Gene
ndufv1
- ID
- ZDB-GENE-040808-73
- Name
- NADH:ubiquinone oxidoreductase core subunit V1
- Symbol
- ndufv1 Nomenclature History
- Previous Names
-
- wu:fc01f01
- wu:fc12f12
- zgc:86620
- Type
- protein_coding_gene
- Location
- Chr: 19 Mapping Details/Browsers
- Description
- Predicted to enable several functions, including 4 iron, 4 sulfur cluster binding activity; NADH dehydrogenase (ubiquinone) activity; and nucleotide binding activity. Predicted to be involved in mitochondrial electron transport, NADH to ubiquinone. Predicted to be located in mitochondrial inner membrane. Predicted to be part of respiratory chain complex I. Is expressed in several structures, including alar plate midbrain region; immature eye; musculature system; optic tectum; and pronephric duct. Human ortholog(s) of this gene implicated in nuclear type mitochondrial complex I deficiency 4. Orthologous to human NDUFV1 (NADH:ubiquinone oxidoreductase core subunit V1).
- Genome Resources
- Note
- None
- Comparative Information
-
- All Expression Data
- 7 figures from Thisse et al., 2004
- Cross-Species Comparison
- High Throughput Data
- Thisse Expression Data
-
- IMAGE:6892746 (1 image)
- IMAGE:7157113 (7 images)
Wild Type Expression Summary
- All Phenotype Data
- No data available
- Cross-Species Comparison
- Alliance
Phenotype Summary
Mutations
| Allele | Type | Localization | Consequence | Mutagen | Supplier |
|---|---|---|---|---|---|
| sa43227 | Allele with one point mutation | Unknown | Splice Site | ENU |
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No data available
Human Disease
| Disease Ontology Term | Multi-Species Data | OMIM Term | OMIM Phenotype ID |
|---|---|---|---|
| nuclear type mitochondrial complex I deficiency 4 | Alliance | Mitochondrial complex I deficiency, nuclear type 4 | 618225 |
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Domain, Family, and Site Summary
| Type | InterPro ID | Name |
|---|---|---|
| Conserved_site | IPR001949 | NADH:ubiquinone oxidoreductase, 51kDa subunit, conserved site |
| Domain | IPR011538 | NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain |
| Domain | IPR019575 | NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain |
| Domain | IPR054765 | SLBB domain |
| Family | IPR011537 | NADH ubiquinone oxidoreductase, F subunit |
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Domain Details Per Protein
| Protein | Length | Complex I 51 kDa subunit | NADH:ubiquinone oxidoreductase, 51kDa subunit, conserved site | NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain | NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain superfamily | NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain | NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain superfamily | NADH ubiquinone oxidoreductase, F subunit | SLBB domain |
|---|---|---|---|---|---|---|---|---|---|
|
UniProtKB:Q6AZA2
|
492 |
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| Type | Name | Annotation Method | Has Havana Data | Length (nt) | Analysis |
|---|---|---|---|---|---|
| mRNA |
ndufv1-201
(1)
|
Ensembl | 1,915 nt | ||
| ncRNA |
ndufv1-003
(1)
|
Ensembl | 1,310 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 | CH211-130O18 | ZFIN Curated Data | |
| Encodes | EST | fc01f01 | ||
| Encodes | EST | fc12f12 | ||
| Encodes | EST | IMAGE:6892746 | Thisse et al., 2004 | |
| Encodes | EST | IMAGE:7157113 | Thisse et al., 2004 | |
| Encodes | cDNA | MGC:86620 | ZFIN Curated Data |
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| Type | Accession # | Sequence | Length (nt/aa) | Analysis |
|---|---|---|---|---|
| RNA | RefSeq:NM_001003747 (1) | 1951 nt | ||
| Genomic | GenBank:CR391915 (1) | 77634 nt | ||
| Polypeptide | UniProtKB:Q6AZA2 (1) | 492 aa |
| Species | Symbol | Chromosome | Accession # | Evidence |
|---|---|---|---|---|
| Human | NDUFV1 | 11 | Amino acid sequence comparison (1) |
- Wu, Y., Liu, W., Li, L., Tai, Z., Gao, B., Liu, J.X. (2023) Atp7b deficiency induces zebrafish eye developmental defects. Metallomics : integrated biometal science. 15(5):
- Miklas, J.W., Levy, S., Hofsteen, P., Mex, D.I., Clark, E., Muster, J., Robitaille, A.M., Sivaram, G., Abell, L., Goodson, J.M., Pranoto, I., Madan, A., Chin, M.T., Tian, R., Murry, C.E., Moon, R.T., Wang, Y., Ruohola-Baker, H. (2021) Amino acid primed mTOR activity is essential for heart regeneration. iScience. 25:103574
- 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
- Woods, I.G., Wilson, C., Friedlander, B., Chang, P., Reyes, D.K., Nix, R., Kelly, P.D., Chu, F., Postlethwait, J.H., and Talbot, W.S. (2005) The zebrafish gene map defines ancestral vertebrate chromosomes. Genome research. 15(9):1307-1314
- 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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