ID G3VT53_SARHA Unreviewed; 675 AA.
AC G3VT53;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 2.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=ZRANB1 {ECO:0000313|Ensembl:ENSSHAP00000006358.2};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000006358.2, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000006358.2, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000006358.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- SIMILARITY: Belongs to the peptidase C64 family.
CC {ECO:0000256|ARBA:ARBA00005865}.
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DR AlphaFoldDB; G3VT53; -.
DR MEROPS; C64.004; -.
DR Ensembl; ENSSHAT00000006413.2; ENSSHAP00000006358.2; ENSSHAG00000005534.2.
DR GeneTree; ENSGT00940000158045; -.
DR HOGENOM; CLU_013907_0_0_1; -.
DR OrthoDB; 2909231at2759; -.
DR Proteomes; UP000007648; 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 GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd22767; OTU_ZRANB1; 1.
DR Gene3D; 1.25.40.560; -; 1.
DR Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 3.
DR InterPro; IPR041294; AnkUBD.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR InterPro; IPR049768; ZRANB1_OTU.
DR PANTHER; PTHR13367; UBIQUITIN THIOESTERASE; 1.
DR PANTHER; PTHR13367:SF28; UBIQUITIN THIOESTERASE ZRANB1; 1.
DR Pfam; PF18418; AnkUBD; 1.
DR Pfam; PF02338; OTU; 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; PS50802; OTU; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 3.
DR PROSITE; PS50199; ZF_RANBP2_2; 3.
PE 3: Inferred from homology;
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:UP000007648};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW 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 DOMAIN 432..592
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT REGION 114..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 675 AA; 76580 MW; 5DCD27D606C80FCD CRC64;
MSERGIKWAC EYCTYENWPS AIKCTMCRAQ RPSGTIITED PFKSGSSDVG RDWDPSVTEG
GSSPLICPDS SARPRVKSSY TVENANKWSC HMCTYLNWPR AIRCTQCLSQ RRTRSPTESP
QSSGSGSRPA PFSVDPCEEY NDRNKLNTRT QHWTCSVCTY ENWAKARKCV VCDHPRPNNI
EAIELAETEE ASSLINEQDR TRWRGSCSGG NSQRRSPPTP QRDSEMNMDF QRIELAGAVG
SKEELEVDFK KLKQIKNRMK KTDWLFLNAC VGVVEGDLAA IEAYKSSGGD IARQLTADEV
RLLNRPSAFD VGYTLVHLAI RFQRQDMLAI LLTEVSQHAA KCIPAMVCPE LTEQIRREIA
ASLHQRKGDF ACYFLTDLVT FTLPADIEDL PPSVQEKLFD EVLDRDVQKE LEEESPIINW
SLELATRLDS RLYALWNRTA GDCLLDSVLQ ATWGIYDKDS VLRKALHDSL HDCSHWFYTR
WKEWESWYSQ SFGLHFSLRE EQWQEDWAFI LSLASQPGAS LEQTHIFVLA HILRRPIIVY
GVKYYKSFRG ETLGYTRFQG VYLPLLWEQS FCWKSPIALG YTRGHFSALV AMENDGYGNR
GAGANLNTDD DVTITFLPLV DSERKLLHIH FLSAQEVRSR LVNPGGVPLW AEFRNGSSTA
TPAPGLHVKS GPFST
//
