Reviewed, UniProtKB/Swiss-Prot Q9DBG1 (CP27A_MOUSE)

Names and origin

Protein names

Recommended name:
    Sterol 26-hydroxylase, mitochondrial
    EC=1.14.13.15
Alternative name(s):
    Cytochrome P450 27
    Cytochrome P-450C27/25
    Sterol 27-hydroxylase
    Vitamin D(3) 25-hydroxylase
    5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 27-hydroxylase

Gene names

Name:

Cyp27a1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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 By similarity.
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 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.

Ontologies

Keywords
Cellular component	Membrane Mitochondrion
Domain	Transit peptide
Ligand	Heme Iron Metal-binding NADP
Molecular function	Monooxygenase Oxidoreductase
PTM	Acetylation
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial inner membrane Inferred from direct assay. Source: MGI
Molecular function	cholestanetriol 26-monooxygenase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 32	32	Mitochondrion By similarity
	Chain	33 – 533	501	Sterol 26-hydroxylase, mitochondrial		PRO_0000003619
Regions
	Region	386 – 400	15	Sterol-binding Potential
Sites
	Metal binding	479	1	Iron (heme axial ligand) By similarity
Amino acid modifications
	Modified residue	125	1	N6-acetyllysine Ref.3
	Modified residue	285	1	N6-acetyllysine Ref.3
	Modified residue	499	1	N6-acetyllysine Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9DBG1-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: A7F808CA505EF4E6	FASTA	533	60,720
	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

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. , 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: 16141072] [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: 15489334] [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: 16916647] [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
EMBLGenBankDDBJ	AK004977 mRNA. Translation: BAB23713.1. BC055028 mRNA. Translation: AAH55028.1.
IPI	IPI00119685.
RefSeq	NP_077226.2.
UniGene	Mm.85083
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q9DBG1.
Proteomic databases
PRIDE	Q9DBG1.
Genome annotation databases
Ensembl	ENSMUSG00000026170. Mus musculus. [Contig view]
GeneID	104086.
KEGG	mmu:104086.
Organism-specific databases
MGI	MGI:88594. Cyp27a1.
Phylogenomic databases
HOGENOM	Q9DBG1.
HOVERGEN	Q9DBG1.
OMA	Q9DBG1. FYYFALE.
Enzyme and pathway databases
BRENDA	1.14.13.15. 244.
Gene expression databases
ArrayExpress	Q9DBG1.
Bgee	Q9DBG1.
GermOnline	ENSMUSG00000026170. Mus musculus.
Family and domain databases
InterPro	IPR001128. Cyt_P450. IPR017973. Cyt_P450_C. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. [Graphical view]
Gene3D	G3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHER	PTHR19383. Cyt_P450. 1 hit.
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00463. EP450I. PR00385. P450.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	356493.
SOURCE	Search...

Entry information

Entry name

CP27A_MOUSE

Accession

Primary (citable) accession number: Q9DBG1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2003
Last sequence update:	June 1, 2001
Last modified:	June 16, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)