ID A0A060X6U4_ONCMY Unreviewed; 597 AA.
AC A0A060X6U4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=GSONMT00062625001 {ECO:0000313|EMBL:CDQ75171.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ75171.1, ECO:0000313|Proteomes:UP000193380};
RN [1] {ECO:0000313|EMBL:CDQ75171.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24755649; DOI=10.1038/ncomms4657;
RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA Guiguen Y.;
RT "The rainbow trout genome provides novel insights into evolution after
RT whole-genome duplication in vertebrates.";
RL Nat. Commun. 5:3657-3657(2014).
RN [2] {ECO:0000313|EMBL:CDQ75171.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSOMYP00000099151.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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; Evidence={ECO:0000256|ARBA:ARBA00000707,
CC ECO:0000256|RuleBase:RU366025};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP2 subfamily.
CC {ECO:0000256|ARBA:ARBA00037943}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FR905033; CDQ75171.1; -; Genomic_DNA.
DR STRING; 8022.A0A060X6U4; -.
DR PaxDb; 8022-A0A060X6U4; -.
DR Ensembl; ENSOMYT00000107625.2; ENSOMYP00000099151.1; ENSOMYG00000044946.2.
DR GeneTree; ENSGT00940000161289; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000193380; Unassembled WGS sequence.
DR Proteomes; UP000694395; Chromosome 27.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF17; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 2; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 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 Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000193380};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 260..592
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 597 AA; 65829 MW; 17BC883B90E836C3 CRC64;
MSRVSTTAKR YTGSSYTSAY SSYGSSLTPS SLSSYTSDRD RLPSYRSNAA SSSGYSSSSY
LSSAASRARN YSTSSELDRG RPIPRTDLLS SSSRRSESLS RTPVKTYGSS GLSGGSGYTG
YSSYSSSTTP SRSSYLSSSP GASSISLSRR RSSSQSDLTR DLSSLGLTEP TSPSCSSSSA
LRGYRSRASD VADSYNSSLQ SSSYGLSHSA TQEALSSSSL KSGGGSRFTS SYERSDSSSN
GRSSSPTRDS LNSKSTQGLV GLRNLGNTCF MNSILQCLSN THNLRDYCLH NSHRRDLNKN
SRTNTGALME EFAKLLQTMW TSSSSEAVGP SEFKTQIQRY APRFVGYNQQ DAQEFLRFLL
DGLHNEVNRV TVRPRGSSED FDHLPDREKG DRMWSKYLER EDSKVVDLFV GQLKSSLTCS
TCGYCSTVFD PFWDLSLPIA KKGYGEVSLM DCVSLFTKED VLDGDEKPTC YRCKARRRCT
KKFTVQKFPK ILVLHLKRFS EARRTSKLST FVNFPMEKLD LREFASENSI NAVYNLYAVS
NHSGTTMGGH YTAYCRNPTS GEWYTFNDSR VSPMSSSQVR SSDAYVLFYE LASSSRM
//