ID   UBP12_SALSA             Reviewed;         372 AA.
AC   C0HB46; B5X1J2;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 12;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 12;
DE   AltName: Full=Ubiquitin thioesterase 12;
DE   AltName: Full=Ubiquitin-specific-processing protease 12;
GN   Name=usp12;
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA   Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA   Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA   Koop B.F.;
RT   "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT   evolutionary pressures on a post-tetraploidization genome.";
RL   BMC Genomics 11:279-279(2010).
CC   -!- FUNCTION: Deubiquitinating enzyme. Has almost no deubiquitinating
CC       activity by itself and requires the interaction with wdr48 to have a
CC       high activity. {ECO:0000250|UniProtKB:O75317}.
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;
CC   -!- SUBUNIT: Interacts with WDR48. {ECO:0000250|UniProtKB:O75317}.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. USP12/USP46 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BT044911; ACI33173.1; -; mRNA.
DR   EMBL; BT059552; ACN11265.1; -; mRNA.
DR   RefSeq; NP_001133405.1; NM_001139933.1.
DR   RefSeq; XP_014014921.1; XM_014159446.1.
DR   RefSeq; XP_014036980.1; XM_014181505.1.
DR   AlphaFoldDB; C0HB46; -.
DR   SMR; C0HB46; -.
DR   STRING; 8030.ENSSSAP00000020383; -.
DR   GeneID; 100194904; -.
DR   GeneID; 106590448; -.
DR   KEGG; sasa:100194904; -.
DR   KEGG; sasa:106590448; -.
DR   CTD; 565736; -.
DR   OrthoDB; 378361at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa19.
DR   Proteomes; UP000087266; Chromosome ssa29.
DR   Bgee; ENSSSAG00000060005; Expressed in ovary and 15 other tissues.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
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   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Metal-binding; Protease; Reference proteome; Thiol protease;
KW   Ubl conjugation pathway; Zinc.
FT   CHAIN           1..372
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 12"
FT                   /id="PRO_0000378992"
FT   DOMAIN          39..371
FT                   /note="USP"
FT   REGION          150..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..169
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        48
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   ACT_SITE        319
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   BINDING         188
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O75317"
FT   BINDING         191
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O75317"
FT   BINDING         235
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O75317"
FT   BINDING         238
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O75317"
FT   CONFLICT        163
FT                   /note="H -> N (in Ref. 1; ACI33173)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   372 AA;  43117 MW;  0C3294DF7CEC4C18 CRC64;
     MEILMTVSKF ASFCTMGANA SALEKEIGSE QFPVNEHYFG LVNFGNTCYC NSVLQALYFC
     RPFREKILAY RSQPRRKENL LTCLADLFHS IANQKRKVGV IPPKKFITRL RKENELFDNY
     MQQDAHEFLN YLLNTIADLL QEERKQDKTN GRLANGSLDS QNHNSNAPPP STWVHEIFQG
     TLTNETRCLT CETISSKDED FLDLSVDVEQ NTSITHCLRG FSNTETLCSE YKYYCEECRS
     KQEAHKRMRV KKLPMILALH LKRFKYMEQL QRYTKLSYRV VFPLELRLFN TSGDATNPER
     LYDLVAVVVH CGSGPNRGHY IAIVKSHDFW LLFDDDIVEK IDAQAIEEFY GLTSEISKNS
     ESGYILFYQS RD