Gene
hspd1
- ID
- ZDB-GENE-021206-1
- Name
- heat shock 60 protein 1
- Symbol
- hspd1 Nomenclature History
- Previous Names
- Type
- protein_coding_gene
- Location
- Chr: 9 Mapping Details/Browsers
- Description
- Predicted to enable protein-folding chaperone binding activity. Acts upstream of or within several processes, including fin regeneration; neuromast regeneration; and regulation of neutrophil chemotaxis. Located in mitochondrial matrix. Is expressed in several structures, including anterior neural keel; digestive system; mesoderm; musculature system; and nervous system. Human ortholog(s) of this gene implicated in several diseases, including artery disease (multiple); autistic disorder; glucose intolerance; hereditary spastic paraplegia (multiple); and hypomyelinating leukodystrophy 4. Orthologous to human HSPD1 (heat shock protein family D (Hsp60) member 1).
- Genome Resources
- Note
- None
- Comparative Information
-
- All Expression Data
- 38 figures from 14 publications
- Cross-Species Comparison
- High Throughput Data
- Thisse Expression Data
-
- cb144 (20 images)
- cb863 (12 images)
Wild Type Expression Summary
Phenotype Summary
Mutations
| Allele | Type | Localization | Consequence | Mutagen | Supplier |
|---|---|---|---|---|---|
| la026911Tg | Transgenic insertion | Unknown | Unknown | DNA | |
| sa11157 | Allele with one point mutation | Unknown | Splice Site | ENU | |
| zp7 | Allele with one point mutation | Unknown | Missense | ENU |
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Human Disease
| Disease Ontology Term | Multi-Species Data | OMIM Term | OMIM Phenotype ID |
|---|---|---|---|
| hereditary spastic paraplegia 13 | Alliance | Spastic paraplegia 13, autosomal dominant | 605280 |
| hypomyelinating leukodystrophy 4 | Alliance | Leukodystrophy, hypomyelinating, 4 | 612233 |
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Domain, Family, and Site Summary
| Type | InterPro ID | Name |
|---|---|---|
| Conserved_site | IPR018370 | Chaperonin Cpn60, conserved site |
| Family | IPR001844 | Chaperonin Cpn60/GroEL |
| Family | IPR002423 | Chaperonin Cpn60/GroEL/TCP-1 family |
| Homologous_superfamily | IPR027409 | GroEL-like apical domain superfamily |
| Homologous_superfamily | IPR027410 | TCP-1-like chaperonin intermediate domain superfamily |
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Domain Details Per Protein
| Protein | Additional Resources | Length | Chaperonin Cpn60, conserved site | Chaperonin Cpn60/GroEL | Chaperonin Cpn60/GroEL/TCP-1 family | GroEL-like apical domain superfamily | GroEL-like equatorial domain superfamily | TCP-1-like chaperonin intermediate domain superfamily |
|---|---|---|---|---|---|---|---|---|
| UniProtKB:Q803B0 | InterPro | 575 |
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Interactions and Pathways
No data available
Plasmids
No data available
| Construct | Regulatory Region | Coding Sequence | Species | Tg Lines | Citations |
|---|---|---|---|---|---|
| Tg(hspd1:d2-GFP) |
|
| 1 | Lin et al., 2021 |
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| Relationship | Marker Type | Marker | Accession Numbers | Citations |
|---|---|---|---|---|
| Contained in | BAC | DKEY-83M22 | ZFIN Curated Data | |
| Contains | SNP | rs3728228 | ZFIN Curated Data | |
| Encodes | EST | cb144 | (2) | |
| Encodes | EST | cb863 | Thisse et al., 2001 | |
| Encodes | EST | fa04a05 | ||
| Encodes | EST | fb22d10 | ||
| Encodes | EST | fi04a12 | ||
| Encodes | EST | fi27b05 | ||
| Encodes | EST | ibd2197 | ||
| Encodes | cDNA | MGC:55967 | ZFIN Curated Data |
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| Type | Accession # | Sequence | Length (nt/aa) | Analysis |
|---|---|---|---|---|
| RNA | RefSeq:NM_181330 (1) | 2739 nt | ||
| Genomic | GenBank:BX530407 (1) | 292409 nt | ||
| Polypeptide | UniProtKB:Q803B0 (1) | 575 aa |
- Cömert, C., Kjær-Sørensen, K., Hansen, J., Carlsen, J., Just, J., Meaney, B.F., Østergaard, E., Luo, Y., Oxvig, C., Schmidt-Laursen, L., Palmfeldt, J., Fernandez-Guerra, P., Bross, P. (2024) HSP60 chaperone deficiency disrupts the mitochondrial matrix proteome and dysregulates cholesterol synthesis. Molecular metabolism. 88:102009
- Wen, W., Guo, C., Chen, Z., Yang, D., Zhu, D., Jing, Q., Zheng, L., Sun, C., Tang, C. (2023) Regular exercise attenuates alcoholic myopathy in zebrafish by modulating mitochondrial homeostasis. PLoS One. 18:e0294700e0294700
- Ha, J., Kim, B.S., Min, B., Nam, J., Lee, J.G., Lee, M., Yoon, B.H., Choi, Y.H., Im, I., Park, J.S., Choi, H., Baek, A., Cho, S.M., Lee, M.O., Nam, K.H., Mun, J.Y., Kim, M., Kim, S.Y., Son, M.Y., Kang, Y.K., Lee, J.S., Kim, J.K., Kim, J. (2022) Intermediate cells of in vitro cellular reprogramming and in vivo tissue regeneration require desmoplakin. Science advances. 8:eabk1239
- Jamieson-Lucy, A.H., Kobayashi, M., James Aykit, Y., Elkouby, Y., Escobar-Aguirre, M., Vejnar, C., Giraldez, A., Mullins, M.C. (2022) A proteomics approach identifies novel resident zebrafish Balbiani body proteins Cirbpa and Cirbpb. Developmental Biology. 484:1-11
- Li, H., Xu, W., Xiang, S., Tao, L., Fu, W., Liu, J., Liu, W., Xiao, Y., Peng, L. (2022) Defining the Pluripotent Marker Genes for Identification of Teleost Fish Cell Pluripotency During Reprogramming. Frontiers in genetics. 13:819682
- Keatinge, M., Tsarouchas, T.M., Munir, T., Porter, N.J., Larraz, J., Gianni, D., Tsai, H.H., Becker, C.G., Lyons, D.A., Becker, T. (2021) CRISPR gRNA phenotypic screening in zebrafish reveals pro-regenerative genes in spinal cord injury. PLoS Genetics. 17:e1009515
- Lin, Y.F., Sam, J., Evans, T. (2021) Sirt1 promotes tissue regeneration in zebrafish through regulating the mitochondrial unfolded protein response. iScience. 24:103118
- Enomoto, H., Mittal, N., Inomata, T., Arimura, T., Izumi, T., Kimura, A., Fukuda, K., Makino, S. (2020) Dilated Cardiomyopathy (DCM)-linked Heat shock protein Family D Member 1 (HSPD1) mutations cause upregulation of ROS and autophagy through mitochondrial dysfunction. Cardiovascular research. 117(4):1118-1131
- Rehman, S.U., Nadeem, A., Javed, M., Hassan, F.U., Luo, X., Khalid, R.B., Liu, Q. (2020) Genomic Identification, Evolution and Sequence Analysis of the Heat-Shock Protein Gene Family in Buffalo. Genes. 11(11):
- Gong, L., Zhang, Q., Pan, X., Chen, S., Yang, L., Liu, B., Yang, W., Yu, L., Xiao, Z.X., Feng, X.H., Wang, H., Yuan, Z.M., Peng, J., Tan, W.Q., Chen, J. (2019) p53 Protects Cells from Death at the Heatstroke Threshold Temperature. Cell Reports. 29:3693-3707.e5
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