Gene
gstz1
- ID
- ZDB-GENE-040718-184
- Name
- glutathione S-transferase zeta 1
- Symbol
- gstz1 Nomenclature History
- Previous Names
-
- zgc:113898
- zgc:92869
- Type
- protein_coding_gene
- Location
- Chr: 17 Mapping Details/Browsers
- Description
- Enables glutathione transferase activity. Predicted to be involved in L-phenylalanine catabolic process and glutathione metabolic process. Predicted to act upstream of or within tyrosine catabolic process. Predicted to be located in cytoplasm. Predicted to be active in mitochondrion. Is expressed in brain; gill; liver; and pleuroperitoneal region. Orthologous to human GSTZ1 (glutathione S-transferase zeta 1).
- Genome Resources
- Note
- None
- Comparative Information
-
- All Expression Data
- 10 figures from 3 publications
- Cross-Species Comparison
- High Throughput Data
- Thisse Expression Data
-
- MGC:113898 (2 images)
Wild Type Expression Summary
- All Phenotype Data
- No data available
- Cross-Species Comparison
- Alliance
Phenotype Summary
Mutations
No data available
Human Disease
Disease Ontology Term | Multi-Species Data | OMIM Term | OMIM Phenotype ID |
---|---|---|---|
[Maleylacetoacetate isomerase deficiency] | 617596 |
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Domain, Family, and Site Summary
Type | InterPro ID | Name |
---|---|---|
Domain | IPR004045 | Glutathione S-transferase, N-terminal |
Domain | IPR004046 | Glutathione S-transferase, C-terminal |
Domain | IPR010987 | Glutathione S-transferase, C-terminal-like |
Domain | IPR034330 | Glutathione S-transferases, class Zeta , C-terminal |
Domain | IPR034333 | Glutathione S-transferases, class Zeta , N-terminal |
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Domain Details Per Protein
Protein | Length | Glutathione S-transferase, C-terminal | Glutathione S-transferase, C-terminal domain superfamily | Glutathione S-transferase, C-terminal-like | Glutathione S-transferase, N-terminal | Glutathione S-transferases, class Zeta | Glutathione S-transferases, class Zeta , C-terminal | Glutathione S-transferases, class Zeta , N-terminal | Glutathione transferase family | Thioredoxin-like superfamily |
---|---|---|---|---|---|---|---|---|---|---|
UniProtKB:X1WBU0
|
216 | |||||||||
UniProtKB:X1WD04
|
160 | |||||||||
UniProtKB:Q6DGL3
|
220 |
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Interactions and Pathways
No data available
Plasmids
No data available
No data available
Relationship | Marker Type | Marker | Accession Numbers | Citations |
---|---|---|---|---|
Contained in | Fosmid | ZFOS-810H6 | ZFIN Curated Data | |
Encodes | cDNA | MGC:92869 | ZFIN Curated Data | |
Encodes | cDNA | MGC:113898 | ZFIN Curated Data | |
Encodes | cDNA | MGC:191161 | ZFIN Curated Data |
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Type | Accession # | Sequence | Length (nt/aa) | Analysis |
---|---|---|---|---|
RNA | RefSeq:NM_001030271 (1) | 1058 nt | ||
Genomic | GenBank:FO704844 (1) | 95469 nt | ||
Polypeptide | UniProtKB:Q6DGL3 (1) | 220 aa |
- Tierbach, A., Groh, K.J., Schoenenberger, R., Schirmer, K., Suter, M.J. (2020) Biotransformation capacity of zebrafish (Danio rerio) early life stages: Functionality of the mercapturic acid pathway. Toxicological sciences : an official journal of the Society of Toxicology. 176(2):355-365
- Tierbach, A., Groh, K.J., Schönenberger, R., Schirmer, K., Suter, M.J. (2018) Glutathione S-transferase protein expression in different life stages of zebrafish (Danio rerio). Toxicological sciences : an official journal of the Society of Toxicology. 162(2):702-712
- Abunnaja, M.S., Kurogi, K., Mohammed, Y.I., Sakakibara, Y., Suiko, M., Hassoun, E.A., Liu, M.C. (2017) Identification and characterization of the zebrafish glutathione S-transferase Pi-1. Journal of biochemical and molecular toxicology. 31(10)
- Bayés, À., Collins, M.O., Reig-Viader, R., Gou, G., Goulding, D., Izquierdo, A., Choudhary, J.S., Emes, R.D., Grant, S.G. (2017) Evolution of complexity in the zebrafish synapse proteome. Nature communications. 8:14613
- Garcia-Reyero, N., Escalon, L., Prats, E., Faria, M., Soares, A.M., Raldúa, D. (2016) Targeted Gene Expression in Zebrafish Exposed to Chlorpyrifos-Oxon Confirms Phenotype-Specific Mechanisms Leading to Adverse Outcomes. Bulletin of environmental contamination and toxicology. 96(6):707-713
- Elkon, R., Milon, B., Morrison, L., Shah, M., Vijayakumar, S., Racherla, M., Leitch, C.C., Silipino, L., Hadi, S., Weiss-Gayet, M., Barras, E., Schmid, C.D., Ait-Lounis, A., Barnes, A., Song, Y., Eisenman, D.J., Eliyahu, E., Frolenkov, G.I., Strome, S.E., Durand, B., Zaghloul, N.A., Jones, S.M., Reith, W., Hertzano, R. (2015) RFX transcription factors are essential for hearing in mice. Nature communications. 6:8549
- Glisic, B., Mihaljevic, I., Popovic, M., Zaja, R., Loncar, J., Fent, K., Kovacevic, R., Smital, T. (2015) Characterization of glutathione-S-transferases in zebrafish (Danio rerio). Aquatic toxicology (Amsterdam, Netherlands). 158C:50-62
- Timme-Laragy, A.R., Goldstone, J.V., Imhoff, B.R., Stegeman, J.J., Hahn, M.E., and Hansen, J.M. (2013) Glutathione redox dynamics and expression of glutathione-related genes in the developing embryo. Free radical biology & medicine. 65:89-101
- Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G., Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D., Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K., Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F., Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L., Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L., Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S., Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J., Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J., McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S., Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W., Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A., Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y., Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M., Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E., Schnerch,A., Schein,J.E., Jones,S.J., and Marra,M.A. (2002) Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proceedings of the National Academy of Sciences of the United States of America. 99(26):16899-903
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