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Q64505 (CP7A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 87. 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:
Cholesterol 7-alpha-monooxygenase
EC=1.14.13.17
Alternative name(s):
CYPVII
Cholesterol 7-alpha-hydroxylase
Cytochrome P450 7A1
Gene names
Name:Cyp7a1
Synonyms:Cyp7
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length503 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes a rate-limiting step in cholesterol catabolism and bile acid biosynthesis by introducing a hydrophilic moiety at position 7 of cholesterol. Important for cholesterol homeostasis. Ref.4

Catalytic activity

Cholesterol + NADPH + O2 = 7-alpha-hydroxycholesterol + NADP+ + H2O.

Cofactor

Heme group By similarity.

Pathway

Lipid metabolism; bile acid biosynthesis.

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.

Induction

Up-regulated by fasting, returns to ground state upon feeding. Up-regulated by experimentally induced diabetes. Down-regulated by insulin treatment. Ref.4 Ref.5

Sequence similarities

Belongs to the cytochrome P450 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 503503Cholesterol 7-alpha-monooxygenase
PRO_0000051902

Sites

Metal binding4441Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict1971S → T in AAA68867. Ref.1
Sequence conflict2281F → L in AAA68867. Ref.1
Sequence conflict3181A → S in AAA68867. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q64505 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: F7F8BC2CDD2C43D1

FASTA50357,262
        10         20         30         40         50         60 
MMSISLIWGI AVVVSCCIWF IIGIRRRKVG EPPLDNGLIP YLGCALKFGS NPLEFLRAKQ 

        70         80         90        100        110        120 
RKHGHVFTCK LMGKYVHFIT NSLSYHKVLC HGKYFDWKKF HYTTSAKAFG HRSIDPSDGN 

       130        140        150        160        170        180 
TTENINKTFN KTLQGDALCS LSEAMMQNLQ SVMRPPGLPK SKSAVWVTEG MYAFCYRVMF 

       190        200        210        220        230        240 
EAGYLTLFGK DISKTDSQRA FIQNNLDSFK QFDQVFPALV AGVPIHLFKT AHKARERLAE 

       250        260        270        280        290        300 
SLKHKNLYMR DQVSELIRLR MFLNDTLSTF DDMEKAKTHL VILWASQANT IPATFWSLFQ 

       310        320        330        340        350        360 
MIRSPEAMKA ASEEVNGALQ SAGQELSSGG NAIYLDQEQL NNLPVLDSII KEALRLSSAS 

       370        380        390        400        410        420 
LNIRTAKEDF TLHLEDGSYN IRKDDIIALY PQLMHLDPEI YPDPLTFKYD RYLDESGKAK 

       430        440        450        460        470        480 
TTFYRNGNKL KYFYMPFGSG ATICPGRLFA VQEIKQFLIL MLSYFELELV ESHTKCPPLD 

       490        500 
QSRAGLGILP PLNDIEFKYK LKH

« Hide

References

« Hide 'large scale' references
[1]"Structure of the mouse cholesterol 7 alpha-hydroxylase gene."
Tzung K.W., Ishimura-Oka K., Kihara S., Oka K., Chan L.
Genomics 21:244-247(1994) [PubMed: 8088795] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Liver.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6.
[4]"PGC-1alpha activates CYP7A1 and bile acid biosynthesis."
Shin D.J., Campos J.A., Gil G., Osborne T.F.
J. Biol. Chem. 278:50047-50052(2003) [PubMed: 14522988] [Abstract]
Cited for: FUNCTION, INDUCTION BY FASTING.
[5]"Functional interaction of hepatic nuclear factor-4 and peroxisome proliferator-activated receptor-gamma coactivator 1alpha in CYP7A1 regulation is inhibited by a key lipogenic activator, sterol regulatory element-binding protein-1c."
Ponugoti B., Fang S., Kemper J.K.
Mol. Endocrinol. 21:2698-2712(2007) [PubMed: 17636037] [Abstract]
Cited for: INDUCTION BY FASTING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L23754 Genomic DNA. Translation: AAA68867.1.
AK050020 mRNA. Translation: BAC34033.1.
AK050210 mRNA. Translation: BAC34123.1.
AK050220 mRNA. Translation: BAC34131.1.
AK050260 mRNA. Translation: BAC34150.1.
AL772306 Genomic DNA. Translation: CAM27235.1.
IPIIPI00135398.
PIRA54779.
RefSeqNP_031850.2. NM_007824.2.
UniGeneMm.57029.

3D structure databases

ProteinModelPortalQ64505.
SMRQ64505. Positions 25-503.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ64505.

PTM databases

PhosphoSiteQ64505.

Proteomic databases

PRIDEQ64505.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029905; ENSMUSP00000029905; ENSMUSG00000028240.
GeneID13122.
KEGGmmu:13122.

Organism-specific databases

CTD1581.
MGIMGI:106091. Cyp7a1.

Phylogenomic databases

HOGENOMHBG446017.
HOVERGENHBG051100.
InParanoidQ64505.
OrthoDBEOG4B5P4W.
PhylomeDBQ64505.

Gene expression databases

ArrayExpressQ64505.
BgeeQ64505.
GenevestigatorQ64505.
GermOnlineENSMUSG00000028240. Mus musculus.

Family and domain databases

InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR024204. Cyt_P450_CYP7A1-type.
IPR002403. Cyt_P450_E_grp-IV.
[Graphical view]
Gene3DG3DSA:1.10.630.10. Cyt_P450. 1 hit.
KOK00489.
PfamPF00067. p450. 1 hit.
[Graphical view]
PIRSFPIRSF000047. Cytochrome_CYPVIIA1. 1 hit.
PRINTSPR00465. EP450IV.
SUPFAMSSF48264. Cytochrome_P450. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

SOURCESearch...

Entry information

Entry nameCP7A1_MOUSE
AccessionPrimary (citable) accession number: Q64505
Secondary accession number(s): Q8BFR7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 27, 2011
Last modified: December 14, 2011
This is version 87 of the entry and version 2 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