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Database: UniProt
Entry: E3T9P3_SPHPU
LinkDB: E3T9P3_SPHPU
Original site: E3T9P3_SPHPU 
ID   E3T9P3_SPHPU            Unreviewed;       265 AA.
AC   E3T9P3;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE   Flags: Fragment;
GN   Name=VCPIP1 {ECO:0000313|EMBL:ADO30318.1};
OS   Sphenodon punctatus (Tuatara) (Hatteria punctata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Sphenodontia; Sphenodontidae; Sphenodon.
OX   NCBI_TaxID=8508 {ECO:0000313|EMBL:ADO30318.1};
RN   [1] {ECO:0000313|EMBL:ADO30318.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20930035; DOI=10.1093/sysbio/syq048;
RA   Wiens J.J., Kuczynski C.A., Townsend T., Reeder T.W., Mulcahy D.G.,
RA   Sites J.W.Jr.;
RT   "Combining phylogenomics and fossils in higher-level squamate reptile
RT   phylogeny: molecular data change the placement of fossil taxa.";
RL   Syst. Biol. 59:674-688(2010).
RN   [2] {ECO:0000313|EMBL:ADO30318.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wiens J.W., Kuczynski C.A., Townsend T., Reeder T.W., Mulcahy D.G.,
RA   Sites J.W.Jr.;
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
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; GU456182; ADO30318.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3T9P3; -.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR   CDD; cd22769; OTU_VCIP135; 1.
DR   Gene3D; 3.90.70.80; -; 1.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR039087; VCPIP1.
DR   InterPro; IPR045827; VCPIP1_N.
DR   PANTHER; PTHR14843; DEUBIQUITINATING PROTEIN VCIP135; 1.
DR   PANTHER; PTHR14843:SF2; DEUBIQUITINATING PROTEIN VCPIP1; 1.
DR   Pfam; PF02338; OTU; 1.
DR   Pfam; PF19437; VCIP135_N; 1.
DR   PROSITE; PS50802; OTU; 1.
PE   4: Predicted;
FT   DOMAIN          59..212
FT                   /note="OTU"
FT                   /evidence="ECO:0000259|PROSITE:PS50802"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADO30318.1"
FT   NON_TER         265
FT                   /evidence="ECO:0000313|EMBL:ADO30318.1"
SQ   SEQUENCE   265 AA;  29602 MW;  85D21F4AE3C7AADC CRC64;
     TEMNQGDVFD CSLLGDRAFL IEPEHVDTVG YGKDRSGSLL YLHDTLEDIK KTNSSQECLI
     PVHVDGDGHC LVHAVSRALV GRELFWHALR ENLKKHFMEN LNHYKALFHD FIDAAEWEDI
     ISECDPSFVP PEGVPLGLRN IHIFGLANVL HRPIILLDSL SGMRSSGDYS GTFLPGLIPE
     EKCMGKDGML NKPICIAWSS SGRNHYIPLV GIKGATLPKL PMKLIPKAWG VPQDLIKKYI
     KLEEDGCCVI GGDRSLQDKY LMRLV
//
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