ID H3DBZ5_TETNG Unreviewed; 623 AA.
AC H3DBZ5;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
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:ENSTNIP00000018038.1, 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:ENSTNIP00000018038.1}
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};
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DR AlphaFoldDB; H3DBZ5; -.
DR STRING; 99883.ENSTNIP00000018038; -.
DR Ensembl; ENSTNIT00000018262.1; ENSTNIP00000018038.1; ENSTNIG00000014989.1.
DR GeneTree; ENSGT00950000183159; -.
DR HOGENOM; CLU_425517_0_0_1; -.
DR InParanoid; H3DBZ5; -.
DR TreeFam; TF316166; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0030155; P:regulation of cell adhesion; IEA:InterPro.
DR GO; GO:0023051; P:regulation of signaling; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd09616; Peptidase_C12_UCH_L1_L3; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR Gene3D; 3.40.532.10; Peptidase C12, ubiquitin carboxyl-terminal hydrolase; 1.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR031865; DUF4757.
DR InterPro; IPR029978; LMO-7.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001578; Peptidase_C12_UCH.
DR InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR PANTHER; PTHR46767; LIM DOMAIN ONLY PROTEIN 7; 1.
DR PANTHER; PTHR46767:SF1; LIM DOMAIN ONLY PROTEIN 7; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF15949; DUF4757; 1.
DR Pfam; PF01088; Peptidase_C12; 1.
DR PRINTS; PR00707; UBCTHYDRLASE.
DR SMART; SM00033; CH; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00140; UCH_1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000007303};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 223..345
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT REGION 482..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 623 AA; 69921 MW; E41B68C371DF1DB0 CRC64;
MDPPRWLPLE SNPEVITKFG ISLGIKPSWQ FVDVYGLDPE ALSTIPKPVC AVLLLFPVTD
AYEAFKQEEE DRLKQQPQDV SPDVYFIKQT IGNACGTIGL IHAVANNQEC LEFDSDSTLM
KFIEQTSKLT PGERAALLEK DESIRVTHES SAQEGQTEAP SLDEKVNLHF IAFVNVGGRL
YELEHYASIS HLRLISFFCL CETLCRLSVT TESAAESVKI LLLSIRAGMR TLSSSTASEE
VTKKTFGSND FRSALENGIL LCDVINRIKP GTIKRVNRLP TPIAGLDNLN VFLRACLKLG
LKEAQLFHPG DLQDLSTRVT VKDQETNRRL KNVLITIYWL GRQAQCDQSY DGPYLNFKAF
EGLLGTALYK KKALHDTSSL KGSSIRDSGF GDSWYAEREE QPHLHKRDNS LDSLNSLSSQ
AHSISSDTTI KGSSEGCCSD TEADAVFKMN DNTQNISYRR SVSITPKSST AFNQFLPTKD
KSSGYVPAPL RKKRAERNED SRHSWASAST EDDHTLTRYC YNAHNGKPLK LFGVSSSVFE
HKSKMEVYDD SEDEDDEVGY ADPIQDDLYA RKMGHKSQPF GNDCHDQFLP KLWTPDEDSH
IQKVKIGSQR RPWYKKIQGF RSV
//
