ID   MINY4_PONAB             Reviewed;         757 AA.
AC   Q5RF72;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 52.
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   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: 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}.
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DR   EMBL; CR857289; CAH89585.1; -; mRNA.
DR   RefSeq; NP_001124700.1; NM_001131228.1.
DR   AlphaFoldDB; Q5RF72; -.
DR   STRING; 9601.ENSPPYP00000019806; -.
DR   PRIDE; Q5RF72; -.
DR   GeneID; 100171547; -.
DR   KEGG; pon:100171547; -.
DR   CTD; 84182; -.
DR   eggNOG; KOG2871; Eukaryota.
DR   InParanoid; Q5RF72; -.
DR   OrthoDB; 1276386at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:1990380; F:Lys48-specific deubiquitinase activity; IEA:InterPro.
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; Phosphoprotein; Protease; Reference proteome; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN           1..757
FT                   /note="Probable ubiquitin carboxyl-terminal hydrolase
FT                   MINDY-4"
FT                   /id="PRO_0000320592"
FT   REGION          141..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          192..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..245
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..292
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..318
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        456
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT   ACT_SITE        677
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT   MOD_RES         219
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q4G0A6"
FT   MOD_RES         223
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q4G0A6"
FT   MOD_RES         289
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q4G0A6"
SQ   SEQUENCE   757 AA;  84416 MW;  C0427CD0B5F66BAA CRC64;
     MDSLFVEEVA ASLVREFLSR KGLKKTCVTM DQERPRSDLS INNRNDLRKV LHLEFLYKEN
     KAKENPLKTS LELITRYFLD HFGNTANNFT QDTPIPALSV PKKNNKVPSR CSETTLVNIY
     DLSDEDAGWR TSLSETSKAR HDNLDGDVLG NFVSSKRPPH KSKPMQTVPG ETPMLASAWE
     KMDKLHLEPS LDVKRMGENS RPKSGLIVRG MMSGPIASSP QDSFHRRSLR RSLPSSSSTQ
     PQEESRKVPE LFIRTQQDIL ASSNSSPSRT SLGQLSELTV EKEKTTASSP PHLPSKRLPP
     RDRARRRDPS EDTLAVDSST DADRMPLKLY LPGGNSRMTQ ERLERAFKRQ GSQPVPVRKN
     QLLLSDKADG ELGTLRLEDV EDELIREEVI LSPVPSVLKL QTASKPIDLS VAKEIKTLLF
     GSSFCCFNEE WKLQSFSFSN TASLKYGIVQ NKGGPCGVLA AVQGCVLQKL LFEGDSKADC
     ARGLQPSDAH RTRCLVLALA DIVWRAGGRE RAVVALASRT QQFSPTGKYK ADGVLETLTL
     HSLTCYGDLV TFLQQSIHQF EVGPHGCILL TLSAILSRST ELIRQDFDVP TSHLIGAHGY
     CTQELVNLLL TGKAVSNVFN DVVELDSGDG NITLLRGIAA RSDIGFLSLF EHYNVCQVGC
     FLKTPRFPIW VVCSESHFSI LFSLQPGLLR DWRTERLFDL YYYDGLANQQ EQIRLTIDTT
     QTISEDTDND LVPPLELCIR TKWKGASVNW NGSDPIL