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Database: UniProt
Entry: A0A060X6U4_ONCMY
LinkDB: A0A060X6U4_ONCMY
Original site: A0A060X6U4_ONCMY 
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}.
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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
//
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