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Protein

Sterol 26-hydroxylase, mitochondrial

Gene

Cyp27a1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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.By similarity

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.By similarity

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 bindingi479 – 4791Iron (heme axial ligand)By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

ReactomeiR-MMU-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
R-MMU-193775. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
R-MMU-193807. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
R-MMU-211976. Endogenous sterols.
UniPathwayiUPA00955.

Names & Taxonomyi

Protein namesi
Recommended name:
Sterol 26-hydroxylase, mitochondrial (EC:1.14.15.15By similarity)
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:88594. Cyp27a1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3232MitochondrionBy similarityAdd
BLAST
Chaini33 – 533501Sterol 26-hydroxylase, mitochondrialPRO_0000003619Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei142 – 1421N6-acetyllysineCombined sources
Modified residuei232 – 2321N6-acetyllysineCombined sources
Modified residuei285 – 2851N6-acetyllysineCombined sources
Modified residuei296 – 2961N6-acetyllysineCombined sources
Modified residuei375 – 3751N6-acetyllysineCombined sources
Modified residuei512 – 5121N6-acetyllysineCombined sources
Modified residuei523 – 5231N6-acetyllysineCombined sources

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9DBG1.
MaxQBiQ9DBG1.
PaxDbiQ9DBG1.
PRIDEiQ9DBG1.

PTM databases

iPTMnetiQ9DBG1.
PhosphoSiteiQ9DBG1.
SwissPalmiQ9DBG1.

Expressioni

Gene expression databases

BgeeiQ9DBG1.
GenevisibleiQ9DBG1. MM.

Interactioni

Protein-protein interaction databases

MINTiMINT-1860912.
STRINGi10090.ENSMUSP00000027356.

Structurei

3D structure databases

ProteinModelPortaliQ9DBG1.
SMRiQ9DBG1. Positions 57-532.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni386 – 40015Sterol-bindingSequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0159. Eukaryota.
COG2124. LUCA.
GeneTreeiENSGT00760000119243.
HOGENOMiHOG000253961.
HOVERGENiHBG106909.
InParanoidiQ9DBG1.
KOiK00488.
OMAiCPQGARA.
OrthoDBiEOG7ZGX4B.
PhylomeDBiQ9DBG1.
TreeFamiTF105094.

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.

Q9DBG1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAWSRTRLR WTLLDPRVVG RGLCPQGARA KATIPAALQA QESTEGPGTG
60 70 80 90 100
QDRPRLRSPA ELPGTGTLQF LFQLFLQGYV LHLPDLQVLN KTKYGPMWTT
110 120 130 140 150
SFGTYTNVNL ASAPLLEQVM RQEGKYPIRD HMDQWKDHRD HKGLTYGIFI
160 170 180 190 200
AQGEQWYHLR QALKQRLLKP DEAALYTDAL NEVISDFITR LDQVRAESES
210 220 230 240 250
GDQVPDMAHL LYHLALEAIT YILFEKRIGC LKPSIPEDTA AFIRSVAIMF
260 270 280 290 300
QNSVYITFLP KWTRPLLPFW KRYLNGWDNI FSFGKKLIDE KVQELKAQLQ
310 320 330 340 350
ETGPDGVRVS GYLHFLLTNE LLSTQETIGT FPELLLAGVD TTSNTLTWAL
360 370 380 390 400
YHLSKSPEIQ EALHKEVTGV VPFGKVPQHK DFAHMPLLKA VIKETLRLYP
410 420 430 440 450
VVPTNSRIIT EKETEINGFL FPKNTQFVLC HYVVSRDPSV FPEPNSFQPH
460 470 480 490 500
RWLRKKEADN PGILHPFGSV PFGYGVRSCL GRRIAELEMQ LMLSRLVQKY
510 520 530
EIALAPGMGE VKTVSRIVLV PSKKVRLHFL QRQ
Length:533
Mass (Da):60,720
Last modified:June 1, 2001 - v1
Checksum:iA7F808CA505EF4E6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004977 mRNA. Translation: BAB23713.1.
BC055028 mRNA. Translation: AAH55028.1.
CCDSiCCDS15054.1.
RefSeqiNP_077226.2. NM_024264.5.
UniGeneiMm.85083.

Genome annotation databases

EnsembliENSMUST00000027356; ENSMUSP00000027356; ENSMUSG00000026170.
GeneIDi104086.
KEGGimmu:104086.
UCSCiuc007bna.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004977 mRNA. Translation: BAB23713.1.
BC055028 mRNA. Translation: AAH55028.1.
CCDSiCCDS15054.1.
RefSeqiNP_077226.2. NM_024264.5.
UniGeneiMm.85083.

3D structure databases

ProteinModelPortaliQ9DBG1.
SMRiQ9DBG1. Positions 57-532.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1860912.
STRINGi10090.ENSMUSP00000027356.

PTM databases

iPTMnetiQ9DBG1.
PhosphoSiteiQ9DBG1.
SwissPalmiQ9DBG1.

Proteomic databases

EPDiQ9DBG1.
MaxQBiQ9DBG1.
PaxDbiQ9DBG1.
PRIDEiQ9DBG1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027356; ENSMUSP00000027356; ENSMUSG00000026170.
GeneIDi104086.
KEGGimmu:104086.
UCSCiuc007bna.1. mouse.

Organism-specific databases

CTDi1593.
MGIiMGI:88594. Cyp27a1.

Phylogenomic databases

eggNOGiKOG0159. Eukaryota.
COG2124. LUCA.
GeneTreeiENSGT00760000119243.
HOGENOMiHOG000253961.
HOVERGENiHBG106909.
InParanoidiQ9DBG1.
KOiK00488.
OMAiCPQGARA.
OrthoDBiEOG7ZGX4B.
PhylomeDBiQ9DBG1.
TreeFamiTF105094.

Enzyme and pathway databases

UniPathwayiUPA00955.
ReactomeiR-MMU-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
R-MMU-193775. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
R-MMU-193807. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
R-MMU-211976. Endogenous sterols.

Miscellaneous databases

NextBioi356493.
PROiQ9DBG1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DBG1.
GenevisibleiQ9DBG1. MM.

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. "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] [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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue and Liver.
  4. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-142; LYS-232; LYS-285; LYS-296; LYS-375; LYS-512 AND LYS-523, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCP27A_MOUSE
AccessioniPrimary (citable) accession number: Q9DBG1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 121 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, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.