ULP2_CAEEL
ID ULP2_CAEEL Reviewed; 893 AA.
AC Q23238;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Ubiquitin-like protease 2 {ECO:0000312|WormBase:Y38A8.3a};
DE EC=3.4.22.- {ECO:0000250|UniProtKB:Q9GZR1};
GN Name=ulp-2 {ECO:0000312|WormBase:Y38A8.3a};
GN ORFNames=Y38A8.3 {ECO:0000312|WormBase:Y38A8.3a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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 [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF CYS-743.
RX PubMed=26412237; DOI=10.1016/j.devcel.2015.08.019;
RA Tsur A., Bening Abu-Shach U., Broday L.;
RT "ULP-2 SUMO Protease Regulates E-Cadherin Recruitment to Adherens
RT Junctions.";
RL Dev. Cell 35:63-77(2015).
CC -!- FUNCTION: Protease that catalyzes two essential functions in the smo-1
CC pathway: processing of full-length smo-1 to their mature forms and
CC deconjugation of smo-1 from targeted proteins (By similarity). May
CC deconjugate smo-1 from the cadherin protein hmr-1 and plays a role in
CC its recruitment to and the maintenance of adherens junctions
CC (PubMed:26412237). Required for epidermal morphogenesis during
CC embryonic development (PubMed:26412237). {ECO:0000250|UniProtKB:Q8RWN0,
CC ECO:0000269|PubMed:26412237}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26412237}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:26412237}.
CC -!- DEVELOPMENTAL STAGE: First expressed mid-gastrulation, at the 200-cell
CC stage of embryogenesis with expression increasing during epidermal
CC morphogenesis. Also expressed in epidermal cells and also in the
CC underlying neuroblasts during embryonic development.
CC {ECO:0000269|PubMed:26412237}.
CC -!- DISRUPTION PHENOTYPE: 64% of embryos arrest in between late
CC gastrulation and epidermal morphogenesis with failures in embryogenesis
CC occurring during late gastrulation, epidermal enclosure and elongation.
CC RNAi-mediated knockdown results in arrest in 29% of embryos which
CC display a range of embryonic abnormalities including increased bulge
CC formation (humpback phenotype), epidermal enclosure defects where the
CC ventral cleft fails to close during embryogenesis, impeded or inhibited
CC ventral neuroblast cell migration and irregular cell shape and
CC positioning. Knockdown also results in failure of the catenin-cadherin
CC complex, specifically the cadherin protein, hmr-1 to localize to
CC adherens junctions, but to accumulate along the basolateral membrane of
CC the cell. {ECO:0000269|PubMed:26412237}.
CC -!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
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DR EMBL; BX284602; CCD73695.1; -; Genomic_DNA.
DR PIR; T26650; T26650.
DR RefSeq; NP_494914.1; NM_062513.4.
DR AlphaFoldDB; Q23238; -.
DR SMR; Q23238; -.
DR STRING; 6239.Y38A8.3; -.
DR MEROPS; C48.A12; -.
DR EPD; Q23238; -.
DR PaxDb; Q23238; -.
DR PeptideAtlas; Q23238; -.
DR EnsemblMetazoa; Y38A8.3a.1; Y38A8.3a.1; WBGene00006737.
DR GeneID; 173859; -.
DR UCSC; Y38A8.3; c. elegans.
DR CTD; 173859; -.
DR WormBase; Y38A8.3a; CE29374; WBGene00006737; ulp-2.
DR eggNOG; KOG0779; Eukaryota.
DR HOGENOM; CLU_354595_0_0_1; -.
DR InParanoid; Q23238; -.
DR OMA; NAPKTYM; -.
DR OrthoDB; 800332at2759; -.
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 Reactome; R-CEL-9035034; RHOF GTPase cycle.
DR PRO; PR:Q23238; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00006737; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q23238; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0016929; F:deSUMOylase activity; ISS:WormBase.
DR GO; GO:0034334; P:adherens junction maintenance; IMP:WormBase.
DR GO; GO:0016926; P:protein desumoylation; IMP:WormBase.
DR GO; GO:0070587; P:regulation of cell-cell adhesion involved in gastrulation; 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 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Hydrolase; Nucleus; Protease;
KW Reference proteome; Thiol protease.
FT CHAIN 1..893
FT /note="Ubiquitin-like protease 2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436262"
FT REGION 538..800
FT /note="Protease"
FT /evidence="ECO:0000250|UniProtKB:Q02724"
FT ACT_SITE 644
FT /evidence="ECO:0000250|UniProtKB:Q02724"
FT ACT_SITE 678
FT /evidence="ECO:0000250|UniProtKB:Q02724"
FT ACT_SITE 743
FT /evidence="ECO:0000305|PubMed:26412237"
FT MUTAGEN 743
FT /note="C->S: Probable loss of catalytic activity. Failed
FT epidermal enclosure during embryogenesis."
FT /evidence="ECO:0000269|PubMed:26412237"
SQ SEQUENCE 893 AA; 102426 MW; EAC4325AD051B908 CRC64;
MSDSTQMEAN AAINEIKKRT RKLDQSLQMR FCADQFFIGN HCTKLASGKS IIISQNSKNR
ICLRFFMAAD PLVGYTGRDF GIAFNQIDHI SLKDEQQENP AVLICTLNLS SYTKMCKLQT
GLKDVVEKPF LYNKSLARNL TFILKPWNDD PDTFVKISYN DEHREYVHSY DYDVAKSLMF
KEVQAVWEQS LKEQLQRRHQ TGRVYLTSQL SEMTPREWVQ FLADQKLSKI VCHNGSIQYA
RVEDNPHGRK HTAVATNGFD HRGTRVLNSF GKAHASLATQ EKSYAKKRKL TEQSLKLIYR
NDRSVWLEGS CAKNLKMPKI NSEPNMGEFM GWPDMDNAMT HPTSNFENED VMKSTKQPND
FVSFEQLQAP PPVLQRQNGA IYSTQSVAFT HISGNDGVED LTEKISHLGE EAYNIDMANA
LHAFSDNWHY EIHPNTVHNA SFEQLHIGDG NSSIGTIGFN PLEPYPQSSF PQSNNWQQAH
GDFTFPQVSF PNTQQGSCLP STPTAALPPT RPVVEKIPPD TQLFTFPPSG SCTTGMDPVV
LLVKDIKTLD RKEFLNDSVM AFMLNYIAFM LSSELMKSVH MCNTFLFVNL TRLLPPLCFS
KRRPIEPEHI KIVKDNCPRV LRWTRKFDVL AKDYIIIPIN EDLHWLVIAV INPSGAIVDM
SNEEASRAAP KCYIVFFDPL SGLDPSKKNH MCHCIKIYLA QLYENTKAPG MKFASKNPTI
YDEERVVVTR AENTPIQDNF YDCGLYVLHF IEGLFCYPNR PVNVNDFPNF DWSKFFPEAN
KMCDLMRDKV YNLILQQADK PARSRLAKFE RENKCGLSRE GALRKARRHS AVNERRTKRH
RDYYARHYSL SPPHRNVMND DPTFMNPRGL AEMPITRLVR RLRIPEDNFP IAY
