ID   MINY1_BOVIN             Reviewed;         469 AA.
AC   Q2KJ22;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase MINDY-1;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme MINDY-1;
DE   AltName: Full=Protein FAM63A;
GN   Name=MINDY1; Synonyms=FAM63A;
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=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Hydrolase that can specifically remove 'Lys-48'-linked
CC       conjugated ubiquitin from proteins. Has exodeubiquitinase activity and
CC       has a preference for long polyubiquitin chains. May play a regulatory
CC       role at the level of protein turnover. {ECO:0000250|UniProtKB:Q8N5J2}.
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:Q8N5J2};
CC   -!- SIMILARITY: Belongs to the MINDY deubiquitinase family. FAM63
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BC105561; AAI05562.1; -; mRNA.
DR   RefSeq; NP_001039389.1; NM_001045924.1.
DR   AlphaFoldDB; Q2KJ22; -.
DR   SMR; Q2KJ22; -.
DR   STRING; 9913.ENSBTAP00000033701; -.
DR   PaxDb; Q2KJ22; -.
DR   PRIDE; Q2KJ22; -.
DR   GeneID; 505719; -.
DR   KEGG; bta:505719; -.
DR   CTD; 55793; -.
DR   eggNOG; KOG2427; Eukaryota.
DR   InParanoid; Q2KJ22; -.
DR   OrthoDB; 1601180at2759; -.
DR   Proteomes; UP000009136; Unplaced.
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:0036435; F:K48-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..469
FT                   /note="Ubiquitin carboxyl-terminal hydrolase MINDY-1"
FT                   /id="PRO_0000344036"
FT   REGION          1..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..428
FT                   /note="Ubiquitin-binding domain (UBD)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT   REGION          401..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..48
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..430
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        137
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT   ACT_SITE        319
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT   SITE            414
FT                   /note="Ubiquitin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT   SITE            417..418
FT                   /note="Ubiquitin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT   SITE            421
FT                   /note="Ubiquitin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT   MOD_RES         103
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT   MOD_RES         441
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
SQ   SEQUENCE   469 AA;  51289 MW;  6C92137E0A45F1DA CRC64;
     MEHHQPEHPA PGETRTAEAV SPENHKVLSE PKEHPQDKDA KEADGAAGEQ EPVDQASLPA
     QGQDNFESPP PDASSSQPGP ARETRPETET AGACSRLQEL PQSPRARQPE LDFYCVKWIP
     WKGEQTPIIT QSANGPCPLI AIANILFLQW KVKLPPQKEV ITSDELMAHL GDCLLSIKPQ
     EKSEGLQLNF QQNVDDAMTV LPKLATGLDV NVRFTGVSDF EYTPECSVFD LLGIPLYHGW
     LVDPQSPEAV SAVGKLSYNQ LVEKIITCKH SSDTNLVTEG LIAEQFLETT AAQLTYHGLC
     ELTAAAKEGE LSVFFRNNHF STMTKHKGHL YLLVTDQGFL QEEQVVWESL HNVDGDSCFC
     DSDFHLSHSP GKGPGTGGGS GSPEKQRQVD QDYLIALSLQ QQQPPPQGTS GLSDLELAQQ
     LQQEEYQQHQ AAQAAPARAP SPQGRGAASG RPAAERRQRP KQESDCVLL