ID   MINY4_XENTR             Reviewed;         746 AA.
AC   Q0VA42;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 53.
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   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC121261; AAI21262.1; -; mRNA.
DR   RefSeq; NP_001072940.1; NM_001079472.1.
DR   AlphaFoldDB; Q0VA42; -.
DR   STRING; 8364.ENSXETP00000056614; -.
DR   PaxDb; Q0VA42; -.
DR   PRIDE; Q0VA42; -.
DR   Ensembl; ENSXETT00000056614; ENSXETP00000056614; ENSXETG00000010688.
DR   GeneID; 780771; -.
DR   KEGG; xtr:780771; -.
DR   CTD; 84182; -.
DR   Xenbase; XB-GENE-6456867; mindy4.
DR   eggNOG; KOG2871; Eukaryota.
DR   InParanoid; Q0VA42; -.
DR   OrthoDB; 1276386at2759; -.
DR   Proteomes; UP000008143; Chromosome 6.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000010688; Expressed in testis and 15 other tissues.
DR   ExpressionAtlas; Q0VA42; baseline.
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; Protease; Reference proteome; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN           1..746
FT                   /note="Probable ubiquitin carboxyl-terminal hydrolase
FT                   MINDY-4"
FT                   /id="PRO_0000320593"
FT   REGION          123..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          198..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          319..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..152
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        448
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT   ACT_SITE        666
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
SQ   SEQUENCE   746 AA;  82954 MW;  C5A28C2508756C1B CRC64;
     MEICYVQEVA SSLVREFLSR KGLKKTSLTL EEELPRAPRS ISTRNELRAA LHLDRLYKEN
     KLTEKPLKTL LEIMTKYFLE HSGKTKALNM RGEQNPAPPK GLATNLQQRH AGDLMMAVCD
     VSDDETGESS AVSDTSKTEI YRSQNDLQFN KSNHLKGPDR KQKQTEAGVT STGVCSEGEL
     MPPRVNIREH QERESWEMAL GAKSSRSETQ RPRSSRMVRG MMSGPTASSQ EDSLKKRGPR
     RSAAANTPNP IKGEVLSEIT GGMGEPSTIA PANTALKLGK EFAAKLLSTS ENLRNVSLCS
     TNAVPKPNAF AAAETAADGK GATEASPYAS NEHRRRSGFS NMDLNSASLA KKTLPFHRER
     NDKEDLKLDD VEDCLVTEEI RNIPTALPGN LKQIEGKPID LAQAVEIKKI LFGSSFCCFS
     DEWKIQSFTF NNNQPLRYGF IQKKGGPCGV LAAVQGCVLK NLLFGKDADL RVLQPSDSQR
     TSCLCKAIAD ILWRAGDNKE AVVALSCGRP QFSPAGRYKA DGILESLILY KIRKYEDLMG
     FVQQHISQFE LGPFGCTLLT LSVVLSRSVE LVQKDFDVST NCLIGAHSYC TQELVNLILS
     GRAVSNVFND VVELDSGNGN ITLLRGVAHR TDIGFLSLFE HYNVCQVGSY LKTPRFPIWV
     ICSESHFSVL FCVRRELMSD WKMERRFDLY YYDGLANQQD EIRLTVDTAA TYIEEQENDL
     TPPLEHCIRT KWKGAVIDWN GTEPIL