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Protein

Sterol 26-hydroxylase, mitochondrial

Gene

CYP27A1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol + 6 reduced adrenodoxin + 6 H+ + 3 O2 = (25R)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26-oate + 6 oxidized adrenodoxin + 4 H2O.1 Publication

Cofactori

hemeBy similarity

Pathwayi: cholecalciferol biosynthesis

This protein is involved in the pathway cholecalciferol biosynthesis, which is part of Hormone biosynthesis.
View all proteins of this organism that are known to be involved in the pathway cholecalciferol biosynthesis and in Hormone biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi480 – 4801Iron (heme axial ligand)

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

UniPathwayiUPA00955.

Names & Taxonomyi

Protein namesi
Recommended name:
Sterol 26-hydroxylase, mitochondrial (EC:1.14.15.151 Publication)
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 namesi
Name:CYP27A1
Synonyms:CYP27
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3636Mitochondrion1 PublicationAdd
BLAST
Chaini37 – 535499Sterol 26-hydroxylase, mitochondrialPRO_0000003620Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei286 – 2861N6-acetyllysineBy similarity
Modified residuei524 – 5241N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Expressioni

Tissue specificityi

Expressed in all tissues tested. Highest expression in liver and duodenum, followed by adrenal gland and lung. Low expression in kidney and spleen.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000002930.

Structurei

3D structure databases

ProteinModelPortaliP17177.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni387 – 40115Sterol-bindingSequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0159. Eukaryota.
COG2124. LUCA.
HOGENOMiHOG000253961.
HOVERGENiHBG106909.
InParanoidiP17177.
KOiK00488.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P17177-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALGCARLR WALLGPRVAG CGLCPQGARA KAAIPTALPA DEAAQAPGAG
60 70 80 90 100
PGDRRRRRSL EELPRLGQLR FFYQAFVQGY LLHLHKLQVL NKARYGPMWV
110 120 130 140 150
SYLGPQLFVN LASAPLVETV MRQEGKYPVR NDMQLWKEHR DHQDLAYGVF
160 170 180 190 200
TTDGHDWYQL RQALNQRLLK PAEAALYTDA LNEVIDSFVV RLDQLRAESA
210 220 230 240 250
SGDQVPDMAD LLYHFALEAI CYILFEKRIG CLEASIPKDT ENFIRSVGLM
260 270 280 290 300
FQNSVYVTFL PKWTRPLLPF WKRYLDGWDT IFSFGKNLID QKLQEVVAQL
310 320 330 340 350
QSAGSDGVQV SGYLHSLLTS GQLSPREALG SLPELLLAGV DTTSNTLTWA
360 370 380 390 400
LYHLSKNPEI QAALRKEVVG VVAAGQVPQH KDFAHMPLLK AVLKETLRLY
410 420 430 440 450
PVIPANSRII VDKEIEVGGF LFPKNTQFVF CHYVTSRDPS TFSEPDTFWP
460 470 480 490 500
YRWLRKGQPE TSKTQHPFGS VPFGYGVRAC LGRRIAELEM QLLLARLIQR
510 520 530
YELMLAPETG EVQSVARIVL VPNKKVGLRF LPTQR
Length:535
Mass (Da):60,255
Last modified:August 1, 1990 - v1
Checksum:iCC44B9820E2FCCC2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04717 mRNA. Translation: AAA31225.1.
PIRiA33813.
RefSeqiNP_001177359.1. NM_001190430.1.
UniGeneiOcu.1859.

Genome annotation databases

GeneIDi100348736.
KEGGiocu:100348736.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04717 mRNA. Translation: AAA31225.1.
PIRiA33813.
RefSeqiNP_001177359.1. NM_001190430.1.
UniGeneiOcu.1859.

3D structure databases

ProteinModelPortaliP17177.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000002930.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100348736.
KEGGiocu:100348736.

Organism-specific databases

CTDi1593.

Phylogenomic databases

eggNOGiKOG0159. Eukaryota.
COG2124. LUCA.
HOGENOMiHOG000253961.
HOVERGENiHBG106909.
InParanoidiP17177.
KOiK00488.

Enzyme and pathway databases

UniPathwayiUPA00955.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 37-51; 357-365; 367-380; 414-424; 505-521 AND 526-535, FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.

Entry informationi

Entry nameiCP27A_RABIT
AccessioniPrimary (citable) accession number: P17177
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: June 8, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.