ID   MINY3_MACFA             Reviewed;         445 AA.
AC   Q4R528; Q9BGR2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase MINDY-3;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme MINDY-3;
DE   AltName: Full=Protein CARP;
GN   Name=MINDY3; Synonyms=CARP, FAM188A;
GN   ORFNames=QflA-10011, QflA-13278, QtsA-14653;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA   Terao K., Sugano S., Hashimoto K.;
RT   "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT   the human genome sequence.";
RL   BMC Genomics 3:36-36(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Frontal cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Hydrolase that can remove 'Lys-48'-linked conjugated
CC       ubiquitin from proteins. {ECO:0000250|UniProtKB:Q9H8M7}.
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:Q9H8M7};
CC   -!- SUBUNIT: Interacts with COPS5. {ECO:0000250|UniProtKB:Q9H8M7}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H8M7}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q4R528-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q4R528-2; Sequence=VSP_031040;
CC   -!- SIMILARITY: Belongs to the MINDY deubiquitinase family. FAM188
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AB169716; BAE01797.1; -; mRNA.
DR   EMBL; AB070132; BAB63077.1; -; mRNA.
DR   EMBL; AB056410; BAB33068.1; -; mRNA.
DR   RefSeq; XP_005564769.1; XM_005564712.2. [Q4R528-1]
DR   AlphaFoldDB; Q4R528; -.
DR   STRING; 9541.XP_005564769.1; -.
DR   Ensembl; ENSMFAT00000016415; ENSMFAP00000042135; ENSMFAG00000039849. [Q4R528-1]
DR   Ensembl; ENSMFAT00000016424; ENSMFAP00000042144; ENSMFAG00000039849. [Q4R528-2]
DR   GeneID; 102116461; -.
DR   KEGG; mcf:102116461; -.
DR   CTD; 80013; -.
DR   VEuPathDB; HostDB:ENSMFAG00000039849; -.
DR   eggNOG; KOG2871; Eukaryota.
DR   GeneTree; ENSGT00940000155958; -.
DR   OMA; HVWDHDQ; -.
DR   Proteomes; UP000233100; Chromosome 9.
DR   Bgee; ENSMFAG00000039849; Expressed in lymph node and 13 other tissues.
DR   GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:1990380; F:Lys48-specific deubiquitinase activity; IEA:Ensembl.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR025257; MINDY-3/4_CD.
DR   InterPro; IPR039785; MINY3/4.
DR   PANTHER; PTHR12473; PTHR12473; 1.
DR   Pfam; PF13898; DUF4205; 1.
DR   SMART; SM01174; DUF4205; 1.
DR   SUPFAM; SSF47473; SSF47473; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Apoptosis; Hydrolase; Nucleus; Phosphoprotein;
KW   Protease; Reference proteome; Thiol protease; Ubl conjugation pathway.
FT   CHAIN           1..445
FT                   /note="Ubiquitin carboxyl-terminal hydrolase MINDY-3"
FT                   /id="PRO_0000317561"
FT   ACT_SITE        51
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT   ACT_SITE        287
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT   MOD_RES         125
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H8M7"
FT   VAR_SEQ         1..295
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12498619, ECO:0000303|Ref.2"
FT                   /id="VSP_031040"
SQ   SEQUENCE   445 AA;  49725 MW;  F30B4A5E357AF52E CRC64;
     MSELTKELME LVWGTKSSPG LSDTIFCRWT QGFVFSESEG SALEQFEGGP CAVIAPVQAF
     LLKKLLFSSE KSSWRDCSEE EQKELLCHTL CDILESACCD HSGSYCLVSW LRGKTTEETA
     SISGSPAESS CQVEHSSALA VEELGFERFH ALIQKRSFRS LPELKDAVLD QYSMWGNKFG
     VLLFLYSVLL TKGIENIKNE IEDASEPLID PVYGHGSQSL INLLLTGHAV SNVWDGDREC
     SGMKLLGIHE QAAVGFLTLM EALRYCKVGS YLKSPKFPIW IVGSETHLTV FFAKDMALVA
     PEAPSEQARR VFQTYDPEDN GFIPDSLLED VMKALDLVSD PEYINLMKNK LDPEGLGIIL
     LGPFLQEFFP DQGSSGPESF TVYHYNGLKQ SNYNEKVMYV EGTAVVMGFE DPMLQTDDTP
     IKRCLQTKWP YIELLWTTDR SPSLN