ID   UBP12_DANRE             Reviewed;         371 AA.
AC   A4FUN7;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   02-SEP-2026, entry version 92.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 12A;
DE            EC=3.4.19.12 {ECO:0000250|UniProtKB:O75317};
DE   AltName: Full=Deubiquitinating enzyme 12A;
DE   AltName: Full=Ubiquitin thioesterase 12A;
DE   AltName: Full=Ubiquitin-specific-processing protease 12A;
GN   Name=usp12a; Synonyms=usp12;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000250|UniProtKB:O75317};
CC   -!- SUBUNIT: Interacts with WDR48. {ECO:0000250|UniProtKB:O75317}.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. USP12/USP46 subfamily.
CC       {ECO:0000305}.
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; BC115286; AAI15287.1; -; mRNA.
DR   RefSeq; NP_001077025.1; NM_001083556.1.
DR   AlphaFoldDB; A4FUN7; -.
DR   SMR; A4FUN7; -.
DR   FunCoup; A4FUN7; 2400.
DR   STRING; 7955.ENSDARP00000103890; -.
DR   PaxDb; 7955-ENSDARP00000103890; -.
DR   PeptideAtlas; A4FUN7; -.
DR   Ensembl; ENSDART00000112670; ENSDARP00000103890; ENSDARG00000078109.
DR   GeneID; 565736; -.
DR   KEGG; dre:565736; -.
DR   AGR; ZFIN:ZDB-GENE-060228-3; -.
DR   CTD; 565736; -.
DR   ZFIN; ZDB-GENE-060228-3; usp12a.
DR   eggNOG; KOG1864; Eukaryota.
DR   GeneTree; ENSGT00940000153284; -.
DR   HOGENOM; CLU_008279_2_0_1; -.
DR   InParanoid; A4FUN7; -.
DR   OMA; KSHNFWL; -.
DR   OrthoDB; 27652at2759; -.
DR   PhylomeDB; A4FUN7; -.
DR   Reactome; R-DRE-5689880; Ub-specific processing proteases.
DR   PRO; PR:A4FUN7; -.
DR   Proteomes; UP000000437; Chromosome 24.
DR   Bgee; ENSDARG00000078109; Expressed in brain and 27 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR   CDD; cd02663; Peptidase_C19G; 1.
DR   FunFam; 3.90.70.10:FF:000003; Ubiquitin carboxyl-terminal hydrolase 46; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR050164; Peptidase_C19.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR028889; USP.
DR   InterPro; IPR018200; USP_CS.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF647; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 12; 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   2: Evidence at transcript level;
KW   Hydrolase; Metal-binding; Protease; Reference proteome; Thiol protease;
KW   Ubl conjugation pathway; Zinc.
FT   CHAIN           1..371
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 12A"
FT                   /id="PRO_0000378991"
FT   DOMAIN          39..370
FT                   /note="USP"
FT   REGION          148..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..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        318
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   BINDING         187
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O75317"
FT   BINDING         190
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O75317"
FT   BINDING         234
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O75317"
FT   BINDING         237
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O75317"
SQ   SEQUENCE   371 AA;  43027 MW;  930E27CEBE0C8A53 CRC64;
     MEILMTVSKF ASFCTMGANA SALEKEIGSE QFPVNEHYFG LVNFGNTCYC NSVLQALYFC
     RPFREKILAY RSQPRRKENL LTCLADLFHS IANQKRKVGV IPPKKFITRL RKENELFDNY
     MQQDAHEFLN YLLNTIADLL QEERKQDKQN GKLANGTLDS QNNNSTPPST TWVHEIFQGT
     LTNETRCLTC ETISSKDEDF LDLSVDVEQN TSITHCLRGF SNTETLCSEY KYYCEECRSK
     QEAHKRMRVK KLPMILALHL KRFKYMEQLQ RYTKLSYRVV FPLELRLFNT SGDATNPERL
     YDLVAVVVHC GSGPNRGHYI AIVKSHDFWL LFDDDIVEKI DAQAIEEFYG LTSEISKNSE
     SGYILFYQSR D
//