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O35132

- CP27B_RAT

UniProt

O35132 - CP27B_RAT

Protein

25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial

Gene

Cyp27b1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 2 (15 Jul 1998)
      Previous versions | rss
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    Functioni

    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 activityi

    Calcidiol + NADPH + O2 = calcitriol + NADP+ + H2O.

    Cofactori

    Heme group.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi448 – 4481Iron (heme axial ligand)By similarity

    GO - Molecular functioni

    1. calcidiol 1-monooxygenase activity Source: BHF-UCL
    2. heme binding Source: InterPro
    3. iron ion binding Source: InterPro

    GO - Biological processi

    1. aging Source: RGD
    2. calcitriol biosynthetic process from calciol Source: GOC
    3. lactation Source: RGD
    4. response to calcium ion Source: RGD
    5. response to cAMP Source: RGD
    6. response to copper ion Source: RGD
    7. response to drug Source: RGD
    8. response to insulin Source: RGD
    9. response to peptide hormone Source: RGD
    10. response to prostaglandin E Source: RGD
    11. response to vitamin D Source: RGD
    12. vitamin D catabolic process Source: BHF-UCL
    13. vitamin D metabolic process Source: RGD

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Ligandi

    Heme, Iron, Metal-binding, NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14354.
    UniPathwayiUPA00955.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial (EC:1.14.13.13)
    Alternative name(s):
    25-OHD-1 alpha-hydroxylase
    25-hydroxyvitamin D(3) 1-alpha-hydroxylase
    Short name:
    VD3 1A hydroxylase
    Calcidiol 1-monooxygenase
    Cytochrome P450 subfamily XXVIIB polypeptide 1
    Cytochrome P450C1 alpha
    Cytochrome P450VD1-alpha
    Cytochrome p450 27B1
    Gene namesi
    Name:Cyp27b1
    Synonyms:Cyp27b
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi69192. Cyp27b1.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial membrane Source: UniProtKB-SubCell
    2. mitochondrion Source: RGD

    Keywords - Cellular componenti

    Membrane, Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 50125-hydroxyvitamin D-1 alpha hydroxylase, mitochondrialPRO_0000003624
    Transit peptidei1 – ?MitochondrionSequence Analysis

    Proteomic databases

    PRIDEiO35132.

    Expressioni

    Tissue specificityi

    Kidney.

    Gene expression databases

    GenevestigatoriO35132.

    Interactioni

    Protein-protein interaction databases

    BioGridi250405. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliO35132.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    HOVERGENiHBG106909.
    KOiK07438.
    PhylomeDBiO35132.

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    InterProiIPR001128. Cyt_P450.
    IPR017972. Cyt_P450_CS.
    IPR002401. Cyt_P450_E_grp-I.
    [Graphical view]
    PfamiPF00067. p450. 1 hit.
    [Graphical view]
    PRINTSiPR00463. EP450I.
    PR00385. P450.
    SUPFAMiSSF48264. SSF48264. 1 hit.
    PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O35132-1 [UniParc]FASTAAdd to Basket

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    MTQAVKLASR VFHRVQLPSQ LGSDSVLRSL SDIPGPSTPS FLAELFCKGG    50
    LSRLHELQVH GAARYGPIWS GSFGTLRTVY VADPALVEQL LRQESHCPER 100
    CSFSSWSEHR RRHQRACGLL TADGEEWQRL RSLLAPLLLR PQAAAGYAGT 150
    LDSVVSDLVR RLRRQRGRGS GLPDLVLDVA GEFYKFGLEG IGAVLLGSRL 200
    GCLEAEVPPD TETFIEAVGS VFVSTLLTMA MPSWLHRLIP GPWARLCRDW 250
    DQMFAFAQKH VEQREGEAAV RNQGKPEEDL PTGHHLTHFL FREKVSVQSI 300
    VGNVTELLLA GVDTVSNTLS WALYELSRHP EVQSALHSEI TGAVNPGSYA 350
    HLQATALSQL PLLKAVIKEV LRLYPVVPGN SRVPDRDICV GNYVIPQDTL 400
    VSLCHYATSR DPAQFREPNS FNPARWLGEG PAPHPFASLP FGFGKRSCIG 450
    RRLAELELQM ALAQILTHFE VLPEPGALPV KPMTRTVLVP ERSIHLQFVD 500
    R 501
    Length:501
    Mass (Da):55,369
    Last modified:July 15, 1998 - v2
    Checksum:iB0A85286A219EA0E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 131H → D in AAB86461. (PubMed:9333115)Curated
    Sequence conflicti55 – 551H → D in AAB86461. (PubMed:9333115)Curated
    Sequence conflicti103 – 11210FSSWSEHRRR → SHLGQSTVAS in AAB86461. (PubMed:9333115)Curated
    Sequence conflicti119 – 1191L → W in AAB86461. (PubMed:9333115)Curated
    Sequence conflicti129 – 14416RLRSL…RPQAA → EAPKSPGPASPPTSSS in AAB86461. (PubMed:9333115)CuratedAdd
    BLAST
    Sequence conflicti201 – 2011G → R in AAB86461. (PubMed:9333115)Curated
    Sequence conflicti251 – 2511D → N in AAB86461. (PubMed:9333115)Curated
    Sequence conflicti288 – 2881H → D in AAB86461. (PubMed:9333115)Curated
    Sequence conflicti305 – 3051T → R in AAB86461. (PubMed:9333115)Curated
    Sequence conflicti372 – 3743RLY → MLD in AAB86461. (PubMed:9333115)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF000139 mRNA. Translation: AAB86461.1.
    AB001992 mRNA. Translation: BAA23271.1.
    RefSeqiNP_446215.1. NM_053763.1.
    UniGeneiRn.10847.

    Genome annotation databases

    GeneIDi114700.
    KEGGirno:114700.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF000139 mRNA. Translation: AAB86461.1 .
    AB001992 mRNA. Translation: BAA23271.1 .
    RefSeqi NP_446215.1. NM_053763.1.
    UniGenei Rn.10847.

    3D structure databases

    ProteinModelPortali O35132.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 250405. 1 interaction.

    Proteomic databases

    PRIDEi O35132.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 114700.
    KEGGi rno:114700.

    Organism-specific databases

    CTDi 1594.
    RGDi 69192. Cyp27b1.

    Phylogenomic databases

    HOVERGENi HBG106909.
    KOi K07438.
    PhylomeDBi O35132.

    Enzyme and pathway databases

    UniPathwayi UPA00955 .
    BioCyci MetaCyc:MONOMER-14354.

    Miscellaneous databases

    NextBioi 618833.

    Gene expression databases

    Genevestigatori O35132.

    Family and domain databases

    Gene3Di 1.10.630.10. 1 hit.
    InterProi IPR001128. Cyt_P450.
    IPR017972. Cyt_P450_CS.
    IPR002401. Cyt_P450_E_grp-I.
    [Graphical view ]
    Pfami PF00067. p450. 1 hit.
    [Graphical view ]
    PRINTSi PR00463. EP450I.
    PR00385. P450.
    SUPFAMi SSF48264. SSF48264. 1 hit.
    PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Kidney.

    Entry informationi

    Entry nameiCP27B_RAT
    AccessioniPrimary (citable) accession number: O35132
    Secondary accession number(s): O35076
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 97 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3