Gene
rbp1.2
- ID
- ZDB-GENE-070912-18
- Name
- retinol binding protein 1, cellular, tandem duplicate 2
- Symbol
- rbp1.2 Nomenclature History
- Previous Names
-
- si:ch211-119o8.7
- Type
- protein_coding_gene
- Location
- Chr: 2 Mapping Details/Browsers
- Description
- Predicted to enable fatty acid binding activity. Predicted to be involved in fatty acid transport. Predicted to act upstream of or within retinoic acid biosynthetic process and vitamin A metabolic process. Predicted to be active in cytosol and nucleus. Is expressed in eye and retinal pigmented epithelium. Human ortholog(s) of this gene implicated in multiple myeloma. Orthologous to human RBP1 (retinol binding protein 1).
- Genome Resources
- Note
- None
- Comparative Information
-
- All Expression Data
- 2 figures from Takita et al., 2020
- Cross-Species Comparison
- High Throughput Data
- Thisse Expression Data
- No data available
Wild Type Expression Summary
- All Phenotype Data
- 1 Figure from Takita et al., 2020
- Cross-Species Comparison
- Alliance
Phenotype Summary
Mutations
| Allele | Type | Localization | Consequence | Mutagen | Supplier |
|---|---|---|---|---|---|
| rr1 | Allele with one delins | Exon 2 | Frameshift | CRISPR |
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Human Disease
Domain, Family, and Site Summary
Domain Details Per Protein
| Protein | Additional Resources | Length | Calycin | Cytosolic fatty-acid binding | Intracellular lipid binding protein | Lipocalin/cytosolic fatty-acid binding domain | Retinol-binding protein 1 |
|---|---|---|---|---|---|---|---|
| UniProtKB:A9JR93 | InterPro | 138 |
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| Type | Name | Annotation Method | Has Havana Data | Length (nt) | Analysis |
|---|---|---|---|---|---|
| mRNA |
rbp1 (1 of many)-201
(1)
|
Ensembl | 448 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 | CH211-119O8 | ZFIN Curated Data | |
| Encodes | cDNA | MGC:171839 | ZFIN Curated Data |
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| Type | Accession # | Sequence | Length (nt/aa) | Analysis |
|---|---|---|---|---|
| RNA | RefSeq:NM_001114899 (1) | 726 nt | ||
| Genomic | GenBank:AL953896 (2) | 158018 nt | ||
| Polypeptide | UniProtKB:A9JR93 (1) | 138 aa |
- Takita, S., Seko, Y. (2020) eys+/- ; lrp5+/- Zebrafish Reveals Lrp5 Can Be the Receptor of Retinol in the Visual Cycle. iScience. 23:101762
- Crespo, B., Lan-Chow-Wing, O., Rocha, A., Zanuy, S., Gómez, A. (2013) foxl2 and foxl3 are two ancient paralogs that remain fully functional in teleosts. General and comparative endocrinology. 194:81-93
- 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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