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UniProtKB/Swiss-Prot entry P17178


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CP27A_RAT
Primary accession number P17178
Secondary accession numbers Q64615 Q64639
Integrated into Swiss-Prot on August 1, 1990
Sequence was last modified on August 1, 1990 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 74)
Name and origin of the protein
Protein name Cytochrome P450 27, mitochondrial [Precursor]
Synonyms EC 1.14.13.15
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 name
Name: Cyp27a1
Synonyms: Cyp27
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 33-37.
STRAIN=Wistar;
TISSUE=Liver;
DOI=10.1016/0014-5793(90)80172-F; PubMed=2318307 [NCBI, ExPASy, EBI, Israel, Japan]
Usui E., Noshiro M., Okuda K.;
"Molecular cloning of cDNA for vitamin D3 25-hydroxylase from rat liver mitochondria.";
FEBS Lett. 262:135-138(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=2175615 [NCBI, ExPASy, EBI, Israel, Japan]
Su P., Rennert H., Shayiq R.M., Yamamoto R., Zheng Y.-M., Addya S., Strauss J.F. III, Avadhani N.G.;
"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.";
DNA Cell Biol. 9:657-665(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=1733943 [NCBI, ExPASy, EBI, Israel, Japan]
Shayiq R.M., Avadhani N.G.;
"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.";
J. Biol. Chem. 267:2421-2428(1992).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1021/bi00042a003; PubMed=7577965 [NCBI, ExPASy, EBI, Israel, Japan]
Mullick J., Addya S., Sucharov C., Avadhani N.G.;
"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.";
Biochemistry 34:13729-13742(1995).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y07534; CAA68822.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M38566; AAB02287.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M73231; AAA41786.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U17375; AAA86314.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U17363; AAA86314.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U17369; AAA86314.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U17370; AAA86314.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U17371; AAA86314.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U17372; AAA86314.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U17373; AAA86314.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U17374; AAA86314.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U17376; AAA86314.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC061848; AAH61848.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B42324; B42324.
S09198; O4RTV3.
RefSeq NP_849178.2; -.
UniGene Rn.94956
3D structure databases
HSSP P00189; 1SCC. [HSSP ENTRY / PDB]
ModBase P17178.
Organism-specific databases
RGD 727915; Cyp27a1.
Gene expression databases
ArrayExpress P17178; -.
GermOnline ENSRNOG00000017188; Rattus norvegicus.
Ontologies
GO
GO:0047749; Molecular function: cholestanetriol 26-monooxygenase activity (inferred from electronic annotation from EC).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001128; Cyt_P450.
IPR002401; Cyt_P450_E_grp-I.
Graphical view of domain structure.
Gene3D G3DSA:1.10.630.10; Cyt_P450; 1.
PANTHER PTHR19383; Cyt_P450; 1.
Pfam PF00067; p450; 1.
Pfam graphical view of domain structure.
PRINTS PR00463; EP450I.
PR00385; P450.
PROSITE PS00086; CYTOCHROME_P450; 1.
BLOCKS P17178.
ProtoNet P17178.
Genome annotation databases
Ensembl ENSRNOG00000017188; Rattus norvegicus. [Contig view]
GeneID 301517; -.
KEGG rno:301517; -.
Phylogenomic databases
HOVERGEN P17178; -.
Other
NextBio 648887; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Direct protein sequencing; Heme; Iron; Membrane; Metal-binding; Mitochondrion; Monooxygenase; NADP; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    32  32     Mitochondrion. 
CHAIN   33   533  501     Cytochrome P450 27, mitochondrial. PRO_0000003621
REGION   386   400  15     Sterol-binding (Potential). 
METAL   479   479        Iron (heme axial ligand). 
MOD_RES   125   125        N6-acetyllysine (By similarity). 
MOD_RES   499   499        N6-acetyllysine (By similarity). 
CONFLICT   88    96        Missing (in Ref. 4; AAA86314). 
CONFLICT   167   168        ML -> IV (in Ref. 3 and 4). 
CONFLICT   209   209        H -> N (in Ref. 3 and 4). 
CONFLICT   358   358        E -> H (in Ref. 4; AAA86314). 
CONFLICT   364   364        Missing (in Ref. 4; AAA86314). 
CONFLICT   393   393        K -> P (in Ref. 4; AAA86314). 
CONFLICT   431   431        H -> T (in Ref. 2; AAB02287). 
Sequence information
Length: 533 AA [This is the length of the unprocessed precursor] Molecular weight: 60733 Da [This is the MW of the unprocessed precursor] CRC64: DC9153BEB6471D63 [This is a checksum on the sequence]
        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 

P17178 in FASTA format

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View entry in raw text format (no links)
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