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Q64505

- CP7A1_MOUSE

UniProt

Q64505 - CP7A1_MOUSE

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Protein

Cholesterol 7-alpha-monooxygenase

Gene
Cyp7a1, Cyp7
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

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.1 Publication

Catalytic activityi

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

Cofactori

Heme group By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi444 – 4441Iron (heme axial ligand) By similarity

GO - Molecular functioni

  1. cholesterol 7-alpha-monooxygenase activity Source: UniProtKB
  2. heme binding Source: InterPro
  3. iron ion binding Source: InterPro

GO - Biological processi

  1. bile acid biosynthetic process Source: UniProtKB
  2. cellular response to cholesterol Source: UniProtKB
  3. cellular response to glucose stimulus Source: UniProtKB
  4. cholesterol catabolic process Source: UniProtKB
  5. cholesterol homeostasis Source: UniProtKB
  6. positive regulation of bile acid biosynthetic process Source: BHF-UCL
  7. regulation of bile acid biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism

Keywords - Ligandi

Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

ReactomeiREACT_198602. PPARA activates gene expression.
REACT_203193. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_227038. Endogenous sterols.
UniPathwayiUPA00221.

Names & Taxonomyi

Protein namesi
Recommended name:
Cholesterol 7-alpha-monooxygenase (EC:1.14.13.17)
Alternative name(s):
CYPVII
Cholesterol 7-alpha-hydroxylase
Cytochrome P450 7A1
Gene namesi
Name:Cyp7a1
Synonyms:Cyp7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:106091. Cyp7a1.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. intracellular membrane-bounded organelle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 503503Cholesterol 7-alpha-monooxygenasePRO_0000051902Add
BLAST

Proteomic databases

MaxQBiQ64505.
PaxDbiQ64505.
PRIDEiQ64505.

PTM databases

PhosphoSiteiQ64505.

Expressioni

Inductioni

Up-regulated by fasting, returns to ground state upon feeding. Up-regulated by experimentally induced diabetes. Down-regulated by insulin treatment.2 Publications

Gene expression databases

BgeeiQ64505.
GenevestigatoriQ64505.

Structurei

3D structure databases

ProteinModelPortaliQ64505.
SMRiQ64505. Positions 25-503.

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.

Phylogenomic databases

eggNOGiCOG2124.
GeneTreeiENSGT00550000074551.
HOGENOMiHOG000231026.
HOVERGENiHBG051100.
InParanoidiQ8BFR7.
KOiK00489.
OMAiFHYTTSA.
OrthoDBiEOG7J9VP6.
TreeFamiTF105090.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR024204. Cyt_P450_CYP7A1-type.
IPR002403. Cyt_P450_E_grp-IV.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PIRSFiPIRSF000047. Cytochrome_CYPVIIA1. 1 hit.
PRINTSiPR00465. EP450IV.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q64505-1 [UniParc]FASTAAdd to Basket

« Hide

MMSISLIWGI AVVVSCCIWF IIGIRRRKVG EPPLDNGLIP YLGCALKFGS    50
NPLEFLRAKQ RKHGHVFTCK LMGKYVHFIT NSLSYHKVLC HGKYFDWKKF 100
HYTTSAKAFG HRSIDPSDGN TTENINKTFN KTLQGDALCS LSEAMMQNLQ 150
SVMRPPGLPK SKSAVWVTEG MYAFCYRVMF EAGYLTLFGK DISKTDSQRA 200
FIQNNLDSFK QFDQVFPALV AGVPIHLFKT AHKARERLAE SLKHKNLYMR 250
DQVSELIRLR MFLNDTLSTF DDMEKAKTHL VILWASQANT IPATFWSLFQ 300
MIRSPEAMKA ASEEVNGALQ SAGQELSSGG NAIYLDQEQL NNLPVLDSII 350
KEALRLSSAS LNIRTAKEDF TLHLEDGSYN IRKDDIIALY PQLMHLDPEI 400
YPDPLTFKYD RYLDESGKAK TTFYRNGNKL KYFYMPFGSG ATICPGRLFA 450
VQEIKQFLIL MLSYFELELV ESHTKCPPLD QSRAGLGILP PLNDIEFKYK 500
LKH 503
Length:503
Mass (Da):57,262
Last modified:July 27, 2011 - v2
Checksum:iF7F8BC2CDD2C43D1
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti197 – 1971S → T in AAA68867. 1 Publication
Sequence conflicti228 – 2281F → L in AAA68867. 1 Publication
Sequence conflicti318 – 3181A → S in AAA68867. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS17950.1.
PIRiA54779.
RefSeqiNP_031850.2. NM_007824.2.
XP_006537666.1. XM_006537603.1.
UniGeneiMm.57029.

Genome annotation databases

EnsembliENSMUST00000029905; ENSMUSP00000029905; ENSMUSG00000028240.
GeneIDi13122.
KEGGimmu:13122.
UCSCiuc008rxk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS17950.1.
PIRi A54779.
RefSeqi NP_031850.2. NM_007824.2.
XP_006537666.1. XM_006537603.1.
UniGenei Mm.57029.

3D structure databases

ProteinModelPortali Q64505.
SMRi Q64505. Positions 25-503.
ModBasei Search...
MobiDBi Search...

Chemistry

ChEMBLi CHEMBL2212.

PTM databases

PhosphoSitei Q64505.

Proteomic databases

MaxQBi Q64505.
PaxDbi Q64505.
PRIDEi Q64505.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000029905 ; ENSMUSP00000029905 ; ENSMUSG00000028240 .
GeneIDi 13122.
KEGGi mmu:13122.
UCSCi uc008rxk.1. mouse.

Organism-specific databases

CTDi 1581.
MGIi MGI:106091. Cyp7a1.

Phylogenomic databases

eggNOGi COG2124.
GeneTreei ENSGT00550000074551.
HOGENOMi HOG000231026.
HOVERGENi HBG051100.
InParanoidi Q8BFR7.
KOi K00489.
OMAi FHYTTSA.
OrthoDBi EOG7J9VP6.
TreeFami TF105090.

Enzyme and pathway databases

UniPathwayi UPA00221 .
Reactomei REACT_198602. PPARA activates gene expression.
REACT_203193. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_227038. Endogenous sterols.

Miscellaneous databases

NextBioi 283162.
PROi Q64505.
SOURCEi Search...

Gene expression databases

Bgeei Q64505.
Genevestigatori Q64505.

Family and domain databases

Gene3Di 1.10.630.10. 1 hit.
InterProi IPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR024204. Cyt_P450_CYP7A1-type.
IPR002403. Cyt_P450_E_grp-IV.
[Graphical view ]
Pfami PF00067. p450. 1 hit.
[Graphical view ]
PIRSFi PIRSF000047. Cytochrome_CYPVIIA1. 1 hit.
PRINTSi PR00465. EP450IV.
SUPFAMi SSF48264. SSF48264. 1 hit.
PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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.
    , 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.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY FASTING.

Entry informationi

Entry nameiCP7A1_MOUSE
AccessioniPrimary (citable) accession number: Q64505
Secondary accession number(s): Q8BFR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 110 of the entry and version 2 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

External Data

Dasty 3

Similar proteinsi