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Reviewed, UniProtKB/Swiss-Prot P17177 (CP27A_RABIT)

Last modified July 22, 2008. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Cytochrome P450 27, mitochondrial
    EC=1.14.13.15
Alternative name(s):
    Cytochrome P-450C27/25
    Sterol 26-hydroxylase
    Sterol 27-hydroxylase
    Vitamin D(3) 25-hydroxylase
    5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 27-hydroxylase
Gene names
Name: CYP27A1
Synonyms: CYP27
OrganismOryctolagus cuniculus (Rabbit)
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

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Protein attributes

Sequence length535 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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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 + O(2) = (25R)-5-beta-cholestane-3-alpha,7-alpha,12-alpha,26-tetraol + NADP(+) + H(2)O.

Cofactor

Heme group By similarity.

Pathway

Hormone biosynthesis; cholecalciferol biosynthesis.

Subcellular location

Mitochondrion membrane.

Sequence similarities

Belongs to the cytochrome P450 family.

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Ontologies

Keywords

   Cellular componentMembrane
Mitochondrion
   DomainTransit peptide
   LigandHeme
Iron
Metal-binding
NADP
   Molecular functionMonooxygenase
Oxidoreductase
   PTMAcetylation

Gene Ontology (GO)

   Molecular functioncholestanetriol 26-monooxygenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Transit peptide1 – 3232Mitochondrion Probable
Chain33 – 535503Cytochrome P450 27, mitochondrial

Regions

Region387 – 40115Sterol-binding Potential

Sites

Metal binding4801Iron (heme axial ligand)

Amino acid modifications

Modified residue1261N6-acetyllysine By similarity
Modified residue2861N6-acetyllysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
P17177-1 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: CC44B9820E2FCCC2

FASTA53560,255
        10         20         30         40         50         60 
MAALGCARLR WALLGPRVAG CGLCPQGARA KAAIPTALPA DEAAQAPGAG PGDRRRRRSL 

        70         80         90        100        110        120 
EELPRLGQLR FFYQAFVQGY LLHLHKLQVL NKARYGPMWV SYLGPQLFVN LASAPLVETV 

       130        140        150        160        170        180 
MRQEGKYPVR NDMQLWKEHR DHQDLAYGVF TTDGHDWYQL RQALNQRLLK PAEAALYTDA 

       190        200        210        220        230        240 
LNEVIDSFVV RLDQLRAESA SGDQVPDMAD LLYHFALEAI CYILFEKRIG CLEASIPKDT 

       250        260        270        280        290        300 
ENFIRSVGLM FQNSVYVTFL PKWTRPLLPF WKRYLDGWDT IFSFGKNLID QKLQEVVAQL 

       310        320        330        340        350        360 
QSAGSDGVQV SGYLHSLLTS GQLSPREALG SLPELLLAGV DTTSNTLTWA LYHLSKNPEI 

       370        380        390        400        410        420 
QAALRKEVVG VVAAGQVPQH KDFAHMPLLK AVLKETLRLY PVIPANSRII VDKEIEVGGF 

       430        440        450        460        470        480 
LFPKNTQFVF CHYVTSRDPS TFSEPDTFWP YRWLRKGQPE TSKTQHPFGS VPFGYGVRAC 

       490        500        510        520        530 
LGRRIAELEM QLLLARLIQR YELMLAPETG EVQSVARIVL VPNKKVGLRF LPTQR

« Hide

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References

[1]"Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme."
Andersson S., Davis D.L., Dahlbaeck H., Joernvall H., Russell D.W.
J. Biol. Chem. 264:8222-8229(1989) [PubMed: 2722778] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

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Cross-references

Sequence databases

J04717 mRNA. Translation: AAA31225.1.
PIRA33813.

3D structure databases

HSSPHSSP built from PDB template 1SCC based on UniProtKB P00189.
ModBaseSearch...

Genome annotation databases

EnsemblENSOCUG00000003377. Oryctolagus cuniculus. [Contig view]

Phylogenomic databases

HOVERGENP17177.

Family and domain databases

InterProIPR001128. Cyt_P450.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
Gene3DG3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHERPTHR19383. Cyt_P450. 1 hit.
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR00385. P450.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProDomP17177.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

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Entry information

Entry nameCP27A_RABIT
AccessionPrimary (citable) accession number: P17177
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: July 22, 2008
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents