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Reviewed, UniProtKB/Swiss-Prot P17178 (CP27A_RAT)

Last modified September 2, 2008. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length533 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

Tissue specificity

Expressed in liver, hepatoma, kidney, ovary and epithelial cells of blood vessels.

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
   Technical termDirect protein sequencing

Gene Ontology (GO)

None. [Check GOA]

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Transit peptide1 – 3232Mitochondrion
Chain33 – 533501Cytochrome P450 27, mitochondrial

Regions

Region386 – 40015Sterol-binding Potential

Sites

Metal binding4791Iron (heme axial ligand)

Amino acid modifications

Modified residue1251N6-acetyllysine By similarity
Modified residue4991N6-acetyllysine By similarity

Experimental info

Sequence conflict88 – 969Missing in AAA86314. Ref.4
Sequence conflict167 – 1682ML → IV Ref.3 Ref.4
Sequence conflict2091H → N Ref.3 Ref.4
Sequence conflict3581E → H in AAA86314. Ref.4
Sequence conflict3641Missing in AAA86314. Ref.4
Sequence conflict3931K → P in AAA86314. Ref.4
Sequence conflict4311H → T in AAB02287. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
P17178-1 [UniParc].

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

FASTA53360,733
        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

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References

« Hide '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. 9:657-665(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.

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Cross-references

Sequence databases

Y07534 Genomic DNA. Translation: CAA68822.1.
M38566 mRNA. Translation: AAB02287.1.
M73231 mRNA. Translation: AAA41786.1.
U17375 expand/collapse EMBL AC list , U17363, U17369, U17370, U17371, U17372, U17373, U17374, U17376 Genomic DNA. Translation: AAA86314.1. Different initiation.
BC061848 mRNA. Translation: AAH61848.1.
PIRB42324.
O4RTV3. S09198.
RefSeqNP_849178.2.
UniGeneRn.94956

3D structure databases

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

Genome annotation databases

EnsemblENSRNOG00000017188. Rattus norvegicus. [Contig view]
GeneID301517.
KEGGrno:301517.

Organism-specific databases

RGD727915. Cyp27a1.

Phylogenomic databases

HOVERGENP17178.

Gene expression databases

ArrayExpressP17178.
GermOnlineENSRNOG00000017188. Rattus norvegicus.

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]
ProDomP17178.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

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Entry information

Entry nameCP27A_RAT
AccessionPrimary (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: September 2, 2008
This is version 73 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

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

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