MINY2_BOVIN
ID MINY2_BOVIN Reviewed; 630 AA.
AC Q2KI23;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase MINDY-2;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme MINDY-2;
DE AltName: Full=Protein FAM63B;
GN Name=MINDY2; Synonyms=FAM63B;
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=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolase that can remove 'Lys-48'-linked conjugated
CC ubiquitin from proteins. Can also bind to polyubiquitin chains of
CC different linkage types, including 'Lys-6', 'Lys-11', 'Lys-29', 'Lys-
CC 33' and 'Lys-63'. May play a regulatory role at the level of protein
CC turnover. {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. FAM63
CC subfamily. {ECO:0000305}.
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DR EMBL; BC112797; AAI12798.1; -; mRNA.
DR RefSeq; NP_001039740.1; NM_001046275.2.
DR AlphaFoldDB; Q2KI23; -.
DR SMR; Q2KI23; -.
DR STRING; 9913.ENSBTAP00000016444; -.
DR PaxDb; Q2KI23; -.
DR PRIDE; Q2KI23; -.
DR Ensembl; ENSBTAT00000016444; ENSBTAP00000016444; ENSBTAG00000012391.
DR GeneID; 524749; -.
DR KEGG; bta:524749; -.
DR CTD; 54629; -.
DR VEuPathDB; HostDB:ENSBTAG00000012391; -.
DR VGNC; VGNC:31477; MINDY2.
DR eggNOG; KOG2427; Eukaryota.
DR GeneTree; ENSGT00390000016607; -.
DR HOGENOM; CLU_022566_3_1_1; -.
DR InParanoid; Q2KI23; -.
DR OMA; THLCPDN; -.
DR OrthoDB; 1601180at2759; -.
DR TreeFam; TF314589; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000012391; Expressed in conceptus and 110 other tissues.
DR ExpressionAtlas; Q2KI23; baseline and differential.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0016807; F:cysteine-type carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0071795; F:K11-linked polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0071796; F:K6-linked polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:1990380; F:Lys48-specific deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; IBA:GO_Central.
DR InterPro; IPR007518; MINDY.
DR InterPro; IPR033979; MINDY_domain.
DR PANTHER; PTHR18063; PTHR18063; 1.
DR Pfam; PF04424; MINDY_DUB; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Phosphoprotein; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..630
FT /note="Ubiquitin carboxyl-terminal hydrolase MINDY-2"
FT /id="PRO_0000344041"
FT REGION 1..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..560
FT /note="Ubiquitin-binding domain (UBD)"
FT /evidence="ECO:0000250|UniProtKB:Q8NBR6"
FT REGION 564..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 267
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT ACT_SITE 449
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT SITE 543
FT /note="Ubiquitin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT SITE 546..547
FT /note="Ubiquitin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT SITE 550
FT /note="Ubiquitin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NBR6"
SQ SEQUENCE 630 AA; 68118 MW; 533117075BA468C9 CRC64;
MESGPESLQP LEHGVAAGPA PGTGSPQEGQ QETRLAAGDG PGVWAAESSG GKGQGAAAGG
RSLSDSASPA GSPQVLVPCS SLPRLDLKES DLESPAAQKE PVRGQHKVTA SPETAEAGAD
HGLGPEGDGG ARPDPAGTCQ EESAAAGSSE PSSGGGLSSS CSDPSPPGES PSLDSLESFS
NLHSFPSSSE FNSEEGAENR VPEEEEGAAV LPGAVPLCGE EEVEEEEAQV LAASKERFPG
QSVYHIKWIQ WKEENTPIIT QNENGPCPLL AILNVLLLAW KVKLPPMMEI ITAEQLMEYL
GDYMLDTKPK EISEIQRLNY EQNMSDAMAV LHKLQTGLDV NVKFTGVRVF EYTPECIVFD
LLDIPLYHGW LVDPQIDDIV KAVGNCSYNQ LVEKIISCKQ SENSELVSEG FVAEQFLNNT
ATQLTYHGLC ELTSTVQEGE LCVFFRNNHF STMTKYKGLL YLLVTDQGFL TEEKVVWESL
HNVDGDGNFC DSEFHLRPPS DPETVYRGQQ DQIDQDYLMA LSLQQEQQSQ EINWEQIPEG
ISDLELAKKL QEEEDRRASQ YYQEQEQAAA AAASASASAS ASASTQAPQS QPVQASPSSG
RQSGNSERKR KEPREKDKEK EKEKNSCVIL
