ID G5AZG1_HETGA Unreviewed; 911 AA.
AC G5AZG1;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
DE Flags: Fragment;
GN ORFNames=GW7_11284 {ECO:0000313|EMBL:EHB02422.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB02422.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB02422.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
CC -!- FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin
CC from specific proteins to regulate different cellular processes.
CC {ECO:0000256|RuleBase:RU366025}.
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:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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DR EMBL; JH167615; EHB02422.1; -; Genomic_DNA.
DR AlphaFoldDB; G5AZG1; -.
DR STRING; 10181.G5AZG1; -.
DR MEROPS; C19.014; -.
DR eggNOG; KOG1870; Eukaryota.
DR InParanoid; G5AZG1; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR028135; Ub_USP-typ.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF29; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 11; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF14836; Ubiquitin_3; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366025};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 23..131
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 255..879
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHB02422.1"
SQ SEQUENCE 911 AA; 104315 MW; 8108D5CC95739D92 CRC64;
TDQAAAAVAT AAEDREPQRE EMPGLEDQWN QIENGESGRE RPLRAGESWF LVEQRWYKQW
EVYVQGGDQD ASTFPGCINN AELFEEQINW CLKEGLMEGK DYVLLPAAAW HYLVSWYGLE
HGQPPIERKV IELYSIPKVE VYPVKLLLVQ HGDTETVLTA QFSLADSVDL LLHTVREQFL
VDAEEDARLW VKNSEGCLDR LCNTHVTLLD AALETGQLVI MEIRNKDGSW PSTQLCVMSN
MAEEDEDFQG QPGICGLTNL GNTCFMNSTL QCLSSVPQLT EYFLDNRYLE ELNFCNPLGM
KGELAEAYAD LVKQTWSGCH RSVVPNVFKN KVSHFASQFL GYQQHDSQEL LSFLLDGLHE
DLNRVKKKEY VELCDAAGRP DQEVAQEAWQ NHKRRNDSVI VDTFHGLFKS TLVCPDCGNV
SVTFDPFCYL SVPLPVCHKR VLEVFFVPMD PRRKPEQHRV VVPKKGNISD LCMALSKHTG
VLPDKMIVAD VFSHRFYKLY QLEDPLSDIL DRDDIFVYEV SGRIEPIEGS KDDIVVPVYL
RERTPAQDYN SYYGLMLFGH PLLVSVPQDR LSWEGLYNIL MYRLSRYVTK PTSDEEDVGE
EKGEDGNSDE EEKDQMPGPS TVGNFRDSER EQAGPSSGTT GRCPFFLDNC FRTSHWPPER
RRKQLFTLQA VDSNGTSDRT TSPEEVDTQP YIAMDWEPEM KRRYYDEAEA EGYVKHECVD
YVLKKVPVQL QECIELFTTV ETLEKENPWY CSSCKQHQLA TKKLDLWMLP EILIIHLKRF
SFSKFSHEKL DTLVHFPIRD LDFSDFVIKP QNESAPELYK YDLIAVSNHY GGIRDGHYTT
FACNKDSGQW HYFDDSSVSP VNENQIESKA AYVLFYQRQD TVHRQSQPSS SSDLSSPACG
STLTPEFMDV N
//
