O35084 (CP27B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Cyp27b1
Synonyms:	Cyp27b, Cyp40

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	507 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	Hormone biosynthesis; cholecalciferol biosynthesis.
Subcellular location	Mitochondrion membrane.
Tissue specificity	Kidney.
Sequence similarities	Belongs to the cytochrome P450 family.
Sequence caution	The sequence BAA22434.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Membrane Mitochondrion
Domain	Transit peptide
Ligand	Heme Iron Metal-binding NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G1 to G0 transition Inferred from electronic annotation. Source: Compara bone mineralization Inferred from electronic annotation. Source: Compara calcium ion homeostasis Inferred from electronic annotation. Source: Compara calcium ion transport Inferred from mutant phenotype PubMed 12205031. Source: MGI decidualization Inferred from electronic annotation. Source: Compara negative regulation of calcidiol 1-monooxygenase activity Inferred from electronic annotation. Source: Compara negative regulation of cell growth Inferred from electronic annotation. Source: Compara negative regulation of cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of keratinocyte differentiation Inferred from electronic annotation. Source: Compara positive regulation of vitamin D 24-hydroxylase activity Inferred from electronic annotation. Source: Compara positive regulation of vitamin D receptor signaling pathway Inferred from electronic annotation. Source: Compara regulation of bone mineralization Inferred from electronic annotation. Source: Compara response to estrogen stimulus Inferred from electronic annotation. Source: Compara response to interferon-gamma Inferred from electronic annotation. Source: Compara response to lipopolysaccharide Inferred from electronic annotation. Source: Compara response to tumor necrosis factor Inferred from electronic annotation. Source: Compara response to vitamin D Inferred from direct assay Ref.1. Source: BHF-UCL vitamin D biosynthetic process Inferred from electronic annotation. Source: Compara vitamin D catabolic process Inferred from direct assay Ref.1. Source: BHF-UCL
Cellular_component	mitochondrial membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay PubMed 14651853PubMed 18614015. Source: MGI
Molecular_function	calcidiol 1-monooxygenase activity Inferred from direct assay Ref.1. Source: BHF-UCL electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred 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	? – 507		25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial		PRO_0000003623
Sites
	Metal binding	454	1	Iron (heme axial ligand) By similarity

Sequences

	Sequence		Length	Mass (Da)
	O35084 [UniParc]. Last modified July 15, 1998. Version 2. Checksum: 0669B4478C461B83	FASTA	507	56,225
	10 20 30 40 50 60 MTQAVKLASR VFHRIHLPLQ LDASLGSRGS ESVLRSLSDI PGPSTLSFLA ELFCKGGLSR 70 80 90 100 110 120 LHELQVHGAA RYGPIWSGSF GTLRTVYVAD PTLVEQLLRQ ESHCPERCSF SSWAEHRRRH 130 140 150 160 170 180 QRACGLLTAD GEEWQRLRSL LAPLLLRPQA AAGYAGTLDN VVRDLVRRLR RQRGRGSGLP 190 200 210 220 230 240 GLVLDVAGEF YKFGLESIGA VLLGSRLGCL EAEVPPDTET FIHAVGSVFV STLLTMAMPN 250 260 270 280 290 300 WLHHLIPGPW ARLCRDWDQM FAFAQRHVEL REGEAAMRNQ GKPEEDMPSG HHLTHFLFRE 310 320 330 340 350 360 KVSVQSIVGN VTELLLAGVD TVSNTLSWTL YELSRHPDVQ TALHSEITAG TRGSCAHPHG 370 380 390 400 410 420 TALSQLPLLK AVIKEVLRLY PVVPGNSRVP DRDIRVGNYV IPQDTLVSLC HYATSRDPTQ 430 440 450 460 470 480 FPDPNSFNPA RWLGEGPTPH PFASLPFGFG KRSCIGRRLA ELELQMALSQ ILTHFEVLPE 490 500 PGALPIKPMT RTVLVPERSI NLQFVDR

References

[1]	"25-hydroxyvitamin D3 1alpha-hydroxylase and vitamin D synthesis." Takeyama K., Kitanaka S., Sato T., Kobori M., Yanagisawa J., Kato S. Science 277:1827-1830(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[2]	"Cloning of the mouse 25-hydroxyvitamin D3 1-alpha hydroxylase gene." Kimmel-Jehan C., DeLuca H.F. Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: 129.
[3]	"25-hydroxyvitamin D 1alpha-hydroxylase: structure of the mouse gene, chromosomal assignment, and developmental expression." Panda D.K., Al-Kawas S., Seldin M.F., Hendy G.N., Goltzman D. J. Bone Miner. Res. 16:46-56(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/SvJ.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB006034 mRNA. Translation: BAA22434.1. Different initiation. AF235021 Genomic DNA. Translation: AAK15024.1. AF286219 Genomic DNA. Translation: AAG44889.1.
IPI	IPI00126549.
RefSeq	NP_034139.2. NM_010009.2.
UniGene	Mm.6216.
3D structure databases
ProteinModelPortal	O35084.
SMR	O35084. Positions 35-504.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000006907.
PTM databases
PhosphoSite	O35084.
Proteomic databases
PaxDb	O35084.
PRIDE	O35084.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000165764; ENSMUSP00000130005; ENSMUSG00000006724.
GeneID	13115.
KEGG	mmu:13115.
UCSC	uc007hhs.2. mouse.
Organism-specific databases
CTD	1594.
MGI	MGI:1098274. Cyp27b1.
Phylogenomic databases
eggNOG	COG2124.
GeneTree	ENSGT00550000074304.
HOGENOM	HOG000253961.
HOVERGEN	HBG106909.
InParanoid	O35084.
KO	K07438.
OMA	PWTEHRR.
OrthoDB	EOG4NS3BB.
Enzyme and pathway databases
BRENDA	1.14.13.13. 3474.
UniPathway	UPA00955.
Gene expression databases
ArrayExpress	O35084.
Bgee	O35084.
Genevestigator	O35084.
GermOnline	ENSMUSG00000006724. Mus musculus.
Family and domain databases
Gene3D	1.10.630.10. 1 hit.
InterPro	IPR001128. Cyt_P450. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. [Graphical view]
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00463. EP450I. PR00385. P450.
SUPFAM	SSF48264. Cytochrome_P450. 1 hit.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	283134.
SOURCE	Search...

Entry information

Entry name

CP27B_MOUSE

Accession

Primary (citable) accession number: O35084

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 15, 1998
Last modified:	May 1, 2013
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program