Gene
bcat2
- ID
- ZDB-GENE-040718-425
- Name
- branched chain amino-acid transaminase 2, mitochondrial
- Symbol
- bcat2 Nomenclature History
- Previous Names
-
- fb37h12
- wu:fb37h12
- zgc:91919
- Type
- protein_coding_gene
- Location
- Chr: 3 Mapping Details/Browsers
- Description
- Predicted to enable branched-chain-amino-acid transaminase activity. Predicted to act upstream of or within amino acid biosynthetic process; branched-chain amino acid biosynthetic process; and lipid metabolic process. Predicted to be active in mitochondrion. Is expressed in liver and muscle. Human ortholog(s) of this gene implicated in hypervalinemia and hyperleucine-isoleucinemia. Orthologous to human BCAT2 (branched chain amino acid transaminase 2).
- Genome Resources
- Note
- None
- Comparative Information
-
- All Expression Data
- 2 figures from 2 publications
- Cross-Species Comparison
- High Throughput Data
- Thisse Expression Data
- No data available
Wild Type Expression Summary
- All Phenotype Data
- No data available
- Cross-Species Comparison
- Alliance
Phenotype Summary
Mutations
| Allele | Type | Localization | Consequence | Mutagen | Supplier |
|---|---|---|---|---|---|
| sa16687 | Allele with one point mutation | Unknown | Splice Site | ENU | |
| sa20027 | Allele with one point mutation | Unknown | Premature Stop | ENU | |
| sa33189 | Allele with one point mutation | Unknown | Premature Stop | ENU | |
| sa33190 | Allele with one point mutation | Unknown | Premature Stop | ENU |
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No data available
Human Disease
| Disease Ontology Term | Multi-Species Data | OMIM Term | OMIM Phenotype ID |
|---|---|---|---|
| hypervalinemia and hyperleucine-isoleucinemia | Alliance | Hypervalinemia and hyperleucine-isoleucinemia | 618850 |
Domain, Family, and Site Summary
| Type | InterPro ID | Name |
|---|---|---|
| Conserved_site | IPR018300 | Aminotransferase, class IV, conserved site |
| Family | IPR001544 | Aminotransferase class IV |
| Family | IPR005786 | Branched-chain amino acid aminotransferase II |
| Family | IPR033939 | Branched-chain aminotransferase |
| Homologous_superfamily | IPR036038 | Aminotransferase-like, PLP-dependent enzymes |
| Homologous_superfamily | IPR043131 | Branched-chain-amino-acid aminotransferase-like, N-terminal |
| Homologous_superfamily | IPR043132 | Branched-chain-amino-acid aminotransferase-like, C-terminal |
Domain Details Per Protein
| Protein | Additional Resources | Length | Aminotransferase class IV | Aminotransferase, class IV, conserved site | Aminotransferase-like, PLP-dependent enzymes | Branched-chain amino acid aminotransferase II | Branched-chain-amino-acid aminotransferase-like, C-terminal | Branched-chain-amino-acid aminotransferase-like, N-terminal | Branched-chain aminotransferase |
|---|---|---|---|---|---|---|---|---|---|
| UniProtKB:E9QCQ6 | InterPro | 406 | |||||||
| UniProtKB:E9QFU8 | InterPro | 391 |
Interactions and Pathways
No data available
Plasmids
No data available
No data available
| Relationship | Marker Type | Marker | Accession Numbers | Citations |
|---|---|---|---|---|
| Contained in | BAC | DKEY-197M10 | ZFIN Curated Data | |
| Encodes | EST | fb37h12 | ||
| Encodes | cDNA | MGC:91919 | ZFIN Curated Data | |
| Encodes | cDNA | MGC:192970 | ZFIN Curated Data |
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| Type | Accession # | Sequence | Length (nt/aa) | Analysis |
|---|---|---|---|---|
| RNA | RefSeq:NM_001002676 (1) | 3447 nt | ||
| Genomic | GenBank:CR384107 (1) | 51533 nt | ||
| Polypeptide | UniProtKB:E9QCQ6 (1) | 406 aa |
- Xi, L., Zhai, G., Liu, Y., Gong, Y., Lu, Q., Zhang, Z., Liu, H., Jin, J., Zhu, X., Yin, Z., Xie, S., Han, D. (2023) Attenuated glucose uptake promotes catabolic metabolism through activated AMPK signaling and impaired insulin signaling in zebrafish. Frontiers in nutrition. 10:11872831187283
- Wang, J.G., Zhao, S.H., Qian, Y.C., Qian, Y.F., Liu, Y.C., Qiao, F., Luo, Y., Zhang, M.L., Du, Z.Y. (2022) The dysfunction of hormone-sensitive lipase induces lipid deposition and reprogramming of nutrient metabolism. The British journal of nutrition. 130(4):588-603
- Li, L.Y., Li, J.M., Ning, L.J., Lu, D.L., Luo, Y., Ma, Q., Limbu, S.M., Li, D.L., Chen, L.Q., Lodhi, I.J., Degrace, P., Zhang, M.L., Du, Z.Y. (2020) Mitochondrial Fatty Acid β-Oxidation Inhibition Promotes Glucose Utilization and Protein Deposition through Energy Homeostasis Remodeling in Fish. The Journal of nutrition. 150(9):2322-2335
- Li, L.Y., Lv, H.B., Jiang, Z.Y., Qiao, F., Chen, L.Q., Zhang, M.L., Du, Z.Y. (2020) Peroxisomal proliferator-activated receptor α-b deficiency induces the reprogramming of nutrient metabolism in zebrafish. The Journal of physiology. 598(20):4537-4553
- 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
- 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
- Hugo, S.E., Cruz-Garcia, L., Karanth, S., Anderson, R.M., Stainier, D.Y., and Schlegel, A. (2012) A monocarboxylate transporter required for hepatocyte secretion of ketone bodies during fasting. Genes & Development. 26(3):282-93
- Nakajima, H., Nakajima-Takagi, Y., Tsujita, T., Akiyama, S., Wakasa, T., Mukaigasa, K., Kaneko, H., Tamaru, Y., Yamamoto, M., and Kobayashi, M. (2011) Tissue-restricted expression of nrf2 and its target genes in zebrafish with gene-specific variations in the induction profiles. PLoS One. 6(10):e26884
- Li, Q., Ritter, D., Yang, N., Dong, Z., Li, H., Chuang, J.H., and Guo, S. (2010) A systematic approach to identify functional motifs within vertebrate developmental enhancers. Developmental Biology. 337(2):484-495
- Singh, S.K., Sundaram, C.S., Shanbhag, S., and Idris, M.M. (2010) Proteomic profile of zebrafish brain based on two-dimensional gel electrophoresis matrix-assisted laser desorption/ionization MS/MS analysis. Zebrafish. 7(2):169-177
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