ID   K4GTY9_BROBR            Unreviewed;       265 AA.
AC   K4GTY9;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=VCPIP {ECO:0000313|EMBL:AFP57191.1};
OS   Brookesia brygooi (Brygoo's leaf chameleon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Acrodonta; Chamaeleonidae; Brookesia.
OX   NCBI_TaxID=179892 {ECO:0000313|EMBL:AFP57191.1};
RN   [1] {ECO:0000313|EMBL:AFP57191.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Lee I.-M., Bottner-Parker K.D., Zhao Y., Bertaccini A., Davis R.E.;
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AFP57191.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=22993238; DOI=10.1098/rsbl.2012.0703;
RA   Wiens J.J., Hutter C.R., Mulcahy D.G., Noonan B.P., Townsend T.M.,
RA   Sites J.W.Jr., Reeder T.W.;
RT   "Resolving the phylogeny of lizards and snakes (Squamata) with extensive
RT   sampling of genes and species.";
RL   Biol. Lett. 8:1043-1046(2012).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JN702935; AFP57191.1; -; Genomic_DNA.
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:AFP57191.1"
FT   NON_TER         265
FT                   /evidence="ECO:0000313|EMBL:AFP57191.1"
SQ   SEQUENCE   265 AA;  29722 MW;  026B25F623E5D2CF CRC64;
     REMNQGDVFD CALLGDRAFL IEPEHVETVG YGKDRSGSLL YLHDTLEDIK KANHSQECLI
     PVHVDGDGHC LVHAISRALV GRELFWHALR ENLKKHFIEN LNRYKALFHD FIDAAEWEDI
     INECDPLFVP PEGVPMGLRN IHIFGLANVL HRPIILLDSL SGMRSSGDYS ATFLPGLIPE
     ENCMGKDGML NKPIXIAWSS SGRNHYIPLV GIKGAALPKL PMKLLPKAWG VPQDLIKKYI
     RLEEDGGCVI GGDRSLQDKY LMRLV
//