Sterol 26-hydroxylase, mitochondrial precursor

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P17178 (CP27A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 102. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Sterol 26-hydroxylase, mitochondrial
EC=1.14.13.15

Alternative name(s):
5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 27-hydroxylase
Cytochrome P-450C27/25
Cytochrome P450 27
Sterol 27-hydroxylase
Vitamin D(3) 25-hydroxylase

Gene names

Name:	Cyp27a1
Synonyms:	Cyp27

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	533 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the first step in the oxidation of the side chain of sterol intermediates; the 27-hydroxylation of 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol. Has also a vitamin D3-25-hydroxylase activity.
Catalytic activity	5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol + NADPH + O₂ = (25R)-5-beta-cholestane-3-alpha,7-alpha,12-alpha,26-tetraol + NADP⁺ + H₂O.
Cofactor	Heme group By similarity.
Pathway	Hormone biosynthesis; cholecalciferol biosynthesis.
Subcellular location	Mitochondrion membrane.
Tissue specificity	Expressed in liver, hepatoma, kidney, ovary and epithelial cells of blood vessels.
Sequence similarities	Belongs to the cytochrome P450 family.
Sequence caution	The sequence AAA86314.1 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
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cholesterol metabolic process Inferred from direct assay Ref.2. Source: RGD steroid catabolic process Traceable author statement. Source: RGD
Molecular function	cholestanetriol 26-monooxygenase activity Inferred from electronic annotation. Source: EC cholesterol 26-hydroxylase activity Inferred from direct assay Ref.2. Source: RGD electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro vitamin D3 25-hydroxylase activity Inferred from direct assay Ref.2. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 32

Mitochondrion Ref.1

Chain

33 – 533

501

Sterol 26-hydroxylase, mitochondrial

PRO_0000003621

Regions

Region

386 – 400

Sterol-binding Potential

Sites

Metal binding

479

Iron (heme axial ligand)

Amino acid modifications

Modified residue

125

N6-acetyllysine By similarity

Modified residue

499

N6-acetyllysine By similarity

Experimental info

Sequence conflict

88 – 96

Missing in AAA86314. Ref.4

Sequence conflict

167 – 168

ML → IV in AAA41786. Ref.3

Sequence conflict

167 – 168

ML → IV in AAA86314. Ref.4

Sequence conflict

209

H → N in AAA41786. Ref.3

Sequence conflict

209

H → N in AAA86314. Ref.4

Sequence conflict

358

E → H in AAA86314. Ref.4

Sequence conflict

364

Missing in AAA86314. Ref.4

Sequence conflict

393

K → P in AAA86314. Ref.4

Sequence conflict

431

H → T in AAB02287. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P17178 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: DC9153BEB6471D63
Show »

FASTA

533

60,733

        10         20         30         40         50         60 
MAVLSRMRLR WALLDTRVMG HGLCPQGARA KAAIPAALRD HESTEGPGTG QDRPRLRSLA 

        70         80         90        100        110        120 
ELPGPGTLRF LFQLFLRGYV LHLHELQALN KAKYGPMWTT TFGTRTNVNL ASAPLLEQVM 

       130        140        150        160        170        180 
RQEGKYPIRD SMEQWKEHRD HKGLSYGIFI TQGQQWYHLR HSLNQRMLKP AEAALYTDAL 

       190        200        210        220        230        240 
NEVISDFIAR LDQVRTESAS GDQVPDVAHL LYHLALEAIC YILFEKRVGC LEPSIPEDTA 

       250        260        270        280        290        300 
TFIRSVGLMF KNSVYVTFLP KWSRPLLPFW KRYMNNWDNI FSFGEKMIHQ KVQEIEAQLQ 

       310        320        330        340        350        360 
AAGPDGVQVS GYLHFLLTKE LLSPQETVGT FPELILAGVD TTSNTLTWAL YHLSKNPEIQ 

       370        380        390        400        410        420 
EALHKEVTGV VPFGKVPQNK DFAHMPLLKA VIKETLRLYP VVPTNSRIIT EKETEINGFL 

       430        440        450        460        470        480 
FPKNTQFVLC HYVVSRDPSV FPEPESFQPH RWLRKREDDN SGIQHPFGSV PFGYGVRSCL 

       490        500        510        520        530 
GRRIAELEMQ LLLSRLIQKY EVVLSPGMGE VKSVSRIVLV PSKKVSLRFL QRQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of cDNA for vitamin D3 25-hydroxylase from rat liver mitochondria." Usui E., Noshiro M., Okuda K. FEBS Lett. 262:135-138(1990) [PubMed: 2318307] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 33-37. Strain: Wistar. Tissue: Liver.
[2]	"A cDNA encoding a rat mitochondrial cytochrome P450 catalyzing both the 26-hydroxylation of cholesterol and 25-hydroxylation of vitamin D3: gonadotropic regulation of the cognate mRNA in ovaries." Su P., Rennert H., Shayiq R.M., Yamamoto R., Zheng Y.-M., Addya S., Strauss J.F. III, Avadhani N.G. DNA Cell Biol. 9:657-667(1990) [PubMed: 2175615] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[3]	"Sequence complementarity between the 5'-terminal regions of mRNAs for rat mitochondrial cytochrome P-450c27/25 and a growth hormone-inducible serine protease inhibitor. A possible gene overlap." Shayiq R.M., Avadhani N.G. J. Biol. Chem. 267:2421-2428(1992) [PubMed: 1733943] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[4]	"Localization of a transcription promoter within the second exon of the cytochrome P-450c27/25 gene for the expression of the major species of two-kilobase mRNA." Mullick J., Addya S., Sucharov C., Avadhani N.G. Biochemistry 34:13729-13742(1995) [PubMed: 7577965] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Prostate.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y07534 Genomic DNA. Translation: CAA68822.1. M38566 mRNA. Translation: AAB02287.1. M73231 mRNA. Translation: AAA41786.1. U17375 U17376 Genomic DNA. Translation: AAA86314.1. Different initiation. BC061848 mRNA. Translation: AAH61848.1.
IPI	IPI00327879.
PIR	B42324. O4RTV3. S09198.
RefSeq	NP_849178.2. NM_178847.2.
UniGene	Rn.94956.
3D structure databases
ProteinModelPortal	P17178.
ModBase	Search...
Protein-protein interaction databases
STRING	P17178.
Proteomic databases
PRIDE	P17178.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000023152; ENSRNOP00000023152; ENSRNOG00000017188.
GeneID	301517.
KEGG	rno:301517.
UCSC	NM_178847. rat.
Organism-specific databases
CTD	1593.
RGD	727915. Cyp27a1.
Phylogenomic databases
eggNOG	roNOG14179.
GeneTree	ENSGT00550000074304.
HOVERGEN	HBG106909.
InParanoid	P17178.
OMA	HFEIKPD.
OrthoDB	EOG4WSW9K.
PhylomeDB	P17178.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-14308.
Gene expression databases
ArrayExpress	P17178.
Genevestigator	P17178.
GermOnline	ENSRNOG00000017188. Rattus norvegicus.
Family and domain databases
InterPro	IPR001128. Cyt_P450. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. [Graphical view]
Gene3D	G3DSA:1.10.630.10. Cyt_P450. 1 hit.
KO	K00488.
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	648887.

Entry information

Entry name

CP27A_RAT

Accession

Primary (citable) accession number: P17178
Secondary accession number(s): Q64615, Q64639

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	November 16, 2011
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents