ID   MINY1_PONAB             Reviewed;         469 AA.
AC   Q5R7G8;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 56.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR860149; CAH92292.1; -; mRNA.
DR   RefSeq; NP_001127534.1; NM_001134062.2.
DR   AlphaFoldDB; Q5R7G8; -.
DR   SMR; Q5R7G8; -.
DR   STRING; 9601.ENSPPYP00000001032; -.
DR   GeneID; 100174611; -.
DR   KEGG; pon:100174611; -.
DR   CTD; 55793; -.
DR   eggNOG; KOG2427; Eukaryota.
DR   InParanoid; Q5R7G8; -.
DR   Proteomes; UP000001595; Unplaced.
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; IEA:InterPro.
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_0000344039"
FT   REGION          1..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..426
FT                   /note="Ubiquitin-binding domain (UBD)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT   REGION          428..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..51
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..469
FT                   /note="Basic and acidic 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            412
FT                   /note="Ubiquitin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT   SITE            415..416
FT                   /note="Ubiquitin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT   SITE            419
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;  51702 MW;  49A2DEA95FCAD350 CRC64;
     MEHHQPEDPA PGKAGTVEAD IPKNHEVLAG PYEHPQDTDA RDADGEAGER EPADQALLPS
     QCGDNLESPL PEAGSAPPGP TLGTLPEVET IKACSMPQEL PQSPRTRQPE PDFYCVKWIP
     WKGERTPIIT QSTNGPCPLL AIMNILFLQW KVKLPPQKEV ITSDELMAHL GNCLLSIKPQ
     EKSEGLQLNF QQNVDDAMTV LPKLATGLDV NARFTGVSDF EYTPECSVFD LLGIPLYHGW
     LVDPQSPEAV RAVGKLSYNQ LVERIITCKH SSDTNLVTKG LVAEQFLETT AAQLTYHGLC
     ELTAAAKEGE LSVFFRNNHF STMTKHKSHL YLLVTDQGFL QEEQIVWESL HNVDGDSCFC
     DSDFHLSHSL GKGPGAEGGS GSPEKQLQVD QDYLIALSLQ QQQPRGTLGL TDLELAQQLQ
     QEEYQQQQAA QPVWMRTRAL SPQGRGATSG RPAGERRQRP KHESDCILL