ID   MINY4_BOVIN             Reviewed;         763 AA.
AC   A1A4L4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Probable ubiquitin carboxyl-terminal hydrolase MINDY-4;
DE            EC=3.4.19.12;
DE   AltName: Full=Probable deubiquitinating enzyme MINDY-4;
GN   Name=MINDY4; Synonyms=FAM188B;
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].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable hydrolase that can remove 'Lys-48'-linked conjugated
CC       ubiquitin from proteins. {ECO:0000250|UniProtKB:Q8NBR6}.
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:Q8NBR6};
CC   -!- SIMILARITY: Belongs to the MINDY deubiquitinase family. FAM188
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BC126671; AAI26672.1; -; mRNA.
DR   RefSeq; NP_001073788.1; NM_001080319.2.
DR   AlphaFoldDB; A1A4L4; -.
DR   STRING; 9913.ENSBTAP00000012360; -.
DR   PaxDb; A1A4L4; -.
DR   PRIDE; A1A4L4; -.
DR   GeneID; 615509; -.
DR   KEGG; bta:615509; -.
DR   CTD; 84182; -.
DR   eggNOG; KOG2871; Eukaryota.
DR   InParanoid; A1A4L4; -.
DR   OrthoDB; 1276386at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:1990380; F:Lys48-specific deubiquitinase activity; IBA:GO_Central.
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.
PE   2: Evidence at transcript level;
KW   Hydrolase; Phosphoprotein; Protease; Reference proteome; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN           1..763
FT                   /note="Probable ubiquitin carboxyl-terminal hydrolase
FT                   MINDY-4"
FT                   /id="PRO_0000320589"
FT   REGION          154..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..203
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..293
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..346
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        463
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT   ACT_SITE        683
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT   MOD_RES         143
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UQI9"
FT   MOD_RES         220
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q4G0A6"
FT   MOD_RES         224
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q4G0A6"
FT   MOD_RES         296
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q4G0A6"
SQ   SEQUENCE   763 AA;  84447 MW;  A48F30F6D98CC401 CRC64;
     MDTLFVEEVA ASLIREFLSR KGLKKTYVTM DQERPRSDLS INSRNDLRKV LHLEFLYKEN
     KAKENPLKTN LELITRYFLD HFGNIGNNVT QETRIPELSV PKKSNKLPLR SSETTLVNIY
     HLADEDETWR TSLSEISKAR HDSLDGDVLG HFVSSKRSSH KSRPIKTVAG ESPTVASAWE
     KTDKLPMSEP SLDTKRMGEK VRPKSGLIVR GMMAGPIASS PQDSLRKRSL RRSPALSSAT
     QPHKEGSPQE PELSTHTSTC PTPLEGPASS TASTSRSPQG PLSELTWEKQ RTSPGSPPHL
     PGKGLLPRGS GRWRDLSEDS PAVDSGSEAI RTPPKFSLSS GNVPKTQERP ERAFERQGSQ
     PASLRKNQLS VSNKLEGDLD VLQLEDVEDE LVREEIILSP VSSVLKLQVV SKPIDLSVAK
     DIKTILFGSS FCCFSDEWKL QSFSFNDSVS LKYGIVQNKG GPCGVLAAVQ GCVLQKLLFE
     GDSSADCARL QPSNARRTHC LALAIADIVW RAGGCERAVV TLASGTQHFS PTGKYKADGV
     LETLILHSLT CYEELVTFLQ QSIHQFEAGP YGCVLLTLSA ILSRSTELVR QDFDVPTSHL
     IGAHGYCTQE LVNLLLTGKA VSNVFNDVVE LDSGNGDVTL LKGISTRSDI GFLSLFEHYN
     VCQVGCFLKT PRFPIWVVCS ESHFSVLFSQ QLELLRDWRA ERLFDLYYYD GLANQQEQIR
     LTVDTTQTVP EDRDNGLVPP LELCNRTKWK GASVNWNGSE PIL