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Cholesterol 7-alpha-monooxygenase (EC 1.14.14.23) (CYPVII) (Cholesterol 7-alpha-hydroxylase) (Cytochrome P450 7A1)

 CP7A1_MOUSE             Reviewed;         503 AA.
Q64505; Q8BFR7;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
12-SEP-2018, entry version 134.
RecName: Full=Cholesterol 7-alpha-monooxygenase;
EC=1.14.14.23 {ECO:0000250|UniProtKB:P18125};
AltName: Full=CYPVII;
AltName: Full=Cholesterol 7-alpha-hydroxylase;
AltName: Full=Cytochrome P450 7A1;
Name=Cyp7a1; Synonyms=Cyp7;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8088795; DOI=10.1006/geno.1994.1250;
Tzung K.W., Ishimura-Oka K., Kihara S., Oka K., Chan L.;
"Structure of the mouse cholesterol 7 alpha-hydroxylase gene.";
Genomics 21:244-247(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Liver;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
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., 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.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
FUNCTION, AND INDUCTION BY FASTING.
PubMed=14522988; DOI=10.1074/jbc.M309736200;
Shin D.J., Campos J.A., Gil G., Osborne T.F.;
"PGC-1alpha activates CYP7A1 and bile acid biosynthesis.";
J. Biol. Chem. 278:50047-50052(2003).
[5]
INDUCTION BY FASTING.
PubMed=17636037; DOI=10.1210/me.2007-0196;
Ponugoti B., Fang S., Kemper J.K.;
"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.";
Mol. Endocrinol. 21:2698-2712(2007).
-!- 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.
{ECO:0000269|PubMed:14522988}.
-!- CATALYTIC ACTIVITY: Cholesterol + [reduced NADPH--hemoprotein
reductase] + O(2) = 7-alpha-hydroxycholesterol + [oxidized NADPH--
hemoprotein reductase] + H(2)O. {ECO:0000250|UniProtKB:P18125}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
-!- 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. {ECO:0000269|PubMed:14522988,
ECO:0000269|PubMed:17636037}.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L23754; AAA68867.1; -; Genomic_DNA.
EMBL; AK050020; BAC34033.1; -; mRNA.
EMBL; AK050210; BAC34123.1; -; mRNA.
EMBL; AK050220; BAC34131.1; -; mRNA.
EMBL; AK050260; BAC34150.1; -; mRNA.
EMBL; AL772306; CAM27235.1; -; Genomic_DNA.
CCDS; CCDS17950.1; -.
PIR; A54779; A54779.
RefSeq; NP_031850.2; NM_007824.2.
RefSeq; XP_006537666.1; XM_006537603.1.
UniGene; Mm.57029; -.
ProteinModelPortal; Q64505; -.
SMR; Q64505; -.
STRING; 10090.ENSMUSP00000029905; -.
ChEMBL; CHEMBL2212; -.
iPTMnet; Q64505; -.
PhosphoSitePlus; Q64505; -.
MaxQB; Q64505; -.
PaxDb; Q64505; -.
PRIDE; Q64505; -.
Ensembl; ENSMUST00000029905; ENSMUSP00000029905; ENSMUSG00000028240.
GeneID; 13122; -.
KEGG; mmu:13122; -.
UCSC; uc008rxk.1; mouse.
CTD; 1581; -.
MGI; MGI:106091; Cyp7a1.
eggNOG; KOG0684; Eukaryota.
eggNOG; COG2124; LUCA.
GeneTree; ENSGT00550000074551; -.
HOGENOM; HOG000231026; -.
HOVERGEN; HBG051100; -.
InParanoid; Q64505; -.
KO; K00489; -.
OMA; HGHVFTC; -.
OrthoDB; EOG091G07UI; -.
TreeFam; TF105090; -.
BRENDA; 1.14.13.17; 3474.
Reactome; R-MMU-192105; Synthesis of bile acids and bile salts.
Reactome; R-MMU-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
Reactome; R-MMU-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
Reactome; R-MMU-211976; Endogenous sterols.
UniPathway; UPA00221; -.
ChiTaRS; Cyp7a1; mouse.
PRO; PR:Q64505; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028240; Expressed in 29 organ(s), highest expression level in liver.
Genevisible; Q64505; MM.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
GO; GO:0008123; F:cholesterol 7-alpha-monooxygenase activity; IDA:MGI.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0006699; P:bile acid biosynthetic process; ISS:UniProtKB.
GO; GO:0071397; P:cellular response to cholesterol; ISS:UniProtKB.
GO; GO:0071333; P:cellular response to glucose stimulus; ISS:UniProtKB.
GO; GO:0006707; P:cholesterol catabolic process; IDA:MGI.
GO; GO:0042632; P:cholesterol homeostasis; ISS:UniProtKB.
GO; GO:0070859; P:positive regulation of bile acid biosynthetic process; TAS:BHF-UCL.
GO; GO:0070857; P:regulation of bile acid biosynthetic process; ISS:UniProtKB.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR030681; Cholesterol_7a_monooxygenase.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR024204; Cyt_P450_CYP7A1-type.
InterPro; IPR002403; Cyt_P450_E_grp-IV.
InterPro; IPR036396; Cyt_P450_sf.
PANTHER; PTHR24304:SF1; PTHR24304:SF1; 1.
Pfam; PF00067; p450; 1.
PIRSF; PIRSF500625; Cytochrome_CYP7A1; 1.
PIRSF; PIRSF000047; Cytochrome_CYPVIIA1; 1.
PRINTS; PR00465; EP450IV.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
2: Evidence at transcript level;
Cholesterol metabolism; Complete proteome; Endoplasmic reticulum;
Heme; Iron; Lipid metabolism; Membrane; Metal-binding; Microsome;
Monooxygenase; Oxidoreductase; Reference proteome; Steroid metabolism;
Sterol metabolism.
CHAIN 1 503 Cholesterol 7-alpha-monooxygenase.
/FTId=PRO_0000051902.
METAL 444 444 Iron (heme axial ligand). {ECO:0000250}.
CONFLICT 197 197 S -> T (in Ref. 1; AAA68867).
{ECO:0000305}.
CONFLICT 228 228 F -> L (in Ref. 1; AAA68867).
{ECO:0000305}.
CONFLICT 318 318 A -> S (in Ref. 1; AAA68867).
{ECO:0000305}.
SEQUENCE 503 AA; 57262 MW; F7F8BC2CDD2C43D1 CRC64;
MMSISLIWGI AVVVSCCIWF IIGIRRRKVG EPPLDNGLIP YLGCALKFGS NPLEFLRAKQ
RKHGHVFTCK LMGKYVHFIT NSLSYHKVLC HGKYFDWKKF HYTTSAKAFG HRSIDPSDGN
TTENINKTFN KTLQGDALCS LSEAMMQNLQ SVMRPPGLPK SKSAVWVTEG MYAFCYRVMF
EAGYLTLFGK DISKTDSQRA FIQNNLDSFK QFDQVFPALV AGVPIHLFKT AHKARERLAE
SLKHKNLYMR DQVSELIRLR MFLNDTLSTF DDMEKAKTHL VILWASQANT IPATFWSLFQ
MIRSPEAMKA ASEEVNGALQ SAGQELSSGG NAIYLDQEQL NNLPVLDSII KEALRLSSAS
LNIRTAKEDF TLHLEDGSYN IRKDDIIALY PQLMHLDPEI YPDPLTFKYD RYLDESGKAK
TTFYRNGNKL KYFYMPFGSG ATICPGRLFA VQEIKQFLIL MLSYFELELV ESHTKCPPLD
QSRAGLGILP PLNDIEFKYK LKH


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