ID   MINY1_RAT               Reviewed;         482 AA.
AC   Q5BJQ2;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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; BC091386; AAH91386.1; -; mRNA.
DR   RefSeq; NP_001020289.1; NM_001025118.1.
DR   RefSeq; XP_017446390.1; XM_017590901.1.
DR   AlphaFoldDB; Q5BJQ2; -.
DR   SMR; Q5BJQ2; -.
DR   STRING; 10116.ENSRNOP00000053218; -.
DR   jPOST; Q5BJQ2; -.
DR   PaxDb; Q5BJQ2; -.
DR   PRIDE; Q5BJQ2; -.
DR   Ensembl; ENSRNOT00000056380; ENSRNOP00000053218; ENSRNOG00000021131.
DR   GeneID; 310665; -.
DR   KEGG; rno:310665; -.
DR   UCSC; RGD:1559660; rat.
DR   CTD; 55793; -.
DR   RGD; 1559660; Mindy1.
DR   eggNOG; KOG2427; Eukaryota.
DR   GeneTree; ENSGT00390000016607; -.
DR   HOGENOM; CLU_022566_5_1_1; -.
DR   InParanoid; Q5BJQ2; -.
DR   OMA; NHEVPLG; -.
DR   OrthoDB; 1601180at2759; -.
DR   PhylomeDB; Q5BJQ2; -.
DR   TreeFam; TF314589; -.
DR   PRO; PR:Q5BJQ2; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000021131; Expressed in ovary and 20 other tissues.
DR   Genevisible; Q5BJQ2; RN.
DR   GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR   GO; GO:0016807; F:cysteine-type carboxypeptidase activity; ISO:RGD.
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; ISO:RGD.
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..482
FT                   /note="Ubiquitin carboxyl-terminal hydrolase MINDY-1"
FT                   /id="PRO_0000344040"
FT   REGION          1..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..441
FT                   /note="Ubiquitin-binding domain (UBD)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT   REGION          437..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..63
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..119
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        151
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT   ACT_SITE        333
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT   SITE            427
FT                   /note="Ubiquitin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT   SITE            430..431
FT                   /note="Ubiquitin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT   SITE            434
FT                   /note="Ubiquitin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT   MOD_RES         117
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT   MOD_RES         454
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
SQ   SEQUENCE   482 AA;  52729 MW;  76E655D252D72827 CRC64;
     MEQPQAECPA PSKTNSAETV ESEKHEALSG PEKHPQDKDG ADAAPEKHPQ DKDGADAHGE
     AGKQKSGDQT LPPVQDGGNL ECPPPEASSS PPGPACGIPS EVETTEACSR PQQLPQSPRI
     QQPDLDFYCV KWIPWKGERT PIITQSSNGP CPLLAIMNIL FLQWKVKLPP QKEVITSDEL
     LTHLGNCLLS IKPQEKSEGL QLNFQQNVGD AMTVLPKLAT GLDVNVRFTG VSDFEYTPEC
     SVFDLLGVPL YHGWLVDPQS PEAVSAVGKL SYNQLVEKII ICKHSSDSNL VTEGLIAEQF
     LETTAAQLTY HGLCELTATA KEDELSVFFR NNHFSTMTKH KSHLYLLVTD QGFLQEEQVV
     WESLHNVDGD SCFCDSDFHL SHSLGKSHGA EGGSGSPEKQ LQVDQDYLIA LSLQQQQQPQ
     GMLGLSDLEL AQQLQQEEYQ QQQAVQPVRT RAPSSPGRGA TSGRPAGERR QRSKTESDCV
     LL