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Database: UniProt
Entry: W5UKZ1_ICTPU
LinkDB: W5UKZ1_ICTPU
Original site: W5UKZ1_ICTPU 
ID   W5UKZ1_ICTPU            Unreviewed;       520 AA.
AC   W5UKZ1;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN   Name=USP3 {ECO:0000313|EMBL:AHH42666.1};
GN   Synonyms=usp3 {ECO:0000313|RefSeq:XP_017341233.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|EMBL:AHH42666.1};
RN   [1] {ECO:0000313|EMBL:AHH42666.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mixed {ECO:0000313|EMBL:AHH42666.1};
RX   PubMed=23127152; DOI=10.1186/1471-2164-13-595;
RA   Liu S., Zhang Y., Zhou Z., Waldbieser G., Sun F., Lu J., Zhang J.,
RA   Jiang Y., Zhang H., Wang X., Rajendran K.V., Khoo L., Kucuktas H.,
RA   Peatman E., Liu Z.;
RT   "Efficient assembly and annotation of the transcriptome of catfish by RNA-
RT   Seq analysis of a doubled haploid homozygote.";
RL   BMC Genomics 13:595-595(2012).
RN   [2] {ECO:0000313|RefSeq:XP_017341233.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017341233.1};
RG   RefSeq;
RL   Submitted (NOV-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   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|RuleBase:RU366025}.
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DR   EMBL; JT418240; AHH42666.1; -; mRNA.
DR   RefSeq; XP_017341233.1; XM_017485744.3.
DR   STRING; 7998.ENSIPUP00000032292; -.
DR   Ensembl; ENSIPUT00000033568; ENSIPUP00000032292; ENSIPUG00000021688.
DR   GeneID; 108275133; -.
DR   CTD; 9960; -.
DR   OMA; AGKRIYN; -.
DR   OrthoDB; 227085at2759; -.
DR   Proteomes; UP000221080; Chromosome 14.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF19; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 3; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   SMART; SM00290; ZnF_UBP; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366025};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|RuleBase:RU366025};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00502}.
FT   DOMAIN          1..119
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50271"
FT   DOMAIN          157..509
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          120..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   520 AA;  58400 MW;  F290CDA09C94FD71 CRC64;
     MECPHLSSTV CVAMDPTRFP HGSPSSWCCS VCRSNKSPWV CLTCLNVHCG RYVNGHAKKH
     FEEVHCSATG QKKTEKFQQH SVCMDCSSYS TFCYRCDDFV VNDTKLGQVQ RVREHLQSLE
     NSVINSDRPR KRKLSGSSSP DLRMSADGEG PPARSATGLR NLGNTCFMNA ILQSLGNIPE
     FSCYFKDLPA VALRSGKTAG RRMYHTRSQG DSSVSLVEEL RKTLCSLWQG SQTAFSPDAL
     FYVIWKIMPS FRGYQQQDAH EFLRYLLDHL HRELQGSKNG LPGPSLLPDI PNLNSGSKCS
     INGTPTMVTA VFGGVLHNEV NCLICGTESK KFDPFLDLSL DIPSQFRVKR TKDQEPGPTC
     TLGDCLSSFT DLEQLDETEL YMCHKCKKRQ KSTKKFWIQK LPKVLCLHLK RFHWTAFLRN
     KVDTYVEFPL RGLDLKCYLL ESENSLPESC LYDLAAVVVH HGSGVGSGHY TAYGLHEGCW
     YHFNDSTVTV VSEETVAKAK AYILFYTEQD NTGSLTKPKL
//
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