ID   M1ESN4_MUSPF            Unreviewed;       491 AA.
AC   M1ESN4;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU367139};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU367139};
DE   Flags: Fragment;
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|EMBL:AER98342.1};
RN   [1] {ECO:0000313|EMBL:AER98342.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Lungs {ECO:0000313|EMBL:AER98342.1};
RX   PubMed=23236062; DOI=10.1128/JVI.02476-12;
RA   Leon A.J., Banner D., Xu L., Ran L., Peng Z., Yi K., Chen C., Xu F.,
RA   Huang J., Zhao Z., Lin Z., Huang S.H., Fang Y., Kelvin A.A., Ross T.M.,
RA   Farooqui A., Kelvin D.J.;
RT   "Sequencing, annotation, and characterization of the influenza ferret
RT   infectome.";
RL   J. Virol. 87:1957-1966(2013).
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:0000256|RuleBase:RU367139}.
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:0000256|RuleBase:RU367139};
CC   -!- SIMILARITY: Belongs to the MINDY deubiquitinase family. FAM63
CC       subfamily. {ECO:0000256|ARBA:ARBA00006616,
CC       ECO:0000256|RuleBase:RU367139}.
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DR   EMBL; JP009745; AER98342.1; -; mRNA.
DR   AlphaFoldDB; M1ESN4; -.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0140934; F:histone deubiquitinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:1990380; F:K48-linked deubiquitinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR007518; MINDY.
DR   InterPro; IPR033979; MINDY_domain.
DR   PANTHER; PTHR18063; NF-E2 INDUCIBLE PROTEIN; 1.
DR   PANTHER; PTHR18063:SF8; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE MINDY-2; 1.
DR   Pfam; PF04424; MINDY_DUB; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase {ECO:0000256|RuleBase:RU367139};
KW   Protease {ECO:0000256|RuleBase:RU367139};
KW   Thiol protease {ECO:0000256|RuleBase:RU367139};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU367139}.
FT   DOMAIN          145..267
FT                   /note="MINDY deubiquitinase"
FT                   /evidence="ECO:0000259|Pfam:PF04424"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          426..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..464
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..491
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AER98342.1"
FT   NON_TER         491
FT                   /evidence="ECO:0000313|EMBL:AER98342.1"
SQ   SEQUENCE   491 AA;  54541 MW;  EE557701D61470ED CRC64;
     AAGRSLLDSV SPASSPQVPG PCSSCPGLDL KENDLENPAA QKTPPRGQYK VTASPETAEA
     GADHGSGPAG DGAGAGAAVL PGAVPLCREE EEEGEEAQVL AVSASKERFP GQSVYHIKWI
     QWKEENTPII TQNENGPCPL LAILNVLLLA WKVKLPPMME IITAEQLMEY LGDYMLDAKP
     KEISEIQRLN YEQNMSDAMA ILHKLQTGLD VNVKFTGVRV FEYTPECIVF DLLDIPLYHG
     WLVDPQIDDI VKAVGNCSYN QLVEKIISCK QSDNSELVSE GFVAEQFLNN TATQLTYHGL
     CELTSTVQEG ELCVFFRNNH FSTMTKYKGL LYLLVTDQGF LTEEKVVWES LHNVDGDGNF
     CDSEFHLRPP SDPETVYRGQ QDQIDQDYLM ALSLQQEQQS QEINWEQIPE GISDLELAKK
     LQEEEDRRAS QYYQEQEQAA AAAASASTQA QQSQPAQASP SRRQPGNSER KRKEPREKDK
     EKEKDKNSCV I
//