ID A0A3P8WSP4_CYNSE Unreviewed; 1008 AA.
AC A0A3P8WSP4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
OS Cynoglossus semilaevis (Tongue sole).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Cynoglossidae;
OC Cynoglossinae; Cynoglossus.
OX NCBI_TaxID=244447 {ECO:0000313|Ensembl:ENSCSEP00000027655.1, ECO:0000313|Proteomes:UP000265120};
RN [1] {ECO:0000313|Ensembl:ENSCSEP00000027655.1, ECO:0000313|Proteomes:UP000265120}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24487278;
RA Chen S., Zhang G., Shao C., Huang Q., Liu G., Zhang P., Song W., An N.,
RA Chalopin D., Volff J.N., Hong Y., Li Q., Sha Z., Zhou H., Xie M., Yu Q.,
RA Liu Y., Xiang H., Wang N., Wu K., Yang C., Zhou Q., Liao X., Yang L.,
RA Hu Q., Zhang J., Meng L., Jin L., Tian Y., Lian J., Yang J., Miao G.,
RA Liu S., Liang Z., Yan F., Li Y., Sun B., Zhang H., Zhang J., Zhu Y., Du M.,
RA Zhao Y., Schartl M., Tang Q., Wang J.;
RT "Whole-genome sequence of a flatfish provides insights into ZW sex
RT chromosome evolution and adaptation to a benthic lifestyle.";
RL Nat. Genet. 46:253-260(2014).
RN [2] {ECO:0000313|Ensembl:ENSCSEP00000027655.1}
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm,
CC perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR RefSeq; XP_008316328.1; XM_008318106.2.
DR STRING; 244447.ENSCSEP00000027655; -.
DR Ensembl; ENSCSET00000028002.1; ENSCSEP00000027633.1; ENSCSEG00000017652.1.
DR Ensembl; ENSCSET00000028010.1; ENSCSEP00000027641.1; ENSCSEG00000017652.1.
DR Ensembl; ENSCSET00000028024.1; ENSCSEP00000027655.1; ENSCSEG00000017652.1.
DR GeneID; 103384550; -.
DR KEGG; csem:103384550; -.
DR GeneTree; ENSGT00390000018123; -.
DR OrthoDB; 5397179at2759; -.
DR Proteomes; UP000265120; Chromosome 1.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 3.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR11830; 40S RIBOSOMAL PROTEIN S3A; 1.
DR PANTHER; PTHR11830:SF45; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE CYLD-LIKE; 1.
DR Pfam; PF01302; CAP_GLY; 3.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM01052; CAP_GLY; 3.
DR SUPFAM; SSF74924; Cap-Gly domain; 3.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50245; CAP_GLY_2; 3.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000265120};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 135..187
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT DOMAIN 288..331
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT DOMAIN 524..567
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT DOMAIN 624..970
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 189..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..408
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..459
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1008 AA; 112162 MW; 0000EC5A13C0ADF7 CRC64;
MMSGANNDQG RKRRPPRVFA ISTDLRVQDQ VEGSIRLLRG FLCQEQDVSR TKGDWVWVKV
LDNNVMVKIE RKFLLEIQSE HGGLLEAVTD LEARLKLIND QGKLQQLATL AVDSPLWVQI
GQKDELAEAE LKYIGPLNRG SGVYFGVQLK GSAAGKGVSN GSYKGHQLFV CPEGCALFLP
ISDIRLRHWP SKSDPNIQEK VRDREQRRSN GHQSSSNSSN NSRTSHQLQP PQQQQGRHQL
RSSSPRPLSP SIIPRTTDPA LTFTIGQRVT FQPEETVYAG EVRFCDLLPG RPSAGTYVGI
LLDTPSGNWD GHYRGEKLCD IPSPLYGLLL PLNVVYAARE PEDSLSIDTF TADSPGTRDG
NCFHDQYHLS IKFLIDSHES KPRPQSPLPQ SHKPLPKPAP PPVNRSTVTS PPPSYNSKVA
LIPPGKQAVK PPPLPPPKPT HKPLSPRPPP LPPPKPRTPS STSITDQSPH ANGIHSFASS
LLLSPDGHKA PTDIGEACLE NEFEVGSLVE VNDPPIFGVI CWIGHISGIS EHVAGIELDH
ELSAGTDGSY LGERYFRCPP NKGLFVKLRN CRRDSRFPAP ETPLNQVERC NSIAFAEWGS
ERVEEHTPPV EGEEARQLYD GCKRGIQGHL NSCYLDATLF SLFSCCSSAD WVLFWPSDLK
TDSDSSQAQD LLRCEIVNPL RRYGYVCASK TMALRHLLEA PNSDTGFTNQ EKDPEEFLNR
LFQLLQVEPL LKIRSMSQQP QECHLYQLFP PTVPHSPSSH LANSPVHSPI PLLSPSSTRM
RVASVQTLLE SSFLHAGLKF VEAPSCLLLL MPRFGKDFKM FDAILPTLSL DITDLLDDTL
RQCSICQATA EFECLQCYDD VDITPGRPKQ FCSTCNTQVH SHRKRMSHSP VKVGIPDGPW
SGSLHCTRRT MSLFAVTCIE TSHYVSFIKH GPLNTDWLFF DSMADREGGQ NGFNIPRVMS
CPEVGRYLSL SEEELSRVDA ASIRETTRRL LCDSYMCLYH SPELSLYK
//
