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Q9DBG1 (CP27A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

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

Catalytic activity

5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol + 3 NADPH + 3 O2 = (25R)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26-oate + 3 NADP+ + 4 H2O.

Cofactor

Heme group By similarity.

Pathway

Hormone biosynthesis; cholecalciferol biosynthesis.

Subcellular location

Mitochondrion membrane By similarity.

Post-translational modification

Acetylation of Lys-125 and Lys-285 is observed in liver mitochondria from fasted mice but not from fed mice.

Sequence similarities

Belongs to the cytochrome P450 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3232Mitochondrion By similarity
Chain33 – 533501Sterol 26-hydroxylase, mitochondrial
PRO_0000003619

Regions

Region386 – 40015Sterol-binding Potential

Sites

Metal binding4791Iron (heme axial ligand) By similarity

Amino acid modifications

Modified residue1251N6-acetyllysine Ref.3
Modified residue2851N6-acetyllysine Ref.3
Modified residue4991N6-acetyllysine Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9DBG1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: A7F808CA505EF4E6

FASTA53360,720
        10         20         30         40         50         60 
MAAWSRTRLR WTLLDPRVVG RGLCPQGARA KATIPAALQA QESTEGPGTG QDRPRLRSPA 

        70         80         90        100        110        120 
ELPGTGTLQF LFQLFLQGYV LHLPDLQVLN KTKYGPMWTT SFGTYTNVNL ASAPLLEQVM 

       130        140        150        160        170        180 
RQEGKYPIRD HMDQWKDHRD HKGLTYGIFI AQGEQWYHLR QALKQRLLKP DEAALYTDAL 

       190        200        210        220        230        240 
NEVISDFITR LDQVRAESES GDQVPDMAHL LYHLALEAIT YILFEKRIGC LKPSIPEDTA 

       250        260        270        280        290        300 
AFIRSVAIMF QNSVYITFLP KWTRPLLPFW KRYLNGWDNI FSFGKKLIDE KVQELKAQLQ 

       310        320        330        340        350        360 
ETGPDGVRVS GYLHFLLTNE LLSTQETIGT FPELLLAGVD TTSNTLTWAL YHLSKSPEIQ 

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

       430        440        450        460        470        480 
FPKNTQFVLC HYVVSRDPSV FPEPNSFQPH RWLRKKEADN PGILHPFGSV PFGYGVRSCL 

       490        500        510        520        530 
GRRIAELEMQ LMLSRLVQKY EIALAPGMGE VKTVSRIVLV PSKKVRLHFL QRQ

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Liver.
[2]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver.
[3]"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.
Mol. Cell 23:607-618(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-125; LYS-285 AND LYS-499, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK004977 mRNA. Translation: BAB23713.1.
BC055028 mRNA. Translation: AAH55028.1.
IPIIPI00119685.
RefSeqNP_077226.2. NM_024264.4.
UniGeneMm.85083.

3D structure databases

ProteinModelPortalQ9DBG1.
SMRQ9DBG1. Positions 57-532.
ModBaseSearch...

PTM databases

PhosphoSiteQ9DBG1.

Proteomic databases

PaxDbQ9DBG1.
PRIDEQ9DBG1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027356; ENSMUSP00000027356; ENSMUSG00000026170.
GeneID104086.
KEGGmmu:104086.
UCSCuc007bna.1. mouse.

Organism-specific databases

CTD1593.
MGIMGI:88594. Cyp27a1.

Phylogenomic databases

eggNOGCOG2124.
GeneTreeENSGT00550000074304.
HOGENOMHOG000253961.
HOVERGENHBG106909.
InParanoidQ9DBG1.
KOK00488.
OMAEVIDDFM.
OrthoDBEOG4WSW9K.

Enzyme and pathway databases

UniPathwayUPA00955.

Gene expression databases

ArrayExpressQ9DBG1.
BgeeQ9DBG1.
GenevestigatorQ9DBG1.
GermOnlineENSMUSG00000026170. Mus musculus.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR00385. P450.
SUPFAMSSF48264. Cytochrome_P450. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio356493.
SOURCESearch...

Entry information

Entry nameCP27A_MOUSE
AccessionPrimary (citable) accession number: Q9DBG1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: June 1, 2001
Last modified: May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents