ID G9KWG2_MUSPF Unreviewed; 335 AA.
AC G9KWG2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU361215};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU361215};
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:AES09241.1};
RN [1] {ECO:0000313|EMBL:AES09241.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Lungs {ECO:0000313|EMBL:AES09241.1};
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 -!- 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|ARBA:ARBA00000707,
CC ECO:0000256|RuleBase:RU361215};
CC -!- SIMILARITY: Belongs to the peptidase C12 family.
CC {ECO:0000256|ARBA:ARBA00009326, ECO:0000256|RuleBase:RU361215}.
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DR EMBL; JP020643; AES09241.1; -; mRNA.
DR MEROPS; C12.005; -.
DR GO; GO:0031011; C:Ino80 complex; IEA:InterPro.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0070628; F:proteasome binding; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd02255; Peptidase_C12; 1.
DR Gene3D; 1.20.58.860; -; 1.
DR Gene3D; 3.40.532.10; Peptidase C12, ubiquitin carboxyl-terminal hydrolase; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001578; Peptidase_C12_UCH.
DR InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR InterPro; IPR017390; Ubiquitinyl_hydrolase_UCH37.
DR InterPro; IPR033837; UCH37.
DR InterPro; IPR041507; UCH_C.
DR PANTHER; PTHR10589; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR10589:SF16; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE ISOZYME L5; 1.
DR Pfam; PF01088; Peptidase_C12; 1.
DR Pfam; PF18031; UCH_C; 1.
DR PIRSF; PIRSF038120; Ubiquitinyl_hydrolase_UCH37; 1.
DR PRINTS; PR00707; UBCTHYDRLASE.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
PE 2: Evidence at transcript level;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361215};
KW Protease {ECO:0000256|RuleBase:RU361215};
KW Thiol protease {ECO:0000256|RuleBase:RU361215};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU361215}.
FT DOMAIN 15..216
FT /note="Ubiquitin carboxyl-terminal hydrolase family 1
FT cysteine active-site"
FT /evidence="ECO:0000259|Pfam:PF01088"
FT DOMAIN 272..316
FT /note="Peptidase C12 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18031"
FT ACT_SITE 95
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR038120-1"
FT ACT_SITE 171
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038120-1"
FT SITE 186
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR038120-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AES09241.1"
FT NON_TER 335
FT /evidence="ECO:0000313|EMBL:AES09241.1"
SQ SEQUENCE 335 AA; 38028 MW; 0A86CDF92F5694CE CRC64;
GRCVAGAMTG NAGEWCLMES DPGVFTELIK GFGCRGAQVE EIWSLEPENF EKLKPVHGLI
FLFKWQPGEE PAGSVVQDSR LDTIFFAKQV INNACATQAI VSVLLNCTHQ DVHLGETLSE
FKEFSQSFDA AMKGLALSNS DVIRQVHNSF ARQQMFEFDA KTSAKEEDAF HFVSYVPVNG
RLYELDGLRE GPIDLGACNQ DDWISAVRPV IEKRIQKYSE GEIRFNLMAI VSDRKMIYEQ
KIAELQRQLA XXEPMDTDQG SNMLSAIQSE VAKNQMLIEE EVQKLKRYKI ENIRRKHNYL
PFIMELLKTL AEHQQLIPLV EKAKEKQNAK KAQET
//
