ID G7MXJ8_MACMU Unreviewed; 623 AA.
AC G7MXJ8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU367139};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU367139};
GN ORFNames=EGK_17532 {ECO:0000313|EMBL:EHH27355.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:EHH27355.1};
RN [1] {ECO:0000313|EMBL:EHH27355.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-5 {ECO:0000313|EMBL:EHH27355.1};
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
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}.
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; CM001259; EHH27355.1; -; Genomic_DNA.
DR AlphaFoldDB; G7MXJ8; -.
DR Proteomes; UP000013456; Chromosome 7.
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 3: Inferred from homology;
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 275..397
FT /note="MINDY deubiquitinase"
FT /evidence="ECO:0000259|Pfam:PF04424"
FT REGION 1..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 623 AA; 67237 MW; 06FB1DA3D3BF4D7E CRC64;
MESSPESLQP LEHGVAAGPA SGTGSSQEGL QETRLAAGDG PGVGAAESSG GNGLGAAAAS
RSLPDSASPA GSPEVPGPCS SSPGLDLKDS GVESPAAAEA PLRGQYKVTA SPETAVAGVG
HELGPAGDAG DRPDLAGTCQ AELTAAGSEE PSSAGGLSSS CSDPTPPGES PSLDSLESFS
NLHSFPSSCE FNSEEGAENR VPEEEEGAAV LPGAVPLCKG EEEEEEETAQ VLAASKERFP
GQSVYHIKWI QWKEENTPII TQNENGPCPL LAILNVLLLA WKVKLPPMME IITAEQLMEY
LGDYMLDAKP KEISEIQRLN YEQNMSDAMA ILHKLQTGLD VNVRFTGVRV FEYTPECIVF
DLLDIPLYHG WLVDPQIDDI VKAVGNCSYN QLVEKIISCK QSDNSELVSE GFVAEQFLNN
TATQLTYHGL CELTSTVQEG ELCVFFRNNH FSTMTKYKGQ LYLLVTDQGF LTEEKVVWES
LHNVDGDGNF CDSEFRLRPP SDPETVYKGQ QDQIDQDYLM ALSLQQEQQS QEINWEQIPE
GISDLELAKK LQEEEDRRAS QYYQEQEQAA AAAAAASTQA QQGQPAQASP SSGRQSGNSE
RKRKEPREKD KEKEKEKNSC VIL
//
