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Database: UniProt
Entry: H3BVR3_TETNG
LinkDB: H3BVR3_TETNG
Original site: H3BVR3_TETNG 
ID   H3BVR3_TETNG            Unreviewed;       704 AA.
AC   H3BVR3;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000000075.1, ECO:0000313|Proteomes:UP000007303};
RN   [1] {ECO:0000313|Proteomes:UP000007303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
RN   [2] {ECO:0000313|Ensembl:ENSTNIP00000000075.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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   STRING; 99883.ENSTNIP00000000075; -.
DR   Ensembl; ENSTNIT00000001234.1; ENSTNIP00000000075.1; ENSTNIG00000000061.1.
DR   GeneTree; ENSGT00940000158045; -.
DR   HOGENOM; CLU_013907_0_0_1; -.
DR   InParanoid; H3BVR3; -.
DR   OMA; YVAKWAC; -.
DR   TreeFam; TF323312; -.
DR   Proteomes; UP000007303; 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:0007420; P:brain development; IEA:Ensembl.
DR   GO; GO:0021551; P:central nervous system morphogenesis; IEA:Ensembl.
DR   Gene3D; 1.25.40.560; -; 1.
DR   Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 1.
DR   Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR   InterPro; IPR041294; AnkUBD.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR001876; Znf_RanBP2.
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   SMART; SM00547; ZnF_RBZ; 3.
DR   PROSITE; PS01358; ZF_RANBP2_1; 2.
DR   PROSITE; PS50199; ZF_RANBP2_2; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022807};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007303};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00322}.
FT   DOMAIN          89..118
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          156..185
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   REGION          190..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..205
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   704 AA;  79726 MW;  E6E48A944A23A40A CRC64;
     MTELVSKWAC EYCTYENWPS AKCTMCHAQR PSRGAIITEE PFKSSPALDA SLHISADLSN
     SPSQGGSSLL ICPDSSARPR VRIADVPEIS SKWSCHMCTY LNWPRAIRCT QCLCQRQPRS
     PTESPQTSGT GCRPTRPAIT ADPCEEYNDR NRLNTHAQHW TCAACTYENW AKALKCVVCD
     HPKPNSLLAE PIQLASESES QQPSVKLNEQ DRDNRLGGCS SSKRRSPPTS KRESDVNMDF
     QRIEVASGAG IGSKEELEVD FKKLKQIKNR MRRTDWLFLN ACVAVVEGDL AAVEAYKSSG
     GDIARQLTAD EVRLLNRPSA FDDGFTLVHL AIRFQRQDML AVLLTEVSQQ AAKCIPAMVC
     PELTEQIRRE VAASLHQRKG DFTCYFLTDL VTFTLPAGQW SRGSQEQNAG VGCFQGLTLL
     VYEAERRARW LLATPATLLA PSLFPPPAKN ELLFCVWXVF TQLNDLWCNA RVFYTRWKEW
     ESWYSQSFGL HFSLREEQWQ EDWAFILSLA SQPGSSLEQT HIFVLAHILR RPIIVYGVKY
     YKSFRGETLG YTRFQGVYLP LLWEQSFCWK SPIALGYTRG HFSALVAMEN DGFDNRGAGA
     NLNTDDDVTV TFLPLVDSER KLLHVHFLSA QEMGNQEQQE KLLREWLDCC VTEGGLLVAL
     QKSSRRRNHP LVTQMVEKWL DGYRQIRPCT SLSDGEEEEE DDDE
//
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