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Protein

25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial

Gene

Cyp27b1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Catalyzes the conversion of 25-hydroxyvitamin D3 (25(OH)D3) to 1-alpha,25-dihydroxyvitamin D3 (1alpha,25(OH)2D3), and of 24,25-dihydroxyvitamin D3 (24,25(OH)2D3) to 1-alpha,24,25-trihydroxyvitamin D3 (1alpha,24,25(OH)3D3). Is also active with 25-hydroxy-24-oxo-vitamin D3. Plays an important role in normal bone growth, calcium metabolism, and tissue differentiation.By similarity

Catalytic activityi

Calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitriol + 2 oxidized adrenodoxin + H2O.By similarity
Secalciferol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitetrol + 2 oxidized adrenodoxin + H2O.By similarity

Cofactori

hemeBy similarity

Pathwayi: cholecalciferol biosynthesis

This protein is involved in the pathway cholecalciferol biosynthesis, which is part of Hormone biosynthesis.
View all proteins of this organism that are known to be involved in the pathway cholecalciferol biosynthesis and in Hormone biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi448Iron (heme axial ligand)By similarity1

GO - Molecular functioni

  • calcidiol 1-monooxygenase activity Source: BHF-UCL
  • heme binding Source: InterPro
  • iron ion binding Source: InterPro

GO - Biological processi

  • aging Source: RGD
  • bone mineralization Source: RGD
  • calcitriol biosynthetic process from calciol Source: RGD
  • calcium ion homeostasis Source: RGD
  • calcium ion transport Source: RGD
  • decidualization Source: RGD
  • G1 to G0 transition Source: RGD
  • lactation Source: RGD
  • negative regulation of calcidiol 1-monooxygenase activity Source: RGD
  • negative regulation of cell growth Source: RGD
  • negative regulation of cell proliferation Source: RGD
  • positive regulation of keratinocyte differentiation Source: RGD
  • positive regulation of vitamin D 24-hydroxylase activity Source: RGD
  • positive regulation of vitamin D receptor signaling pathway Source: RGD
  • regulation of bone mineralization Source: RGD
  • response to calcium ion Source: RGD
  • response to cAMP Source: RGD
  • response to copper ion Source: RGD
  • response to drug Source: RGD
  • response to estrogen Source: RGD
  • response to insulin Source: RGD
  • response to interferon-gamma Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to peptide hormone Source: RGD
  • response to prostaglandin E Source: RGD
  • response to vitamin D Source: RGD
  • vitamin D catabolic process Source: BHF-UCL
  • vitamin D metabolic process Source: RGD

Keywordsi

Molecular functionMonooxygenase, Oxidoreductase
LigandHeme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14354.
SABIO-RKiO35132.
UniPathwayiUPA00955.

Names & Taxonomyi

Protein namesi
Recommended name:
25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial (EC:1.14.15.18By similarity)
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi69192. Cyp27b1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000003624? – 50125-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial
Transit peptidei1 – ?MitochondrionSequence analysis

Proteomic databases

PaxDbiO35132.
PRIDEiO35132.

Expressioni

Tissue specificityi

Kidney.

Interactioni

Protein-protein interaction databases

BioGridi250405. 1 interactor.
STRINGi10116.ENSRNOP00000064023.

Structurei

3D structure databases

ProteinModelPortaliO35132.
SMRiO35132.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0159. Eukaryota.
COG2124. LUCA.
HOVERGENiHBG106909.
InParanoidiO35132.
KOiK07438.
PhylomeDBiO35132.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiView protein in InterPro
IPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
IPR036396. Cyt_P450_sf.
PfamiView protein in Pfam
PF00067. p450. 1 hit.
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiView protein in PROSITE
PS00086. CYTOCHROME_P450. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O35132-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQAVKLASR VFHRVQLPSQ LGSDSVLRSL SDIPGPSTPS FLAELFCKGG
60 70 80 90 100
LSRLHELQVH GAARYGPIWS GSFGTLRTVY VADPALVEQL LRQESHCPER
110 120 130 140 150
CSFSSWSEHR RRHQRACGLL TADGEEWQRL RSLLAPLLLR PQAAAGYAGT
160 170 180 190 200
LDSVVSDLVR RLRRQRGRGS GLPDLVLDVA GEFYKFGLEG IGAVLLGSRL
210 220 230 240 250
GCLEAEVPPD TETFIEAVGS VFVSTLLTMA MPSWLHRLIP GPWARLCRDW
260 270 280 290 300
DQMFAFAQKH VEQREGEAAV RNQGKPEEDL PTGHHLTHFL FREKVSVQSI
310 320 330 340 350
VGNVTELLLA GVDTVSNTLS WALYELSRHP EVQSALHSEI TGAVNPGSYA
360 370 380 390 400
HLQATALSQL PLLKAVIKEV LRLYPVVPGN SRVPDRDICV GNYVIPQDTL
410 420 430 440 450
VSLCHYATSR DPAQFREPNS FNPARWLGEG PAPHPFASLP FGFGKRSCIG
460 470 480 490 500
RRLAELELQM ALAQILTHFE VLPEPGALPV KPMTRTVLVP ERSIHLQFVD

R
Length:501
Mass (Da):55,369
Last modified:July 15, 1998 - v2
Checksum:iB0A85286A219EA0E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti13H → D in AAB86461 (PubMed:9333115).Curated1
Sequence conflicti55H → D in AAB86461 (PubMed:9333115).Curated1
Sequence conflicti103 – 112FSSWSEHRRR → SHLGQSTVAS in AAB86461 (PubMed:9333115).Curated10
Sequence conflicti119L → W in AAB86461 (PubMed:9333115).Curated1
Sequence conflicti129 – 144RLRSL…RPQAA → EAPKSPGPASPPTSSS in AAB86461 (PubMed:9333115).CuratedAdd BLAST16
Sequence conflicti201G → R in AAB86461 (PubMed:9333115).Curated1
Sequence conflicti251D → N in AAB86461 (PubMed:9333115).Curated1
Sequence conflicti288H → D in AAB86461 (PubMed:9333115).Curated1
Sequence conflicti305T → R in AAB86461 (PubMed:9333115).Curated1
Sequence conflicti372 – 374RLY → MLD in AAB86461 (PubMed:9333115).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

Similar proteinsi

Entry informationi

Entry nameiCP27B_RAT
AccessioniPrimary (citable) accession number: O35132
Secondary accession number(s): O35076
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: February 28, 2018
This is version 113 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome