UBP12_BOVIN
ID UBP12_BOVIN Reviewed; 369 AA.
AC A5D9H7;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: Deubiquitinating enzyme. Has almost no deubiquitinating
CC activity by itself and requires the interaction with WDR48 to have a
CC high activity. Not involved in deubiquitination of monoubiquitinated
CC FANCD2. {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 -!- ACTIVITY REGULATION: Activated by interaction with WDR20 and WDR48
CC through different allosteric mechanisms.
CC {ECO:0000250|UniProtKB:O75317}.
CC -!- SUBUNIT: Interacts with WDR48. Interacts with WDR20. Component of the
CC USP12/WDR20/WDR48 deubiquitinating complex.
CC {ECO:0000250|UniProtKB:O75317}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP12/USP46 subfamily.
CC {ECO:0000305}.
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DR EMBL; BT030596; ABQ13036.1; -; mRNA.
DR RefSeq; NP_001091528.1; NM_001098059.1.
DR AlphaFoldDB; A5D9H7; -.
DR SMR; A5D9H7; -.
DR STRING; 9913.ENSBTAP00000022828; -.
DR PaxDb; A5D9H7; -.
DR PRIDE; A5D9H7; -.
DR Ensembl; ENSBTAT00000022828; ENSBTAP00000022828; ENSBTAG00000017179.
DR GeneID; 525655; -.
DR KEGG; bta:525655; -.
DR CTD; 219333; -.
DR VEuPathDB; HostDB:ENSBTAG00000017179; -.
DR VGNC; VGNC:52840; USP12.
DR eggNOG; KOG1864; Eukaryota.
DR GeneTree; ENSGT00940000153284; -.
DR HOGENOM; CLU_008279_2_0_1; -.
DR InParanoid; A5D9H7; -.
DR OMA; ATVVHCG; -.
DR OrthoDB; 378361at2759; -.
DR TreeFam; TF314144; -.
DR Proteomes; UP000009136; Chromosome 12.
DR Bgee; ENSBTAG00000017179; Expressed in spermatocyte and 105 other tissues.
DR ExpressionAtlas; A5D9H7; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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..369
FT /note="Ubiquitin carboxyl-terminal hydrolase 12"
FT /id="PRO_0000378990"
FT DOMAIN 39..368
FT /note="USP"
FT REGION 145..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..165
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 316
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O75317"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O75317"
FT BINDING 232
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"
SQ SEQUENCE 369 AA; 42683 MW; E0AC3405433BB353 CRC64;
MEILMTVSKL ASICTMGANA SALEKEIGPE QFPVNEHYFG LVNFGNTCYC NSVLQALYFC
RPFREKVLAY KSQPRKKESL LTCLADLFHS IATQKKKVGV IPPKKFITRL RKENELFDNY
MQQDAHEFLN YLLNTIADIL QEERKQEKQN GRLPNGNIDS ENNSTPDPTW VHEIFQGTLT
NETRCLTCET ISSKDEDFLD LSVDVEQNTS ITHCLRGFSN TETLCSEYKY YCEECRSKQE
AHKRMKVKKL PMILALHLKR FKYMDQLHRY TKLSYRVVFP LELRLFNTSG DATNPDRMYD
LVAVVVHCGS GPNRGHYIAI VKSHDFWLLF DDDIVEKIDA QAIEEFYGLT SDISKNSESG
YILFYQSRD
