10F2.3.

Structurei

3D structure databases

ProteinModelPortaliQ09353.
SMRiQ09353.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni501 – 664ProteaseAdd BLAST164

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi15 – 19Nuclear localization signalSequence analysis5
Motifi462 – 467Nuclear localization signalSequence analysis6

Sequence similaritiesi

Belongs to the peptidase C48 family.Curated

Phylogenomic databases

eggNOGiKOG0778. Eukaryota.
COG5160. LUCA.
GeneTreeiENSGT00530000062941.
InParanoidiQ09353.
KOiK08592.
OMAiPRFTQKN.
OrthoDBiEOG091G092N.

Family and domain databases

InterProiIPR003653. Peptidase_C48_C.
[Graphical view]
PfamiPF02902. Peptidase_C48. 1 hit.
[Graphical view]
PROSITEiPS50600. ULP_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q09353-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRRSDLSDK DSQSRKRHWL TDQAVTNEEK EQSPTKRTRK TKSQGLGGLF
60 70 80 90 100
NTFFGMFVSS NSGEKEKTEV SGEVQVQEDD EIIVEGTTRR VAENKKYMIF
110 120 130 140 150
LNEDAPVRAN AGSEENEVII EKHVQKNVEI RNDEEKQEVQ GDLVLTLSSS
160 170 180 190 200
PKSPKNLEKS FEVQQDDEEP DVLFEKVVKT PNKQLQEARR FQNELIFLND
210 220 230 240 250
NPDTPDDVSV ISDSRSKEFI SPTPDDSVSR PITPSLSSLS NYTSNNVRDY
260 270 280 290 300
WRRNSAKKPE VLRRVPVRHQ FKHSTSVRKM NTIIDLKKIK NHLSSRDRLL
310 320 330 340 350
QGVVASGQYE AKAISGIVEK KPKKMQRTSS TDILARAKNK IAELGGSRSN
360 370 380 390 400
TPSLLSREPS IIIDSEESTS SSYRQHARSN SSESDSYRKL NDILSQINSL
410 420 430 440 450
GIGSAYRGPQ RYQNSYQLSK QKEDKLLEEA RIREGHRSQT RGDRLEDVRK
460 470 480 490 500
RLELQGIAIR PKVEKKKVDD FMALPDAADA LVERAWSGGN PNEQFVDAFS
510 520 530 540 550
IQICKKDLAT LSGLHWLNDE IINFYLQLIC DRSNGDSKYP KIYAFNTFFY
560 570 580 590 600
SNIVSKGYAS VKRWTRKVDI FAFDIVLVPV HLGMHWCMAV IDMGEKKIEF
610 620 630 640 650
YDSLYDGNTA VLPALRGYLE AESLDKKKTA MNFSGWTIQQ MTDIPRQQNG
660 670 680 690
SDCGVFSCQF GEWASRRTTP RFTQKNMPYY RKRMVYEIVS KKLLATI
Length:697
Mass (Da):79,647
Last modified:June 20, 2003 - v3
Checksum:iE825B031779E3B04
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB095020 mRNA. Translation: BAC22612.1.
FO081619 Genomic DNA. Translation: CCD72868.1.
RefSeqiNP_498095.3. NM_065694.6.
UniGeneiCel.5297.

Genome annotation databases

EnsemblMetazoaiT10F2.3; T10F2.3; WBGene00006736.
GeneIDi175704.
KEGGicel:CELE_T10F2.3.
UCSCiT10F2.3. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB095020 mRNA. Translation: BAC22612.1.
FO081619 Genomic DNA. Translation: CCD72868.1.
RefSeqiNP_498095.3. NM_065694.6.
UniGeneiCel.5297.

3D structure databases

ProteinModelPortaliQ09353.
SMRiQ09353.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi40935. 2 interactors.
STRINGi6239.T10F2.3.

Protein family/group databases

MEROPSiC48.A15.

PTM databases

iPTMnetiQ09353.

Proteomic databases

EPDiQ09353.
PaxDbiQ09353.
PeptideAtlasiQ09353.
PRIDEiQ09353.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiT10F2.3; T10F2.3; WBGene00006736.
GeneIDi175704.
KEGGicel:CELE_T10F2.3.
UCSCiT10F2.3. c. elegans.

Organism-specific databases

CTDi175704.
WormBaseiT10F2.3; CE33694; WBGene00006736; ulp-1.

Phylogenomic databases

eggNOGiKOG0778. Eukaryota.
COG5160. LUCA.
GeneTreeiENSGT00530000062941.
InParanoidiQ09353.
KOiK08592.
OMAiPRFTQKN.
OrthoDBiEOG091G092N.

Enzyme and pathway databases

ReactomeiR-CEL-3065679. SUMO is proteolytically processed.

Miscellaneous databases

PROiQ09353.

Gene expression databases

BgeeiWBGene00006736.

Family and domain databases

InterProiIPR003653. Peptidase_C48_C.
[Graphical view]
PfamiPF02902. Peptidase_C48. 1 hit.
[Graphical view]
PROSITEiPS50600. ULP_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSENP_CAEEL
AccessioniPrimary (citable) accession number: Q09353
Secondary accession number(s): Q8IU18
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 20, 2003
Last modified: November 2, 2016
This is version 103 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.