Gene
ptprdb
- ID
- ZDB-GENE-070615-38
- Name
- protein tyrosine phosphatase receptor type Db
- Symbol
- ptprdb Nomenclature History
- Previous Names
-
- ptprd
- zgc:165626
- Type
- protein_coding_gene
- Location
- Chr: 1 Mapping Details/Browsers
- Description
- Predicted to enable protein tyrosine phosphatase activity. Predicted to be involved in nervous system development; signal transduction; and synaptic membrane adhesion. Predicted to act upstream of or within protein dephosphorylation. Predicted to be located in plasma membrane. Is expressed in Rohon-Beard neurons; lateral line ganglion; olfactory placode; and trigeminal ganglion. Human ortholog(s) of this gene implicated in coronary artery disease; diabetes mellitus; hypertension; and type 2 diabetes mellitus. Orthologous to human PTPRD (protein tyrosine phosphatase receptor type D).
- 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 |
|---|---|---|---|---|---|
| la013588Tg | Transgenic insertion | Unknown | Unknown | DNA | |
| sa450 | Allele with one point mutation | Unknown | Splice Site | ENU | |
| sa6579 | Allele with one point mutation | Unknown | Premature Stop | ENU | |
| sa10181 | Allele with one point mutation | Unknown | Premature Stop | ENU | |
| sa14902 | Allele with one point mutation | Unknown | Splice Site | ENU | |
| sa16499 | Allele with one point mutation | Unknown | Premature Stop | ENU | |
| sa19467 | Allele with one point mutation | Unknown | Premature Stop | ENU | |
| sa19468 | Allele with one point mutation | Unknown | Splice Site | ENU | |
| sa19469 | Allele with one point mutation | Unknown | Premature Stop | ENU | |
| sa32644 | Allele with one point mutation | Unknown | Premature Stop | ENU |
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Human Disease
Domain, Family, and Site Summary
| Type | InterPro ID | Name |
|---|---|---|
| Active_site | IPR016130 | Protein-tyrosine phosphatase, active site |
| Domain | IPR000242 | Tyrosine-specific protein phosphatase, PTPase domain |
| Domain | IPR000387 | Tyrosine-specific protein phosphatases domain |
| Domain | IPR003595 | Protein-tyrosine phosphatase, catalytic |
| Domain | IPR003598 | Immunoglobulin subtype 2 |
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Domain Details Per Protein
| Protein | Additional Resources | Length | Fibronectin type III | Fibronectin type III superfamily | Immunoglobulin domain subtype | Immunoglobulin I-set | Immunoglobulin-like domain | Immunoglobulin-like domain superfamily | Immunoglobulin-like fold | Immunoglobulin subtype 2 | Protein-tyrosine phosphatase, active site | Protein-tyrosine phosphatase, catalytic | Protein-tyrosine phosphatase-like | Receptor-type Tyrosine-protein Phosphatases/Ushers | Tyrosine-specific protein phosphatase, PTPase domain | Tyrosine-specific protein phosphatases domain |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| UniProtKB:A0A8M9PV64 | InterPro | 1942 | ||||||||||||||
| UniProtKB:A0A8M9PHQ2 | InterPro | 1949 | ||||||||||||||
| UniProtKB:A5PLI0 | InterPro | 205 | ||||||||||||||
| UniProtKB:A0A8M9PHN2 | InterPro | 1951 | ||||||||||||||
| UniProtKB:A0A8M3AYU7 | InterPro | 1505 |
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| Type | Name | Annotation Method | Has Havana Data | Length (nt) | Analysis |
|---|---|---|---|---|---|
| mRNA |
ptprdb-201
(1)
|
Ensembl | 1,140 nt | ||
| mRNA |
ptprdb-202
(1)
|
Ensembl | 6,806 nt | ||
| mRNA |
ptprdb-203
(1)
|
Ensembl | 957 nt | ||
| mRNA |
ptprdb-204
(1)
|
Ensembl | 5,805 nt | ||
| mRNA |
ptprdb-205
(1)
|
Ensembl | 4,548 nt |
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Interactions and Pathways
No data available
Plasmids
No data available
| Relationship | Marker Type | Marker | Accession Numbers | Citations |
|---|---|---|---|---|
| Contained in | BAC | DKEY-46O4 | ZFIN Curated Data | |
| Contained in | BAC | DKEYP-118A3 | ZFIN Curated Data | |
| Encodes | cDNA | MGC:165626 | ZFIN Curated Data |
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| Type | Accession # | Sequence | Length (nt/aa) | Analysis |
|---|---|---|---|---|
| RNA | RefSeq:NM_001166048 (1) | 5805 nt | ||
| Genomic | GenBank:BX546494 (1) | 174501 nt | ||
| Polypeptide | UniProtKB:A0A8M9PHF1 (1) | 1955 aa |
- Sun, Y., Zhang, B., Luo, L., Shi, D.L., Wang, H., Cui, Z., Huang, H., Cao, Y., Shu, X., Zhang, W., Zhou, J., Li, Y., Du, J., Zhao, Q., Chen, J., Zhong, H., Zhong, T.P., Li, L., Xiong, J.W., Peng, J., Xiao, W., Zhang, J., Yao, J., Yin, Z., Mo, X., Peng, G., Zhu, J., Chen, Y., Zhou, Y., Liu, D., Pan, W., Zhang, Y., Ruan, H., Liu, F., Zhu, Z., Meng, A., ZAKOC Consortium (2019) Systematic genome editing of the genes on zebrafish Chromosome 1 by CRISPR/Cas9. Genome research. 30(1):118-26
- 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
- Deng, C., Chen, H., Yang, N., Feng, Y., Hsueh, A.J. (2015) Apela regulates fluid homeostasis by binding to the APJ receptor to activate Gi signaling. The Journal of biological chemistry. 290(30):18261-8
- 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
- Overman, J.P., and den Hertog, J. (2014) Zebrafish as a model to study PTPs during development. Methods (San Diego, Calif.). 65(2):247-53
- Varshney, G.K., Lu, J., Gildea, D., Huang, H., Pei, W., Yang, Z., Huang, S.C., Schoenfeld, D.S., Pho, N., Casero, D., Hirase, T., Mosbrook-Davis, D.M., Zhang, S., Jao, L.E., Zhang, B., Woods, I.G., Zimmerman, S., Schier, A.F., Wolfsberg, T., Pellegrini, M., Burgess, S.M., and Lin, S. (2013) A large-scale zebrafish gene knockout resource for the genome-wide study of gene function. Genome research. 23(4):727-735
- Wang, F., Wolfson, S.N., Gharib, A., and Sagasti, A. (2012) LAR Receptor Tyrosine Phosphatases and HSPGs Guide Peripheral Sensory Axons to the Skin. Current biology : CB. 22(5):373-382
- van Eekelen, M., Overvoorde, J., van Rooijen, C., and den Hertog, J. (2010) Identification and expression of the family of classical protein-tyrosine phosphatases in zebrafish. PLoS One. 5(9):e12573
- Hufton, A.L., Mathia, S., Braun, H., Georgi, U., Lehrach, H., Vingron, M., Poustka, A.J., and Panopoulou, G. (2009) Deeply conserved chordate non-coding sequences preserve genome synteny but do not drive gene duplicate retention. Genome research. 19(11):2036-2051
- Braasch, I., Schartl, M., and Volff, J.N. (2007) Evolution of pigment synthesis pathways by gene and genome duplication in fish. BMC Evolutionary Biology. 7(1):74
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