ID L9L4L3_TUPCH Unreviewed; 478 AA.
AC L9L4L3;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=TREES_T100012937 {ECO:0000313|EMBL:ELW69689.1};
OS Tupaia chinensis (Chinese tree shrew).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX NCBI_TaxID=246437 {ECO:0000313|EMBL:ELW69689.1, ECO:0000313|Proteomes:UP000011518};
RN [1] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhang G., Fan Y., Yao Y., Huang Z.;
RT "Genome of the Chinese tree shrew, a rising model animal genetically
RT related to primates.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23385571; DOI=10.1038/ncomms2416;
RA Fan Y., Huang Z.Y., Cao C.C., Chen C.S., Chen Y.X., Fan D.D., He J.,
RA Hou H.L., Hu L., Hu X.T., Jiang X.T., Lai R., Lang Y.S., Liang B.,
RA Liao S.G., Mu D., Ma Y.Y., Niu Y.Y., Sun X.Q., Xia J.Q., Xiao J.,
RA Xiong Z.Q., Xu L., Yang L., Zhang Y., Zhao W., Zhao X.D., Zheng Y.T.,
RA Zhou J.M., Zhu Y.B., Zhang G.J., Wang J., Yao Y.G.;
RT "Genome of the Chinese tree shrew.";
RL Nat. Commun. 4:1426-1426(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};
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DR EMBL; KB320524; ELW69689.1; -; Genomic_DNA.
DR AlphaFoldDB; L9L4L3; -.
DR STRING; 246437.L9L4L3; -.
DR eggNOG; KOG4345; Eukaryota.
DR InParanoid; L9L4L3; -.
DR Proteomes; UP000011518; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.560; -; 1.
DR Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 3.
DR InterPro; IPR041294; AnkUBD.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR13367; UBIQUITIN THIOESTERASE; 1.
DR PANTHER; PTHR13367:SF28; UBIQUITIN THIOESTERASE ZRANB1; 1.
DR Pfam; PF18418; AnkUBD; 1.
DR Pfam; PF00641; zf-RanBP; 2.
DR SMART; SM00547; ZnF_RBZ; 3.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 3.
DR PROSITE; PS01358; ZF_RANBP2_1; 3.
DR PROSITE; PS50199; ZF_RANBP2_2; 3.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000011518};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT DOMAIN 3..33
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 84..113
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 149..178
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT REGION 38..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 478 AA; 53904 MW; F8EA1917C0B3B7E7 CRC64;
MSERGIKWAC EYCTYENWPS AIKCTMCRAQ RPSGTIITED PFKSGSSDVG RDWDPSSTEG
GSSPLICPDS SARPRVKSSY SMENANKWSC HMCTYLNWPR AIRCTQCLSQ RRTRSPTESP
QSSGSGSRPV AFSVDPCEEY NDRNKLNTRT QHWTCSICTY ENWAKAKKCV VCDHPRPNNI
EAIELAETEE ASSIINEQDR ARWRGSCSSG NSQRRSPPTT KRDSEVKMDF QRIELAGAVG
SKEELEVDFK KLKQIKNRMK KTDWLFLNAC VDIVESIENT VTGILSNTWV PEIVPADSKS
TLTPQHKPCC DVTATIELQG SVELAHVGSG VYLPLLWEQS FCWKSPIALG YTRGHFSALV
AMENDGYGNR GAGANLNTDD DVTITFLPLV DSERKLLHVH FLSAQELGNE EQQEKLLREW
LDCCVTEGGV LVAMQKSSRR RNHPLVTQMV EKWLDRYRQI RPCTSLSDGE EDEDDEDE
//
