Reviewed,
UniProtKB/Swiss-Prot O35132 (CP27B_RAT)
Last modified
June 16, 2009.
Version 67.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial EC=1.14.13.13 Alternative name(s): Cytochrome P450 subfamily XXVIIB polypeptide 1 Cytochrome p450 27B1 Calcidiol 1-monooxygenase 25-OHD-1 alpha-hydroxylase 25-hydroxyvitamin D(3) 1-alpha-hydroxylase Short name=VD3 1A hydroxylase P450C1 alpha P450VD1-alpha | ||||
| Gene names |
| ||||
| Organism | Rattus norvegicus (Rat) | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 501 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Catalyzes the conversion of 25-hydroxyvitamin D3 (25(OH)D) to 1-alpha,25-dihydroxyvitamin D3 (1,25(OH)2D) plays an important role in normal bone growth, calcium metabolism, and tissue differentiation. |
| Catalytic activity | Calcidiol + NADPH + O2 = calcitriol + NADP+ + H2O. |
| Cofactor | Heme group By similarity. |
| Pathway | |
| Subcellular location | |
| Tissue specificity | Kidney. |
| Sequence similarities | Belongs to the cytochrome P450 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Membrane Mitochondrion |
| Domain | Transit peptide |
| Ligand | Heme Iron Metal-binding NADP |
| Molecular function | Monooxygenase Oxidoreductase |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW vitamin D catabolic process Ref.1Inferred from direct assay. Source: UniProtKB |
| Cellular component | mitochondrial membrane Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | calcidiol 1-monooxygenase activity Ref.1 Ref.2 Inferred from direct assay. Source: UniProtKB electron carrier activityInferred from electronic annotation. Source: InterPro heme bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – ? | Mitochondrion Potential | |||||||
| Chain | ? – 501 | 25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial | PRO_0000003624 | ||||||
Sites | |||||||||
| Metal binding | 448 | 1 | Iron (heme axial ligand) By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 13 | 1 | H → D in AAB86461. Ref.1 | ||||||
| Sequence conflict | 55 | 1 | H → D in AAB86461. Ref.1 | ||||||
| Sequence conflict | 103 – 112 | 10 | FSSWSEHRRR → SHLGQSTVAS in AAB86461. Ref.1 | ||||||
| Sequence conflict | 119 | 1 | L → W in AAB86461. Ref.1 | ||||||
| Sequence conflict | 129 – 144 | 16 | RLRSL…RPQAA → EAPKSPGPASPPTSSS in AAB86461. Ref.1 | ||||||
| Sequence conflict | 201 | 1 | G → R in AAB86461. Ref.1 | ||||||
| Sequence conflict | 251 | 1 | D → N in AAB86461. Ref.1 | ||||||
| Sequence conflict | 288 | 1 | H → D in AAB86461. Ref.1 | ||||||
| Sequence conflict | 305 | 1 | T → R in AAB86461. Ref.1 | ||||||
| Sequence conflict | 372 – 374 | 3 | RLY → MLD in AAB86461. Ref.1 | ||||||
Sequences
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References
| [1] | "The 25-hydroxyvitamin D 1-alpha-hydroxylase gene maps to the pseudovitamin D-deficiency rickets (PDDR) disease locus." St Arnaud R., Messerlian S., Moir J.M., Omdahl J.L., Glorieux F.H. J. Bone Miner. Res. 12:1552-1559(1997) [PubMed: 9333115] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. |
| [2] | "Cloning and expression of rat 25-hydroxyvitamin D3-1alpha-hydroxylase cDNA." Shinki T., Shimada H., Wakino S., Anazawa H., Hayashi M., Saruta T., Deluca H.F., Suda T. Proc. Natl. Acad. Sci. U.S.A. 94:12920-12925(1997) [PubMed: 9371776] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney. |
Cross-references
Sequence databases | |
|---|---|
| AF000139 mRNA. Translation: AAB86461.1. AB001992 mRNA. Translation: BAA23271.1. | |
| IPI | IPI00206228. |
| RefSeq | NP_446215.1. |
| UniGene | Rn.10847 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1SCC based on UniProtKB P00189. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 114700. |
| KEGG | rno:114700. |
Organism-specific databases | |
| RGD | 69192. Cyp27b1. |
Phylogenomic databases | |
| HOVERGEN | O35132. |
Enzyme and pathway databases | |
| BRENDA | 1.14.13.13. 248. |
Family and domain databases | |
| InterPro | IPR001128. Cyt_P450. IPR017973. Cyt_P450_C. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. [Graphical view] |
| Gene3D | G3DSA:1.10.630.10. Cyt_P450. 1 hit. |
| PANTHER | PTHR19383. Cyt_P450. 1 hit. |
| Pfam | PF00067. p450. 1 hit. [Graphical view] |
| PRINTS | PR00463. EP450I. PR00385. P450. |
| PROSITE | PS00086. CYTOCHROME_P450. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 618833. |
Entry information
| Entry name | CP27B_RAT | ||||||||
| Accession | Primary (citable) accession number: O35132 Secondary accession number(s): O35076 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


