Reviewed, UniProtKB/Swiss-Prot P17177 (CP27A_RABIT)

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
Synonyms:	CYP27

Organism

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	535 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.
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.
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
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 Probable
	Chain	33 – 535	503	Sterol 26-hydroxylase, mitochondrial		PRO_0000003620
Regions
	Region	387 – 401	15	Sterol-binding Potential
Sites
	Metal binding	480	1	Iron (heme axial ligand)
Amino acid modifications
	Modified residue	126	1	N6-acetyllysine By similarity
	Modified residue	286	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P17177-1 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: CC44B9820E2FCCC2	FASTA	535	60,255
	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

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].

Cross-references

Sequence databases
EMBLGenBankDDBJ	J04717 mRNA. Translation: AAA31225.1.
PIR	A33813.
3D structure databases
HSSP	HSSP built from PDB template 1SCC based on UniProtKB P00189.
ModBase	Search...
Genome annotation databases
Ensembl	ENSOCUG00000003377. Oryctolagus cuniculus. [Contig view]
Phylogenomic databases
HOVERGEN	P17177.
Enzyme and pathway databases
BRENDA	1.14.13.15. 255.
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...

Entry information

Entry name

CP27A_RABIT

Accession

Primary (citable) accession number: P17177

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	May 26, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)