Gene
hadhab
- ID
- ZDB-GENE-041111-204
- Name
- hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit alpha b
- Symbol
- hadhab Nomenclature History
- Previous Names
-
- im:7144234
- zgc:158138 (1)
- Type
- protein_coding_gene
- Location
- Chr: 17 Mapping Details/Browsers
- Description
- Predicted to enable enoyl-CoA hydratase activity and long-chain-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity. Predicted to be involved in fatty acid beta-oxidation. Predicted to act upstream of or within fatty acid metabolic process. Predicted to be located in mitochondrial inner membrane. Predicted to be part of mitochondrial fatty acid beta-oxidation multienzyme complex. Is expressed in liver. Human ortholog(s) of this gene implicated in mitochondrial trifunctional protein deficiency 1 and steatotic liver disease. Orthologous to human HADHA (hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit alpha).
- Genome Resources
- Note
- None
- Comparative Information
-
- All Expression Data
- 2 figures from 2 publications
- Cross-Species Comparison
- High Throughput Data
- Thisse Expression Data
-
- IMAGE:7144234 (1 image)
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 |
|---|---|---|---|
| mitochondrial trifunctional protein deficiency 1 | Alliance | Mitochondrial trifunctional protein deficiency 1 | 609015 |
| Fatty liver, acute, of pregnancy | 609016 | ||
| HELLP syndrome, maternal, of pregnancy | 609016 | ||
| LCHAD deficiency | 609016 |
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Domain, Family, and Site Summary
| Type | InterPro ID | Name |
|---|---|---|
| Conserved_site | IPR006180 | 3-hydroxyacyl-CoA dehydrogenase, conserved site |
| Conserved_site | IPR018376 | Enoyl-CoA hydratase/isomerase, conserved site |
| Domain | IPR006108 | 3-hydroxyacyl-CoA dehydrogenase, C-terminal |
| Domain | IPR006176 | 3-hydroxyacyl-CoA dehydrogenase, NAD binding |
| Family | IPR001753 | Enoyl-CoA hydratase/isomerase |
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Domain Details Per Protein
| Protein | Additional Resources | Length | 3-hydroxyacyl-CoA dehydrogenase, conserved site | 3-hydroxyacyl-CoA dehydrogenase, C-terminal | 3-hydroxyacyl-CoA dehydrogenase, NAD binding | 6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily | ClpP/crotonase-like domain superfamily | Enoyl-CoA hydratase/isomerase | Enoyl-CoA hydratase/isomerase, conserved site | Fatty acid oxidation complex, alpha subunit, mitochondrial | Fatty acid oxidation complex subunit alpha | NAD(P)-binding domain superfamily |
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| UniProtKB:A3KMH5 | InterPro | 763 |
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| Type | Name | Annotation Method | Has Havana Data | Length (nt) | Analysis |
|---|---|---|---|---|---|
| mRNA |
hadhab-201
(1)
|
Ensembl | 2,851 nt | ||
| mRNA |
hadhab-202
(1)
|
Ensembl | 941 nt | ||
| ncRNA |
hadhab-002
(1)
|
Ensembl | 2,851 nt |
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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 | BAC | DKEY-119A7 | ZFIN Curated Data | |
| Encodes | EST | IMAGE:7144234 | Thisse et al., 2004 | |
| Encodes | cDNA | MGC:158138 | ZFIN Curated Data |
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| Type | Accession # | Sequence | Length (nt/aa) | Analysis |
|---|---|---|---|---|
| RNA | RefSeq:NM_001089437 (1) | 2870 nt | ||
| Genomic | GenBank:CT027616 (1) | 200563 nt | ||
| Polypeptide | UniProtKB:A3KMH5 (1) | 763 aa |
- Tian, J., Du, Y., Yu, E., Lei, C., Xia, Y., Jiang, P., Li, H., Zhang, K., Li, Z., Gong, W., Xie, J., Wang, G. (2022) Prostaglandin 2α Promotes Autophagy and Mitochondrial Energy Production in Fish Hepatocytes. Cells. 11(12)
- Yu, F., Luo, H.R., Cui, X.F., Wu, Y.J., Li, J.L., Feng, W.R., Tang, Y.K., Su, S.Y., Xiao, J., Hou, Z.S., Xu, P. (2022) Changes in aggression and locomotor behaviors in response to zinc is accompanied by brain cell heterogeneity and metabolic and circadian dysregulation of the brain-liver axis. Ecotoxicology and environmental safety. 248:114303
- Takashima, S., Takemoto, S., Toyoshi, K., Ohba, A., Shimozawa, N. (2021) Zebrafish model of human Zellweger syndrome reveals organ-specific accumulation of distinct fatty acid species and widespread gene expression changes. Molecular genetics and metabolism. 133(3):307-323
- Xu, H., Jiang, Y., Miao, X.M., Tao, Y.X., Xie, L., Li, Y. (2021) A Model Construction of Starvation Induces Hepatic Steatosis and Transcriptome Analysis in Zebrafish Larvae. Biology. 10(2):
- 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
- Bui-Nguyen, T.M., Baer, C.E., Lewis, J.A., Yang, D., Lein, P.J., Jackson, D.A. (2015) Dichlorvos exposure results in large scale disruption of energy metabolism in the liver of the zebrafish, Danio rerio. BMC Genomics. 16:853
- 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
- Aanes, H., Winata, C.L., Lin, C.H., Chen, J.P., Srinivasan, K.G., Lee, S.G., Lim, A.Y., Hajan, H.S., Collas, P., Bourque, G., Gong, Z., Korzh, V., Aleström, P., and Mathavan, S. (2011) Zebrafish mRNA sequencing deciphers novelties in transcriptome dynamics during maternal to zygotic transition. Genome research. 21(8):1328-38
- 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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