Gene
cpo
- ID
- ZDB-GENE-070619-6
- Name
- carboxypeptidase O
- Symbol
- cpo Nomenclature History
- Previous Names
- None
- Type
- protein_coding_gene
- Location
- Chr: 1 Mapping Details/Browsers
- Description
- Enables metallocarboxypeptidase activity. Predicted to be involved in proteolysis. Located in plasma membrane. Is expressed in intestinal epithelium. Orthologous to human CPO (carboxypeptidase O).
- Genome Resources
- Note
- None
- Comparative Information
-
- All Expression Data
- 1 figure from Lyons et al., 2011
- 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 |
|---|---|---|---|---|---|
| la021208Tg | Transgenic insertion | Unknown | Unknown | DNA | |
| sa1190 | Allele with one point mutation | Unknown | Splice Site | ENU |
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No data available
Human Disease
Domain, Family, and Site Summary
Domain Details Per Protein
| Protein | Additional Resources | Length | Carboxypeptidase O | Peptidase M14, carboxypeptidase A |
|---|---|---|---|---|
| UniProtKB:B8JLQ9 | InterPro | 363 |
Interactions and Pathways
No data available
Plasmids
No data available
No data available
| Relationship | Marker Type | Marker | Accession Numbers | Citations |
|---|---|---|---|---|
| Contained in | BAC | CH73-76B22 | ZFIN Curated Data |
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| Type | Accession # | Sequence | Length (nt/aa) | Analysis |
|---|---|---|---|---|
| RNA | RefSeq:NM_001145629 (1) | 1162 nt | ||
| Genomic | GenBank:CU469569 (1) | 102276 nt | ||
| Polypeptide | UniProtKB:B8JLQ9 (1) | 363 aa |
- Suzuki, H., Ogawa, T., Fujita, S., Sone, R., Kawahara, A. (2023) Cooperative contributions of the klf1 and klf17 genes in zebrafish primitive erythropoiesis. Scientific Reports. 13:1227912279
- Akula, S., Hellman, L., Avilés, F.X., Wernersson, S. (2021) Analysis of the mast cell expressed carboxypeptidase A3 and its structural and evolutionary relationship to other vertebrate carboxypeptidases. Developmental and comparative immunology. 127:104273
- 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
- Lyons, P.J., and Fricker, L.D. (2011) Carboxypeptidase O is a glycosylphosphatidylinositol-anchored intestinal peptidase with acidic amino acid specificity. The Journal of biological chemistry. 286(45):39023-32
- Lyons, P.J., Ma, L.H., Baker, R., and Fricker, L.D. (2010) Carboxypeptidase A6 in zebrafish development and implications for VIth cranial nerve pathfinding. PLoS One. 5(9):e12967
- Wang, D., Jao, L.E., Zheng, N., Dolan, K., Ivey, J., Zonies, S., Wu, X., Wu, K., Yang, H., Meng, Q., Zhu, Z., Zhang, B., Lin, S., and Burgess, S.M. (2007) Efficient genome-wide mutagenesis of zebrafish genes by retroviral insertions. Proceedings of the National Academy of Sciences of the United States of America. 104(30):12428-12433
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