CP7A1_HUMAN
ID CP7A1_HUMAN Reviewed; 504 AA.
AC P22680; P78454; Q3MIL8; Q7KZ19;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Cytochrome P450 7A1 {ECO:0000303|PubMed:21813643};
DE AltName: Full=24-hydroxycholesterol 7-alpha-hydroxylase {ECO:0000305|PubMed:11013305};
DE EC=1.14.14.26 {ECO:0000269|PubMed:11013305};
DE AltName: Full=CYPVII;
DE AltName: Full=Cholesterol 7-alpha-hydroxylase {ECO:0000303|PubMed:11013305};
DE AltName: Full=Cholesterol 7-alpha-monooxygenase;
DE EC=1.14.14.23 {ECO:0000269|PubMed:2384150};
GN Name=CYP7A1 {ECO:0000303|PubMed:12077124, ECO:0000312|HGNC:HGNC:2651};
GN Synonyms=CYP7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8439551; DOI=10.1016/0167-4781(93)90281-h;
RA Nishimoto M., Noshiro M., Okuda K.;
RT "Structure of the gene encoding human liver cholesterol 7 alpha-
RT hydroxylase.";
RL Biochim. Biophys. Acta 1172:147-150(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, VARIANT ASN-347, FUNCTION,
RP PATHWAY, AND SUBCELLULAR LOCATION.
RX PubMed=2384150; DOI=10.1016/0014-5793(90)80992-r;
RA Noshiro M., Okuda K.;
RT "Molecular cloning and sequence analysis of cDNA encoding human cholesterol
RT 7 alpha-hydroxylase.";
RL FEBS Lett. 268:137-140(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-100.
RX PubMed=1610352; DOI=10.1016/0006-291x(92)91665-d;
RA Karam W.G., Chiang J.Y.;
RT "Polymorphisms of human cholesterol 7 alpha-hydroxylase.";
RL Biochem. Biophys. Res. Commun. 185:588-595(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-140.
RC TISSUE=Placenta;
RX PubMed=8020987; DOI=10.1006/geno.1994.1177;
RA Wang D.P., Chiang J.Y.;
RT "Structure and nucleotide sequences of the human cholesterol 7 alpha-
RT hydroxylase gene (CYP7).";
RL Genomics 20:320-323(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
RX PubMed=1312351; DOI=10.1021/bi00124a014;
RA Molowa D.T., Chen W.S., Cimis G.M., Tan C.P.;
RT "Transcriptional regulation of the human cholesterol 7 alpha-hydroxylase
RT gene.";
RL Biochemistry 31:2539-2544(1992).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11013305;
RA Norlin M., Toll A., Bjoerkhem I., Wikvall K.;
RT "24-hydroxycholesterol is a substrate for hepatic cholesterol 7alpha-
RT hydroxylase (CYP7A).";
RL J. Lipid Res. 41:1629-1639(2000).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=12077124; DOI=10.1074/jbc.m201712200;
RA Bodin K., Andersson U., Rystedt E., Ellis E., Norlin M., Pikuleva I.,
RA Eggertsen G., Bjoerkhem I., Diczfalusy U.;
RT "Metabolism of 4 beta -hydroxycholesterol in humans.";
RL J. Biol. Chem. 277:31534-31540(2002).
RN [9]
RP INDUCTION BY CHENODEOXYCHOLIC ACID AND CHOLESTYRAMINE, AND TISSUE
RP SPECIFICITY.
RX PubMed=15796896; DOI=10.1016/j.bbrc.2005.02.170;
RA Abrahamsson A., Gustafsson U., Ellis E., Nilsson L.M., Sahlin S.,
RA Bjorkhem I., Einarsson C.;
RT "Feedback regulation of bile acid synthesis in human liver: importance of
RT HNF-4alpha for regulation of CYP7A1.";
RL Biochem. Biophys. Res. Commun. 330:395-399(2005).
RN [10]
RP INDUCTION BY GLUCOSE, AND FUNCTION.
RX PubMed=19965590; DOI=10.1194/jlr.m002782;
RA Li T., Chanda D., Zhang Y., Choi H.S., Chiang J.Y.;
RT "Glucose stimulates cholesterol 7alpha-hydroxylase gene transcription in
RT human hepatocytes.";
RL J. Lipid Res. 51:832-842(2010).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21813643; DOI=10.1074/jbc.m111.282434;
RA Shinkyo R., Xu L., Tallman K.A., Cheng Q., Porter N.A., Guengerich F.P.;
RT "Conversion of 7-dehydrocholesterol to 7-ketocholesterol is catalyzed by
RT human cytochrome P450 7A1 and occurs by direct oxidation without an epoxide
RT intermediate.";
RL J. Biol. Chem. 286:33021-33028(2011).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH HEME, AND COFACTOR.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human CYP7A1.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [13]
RP VARIANTS SER-233 AND ASN-347.
RX PubMed=12721789; DOI=10.1007/s10038-003-0021-7;
RA Saito S., Iida A., Sekine A., Kawauchi S., Higuchi S., Ogawa C.,
RA Nakamura Y.;
RT "Catalog of 680 variations among eight cytochrome p450 (CYP) genes, nine
RT esterase genes, and two other genes in the Japanese population.";
RL J. Hum. Genet. 48:249-270(2003).
CC -!- FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of
CC endogenous cholesterol and its oxygenated derivatives (oxysterols)
CC (PubMed:11013305, PubMed:12077124, PubMed:19965590, PubMed:2384150,
CC PubMed:21813643). Mechanistically, uses molecular oxygen inserting one
CC oxygen atom into a substrate, and reducing the second into a water
CC molecule, with two electrons provided by NADPH via cytochrome P450
CC reductase (CPR; NADPH-ferrihemoprotein reductase) (PubMed:2384150,
CC PubMed:11013305, PubMed:12077124, PubMed:19965590, PubMed:21813643).
CC Functions as a critical regulatory enzyme of bile acid biosynthesis and
CC cholesterol homeostasis. Catalyzes the hydroxylation of carbon hydrogen
CC bond at 7-alpha position of cholesterol, a rate-limiting step in
CC cholesterol catabolism and bile acid biosynthesis (PubMed:12077124,
CC PubMed:19965590, PubMed:2384150). 7-alpha hydroxylates several
CC oxysterols, including 4beta-hydroxycholesterol and 24-
CC hydroxycholesterol (PubMed:11013305, PubMed:12077124). Catalyzes the
CC oxidation of the 7,8 double bond of 7-dehydrocholesterol and
CC lathosterol with direct and predominant formation of the 7-keto
CC derivatives (PubMed:21813643). {ECO:0000269|PubMed:11013305,
CC ECO:0000269|PubMed:12077124, ECO:0000269|PubMed:19965590,
CC ECO:0000269|PubMed:21813643, ECO:0000269|PubMed:2384150}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol + O2 + reduced [NADPH--hemoprotein reductase] =
CC 7alpha-hydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:21812, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16113, ChEBI:CHEBI:17500, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; EC=1.14.14.23;
CC Evidence={ECO:0000269|PubMed:11013305, ECO:0000269|PubMed:12077124,
CC ECO:0000269|PubMed:2384150};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21813;
CC Evidence={ECO:0000305|PubMed:11013305, ECO:0000305|PubMed:12077124,
CC ECO:0000305|PubMed:2384150};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4beta-hydroxycholesterol + O2 + reduced [NADPH--hemoprotein
CC reductase] = 4beta,7alpha-dihydroxycholesterol + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46120,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:85778, ChEBI:CHEBI:85779;
CC Evidence={ECO:0000269|PubMed:12077124};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46121;
CC Evidence={ECO:0000305|PubMed:12077124};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=lathosterol + O2 + reduced [NADPH--hemoprotein reductase] =
CC 7alpha,8alpha-epoxy-5alpha-cholestan-3beta-ol + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53256, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17168,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:137063;
CC Evidence={ECO:0000269|PubMed:21813643};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53257;
CC Evidence={ECO:0000305|PubMed:21813643};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=lathosterol + O2 + reduced [NADPH--hemoprotein reductase] =
CC 5alpha-cholestan-7-oxo-3beta-ol + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:53252, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17168, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:137062;
CC Evidence={ECO:0000269|PubMed:21813643};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53253;
CC Evidence={ECO:0000305|PubMed:21813643};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-dehydrocholesterol + O2 + reduced [NADPH--hemoprotein
CC reductase] = 7-oxocholesterol + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:53248, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17759, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:64294;
CC Evidence={ECO:0000269|PubMed:21813643};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53249;
CC Evidence={ECO:0000305|PubMed:21813643};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(24S)-hydroxycholesterol + O2 + reduced [NADPH--hemoprotein
CC reductase] = (24S)-7alpha-dihydroxycholesterol + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46124,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:34310,
CC ChEBI:CHEBI:37640, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC EC=1.14.14.26; Evidence={ECO:0000269|PubMed:11013305};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46125;
CC Evidence={ECO:0000305|PubMed:11013305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(24R)-hydroxycholesterol + O2 + reduced [NADPH--hemoprotein
CC reductase] = (24R)-7alpha-dihydroxycholesterol + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:16093,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:50516,
CC ChEBI:CHEBI:50518, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:11013305};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16094;
CC Evidence={ECO:0000305|PubMed:11013305};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|Ref.12};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3 uM for cholesterol {ECO:0000269|PubMed:11013305};
CC KM=6 uM for 24-hydroxycholesterol {ECO:0000269|PubMed:11013305};
CC KM=1.8 uM for 5alpha-cholest-7-en-3beta-ol (lathosterol)
CC {ECO:0000269|PubMed:21813643};
CC KM=1.1 uM for cholesta-5,7-dien-3beta-ol (7-dehydrocholesterol)
CC {ECO:0000269|PubMed:21813643};
CC Vmax=0.184 nmol/min/nmol enzyme toward cholesterol
CC {ECO:0000269|PubMed:12077124};
CC Vmax=0.087 nmol/min/nmol enzyme toward 4beta-hydroxycholesterol
CC {ECO:0000269|PubMed:12077124};
CC Note=kcat is 3.7 min(-1) with 5alpha-cholest-7-en-3beta-ol
CC (lathosterol) as substrate. kcat is 2.2 min(-1) with cholesta-5,7-
CC dien-3beta-ol (7-dehydrocholesterol) as substrate.
CC {ECO:0000269|PubMed:21813643};
CC -!- PATHWAY: Lipid metabolism; bile acid biosynthesis.
CC {ECO:0000305|PubMed:11013305, ECO:0000305|PubMed:12077124,
CC ECO:0000305|PubMed:2384150}.
CC -!- PATHWAY: Steroid metabolism; cholesterol degradation.
CC {ECO:0000305|PubMed:11013305, ECO:0000305|PubMed:12077124,
CC ECO:0000305|PubMed:2384150}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:11013305, ECO:0000305|PubMed:2384150}; Single-pass
CC membrane protein {ECO:0000305}. Microsome membrane
CC {ECO:0000305|PubMed:11013305, ECO:0000305|PubMed:2384150}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in liver. {ECO:0000269|PubMed:15796896}.
CC -!- INDUCTION: Up-regulated by glucose and by cholestyramine. Down-
CC regulated by chenodeoxycholic acid. {ECO:0000269|PubMed:15796896,
CC ECO:0000269|PubMed:19965590}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Cholesterol-7 alpha-hydroxylase
CC entry;
CC URL="https://en.wikipedia.org/wiki/Cholesterol_7_alpha-hydroxylase";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CYP7A1ID40254ch8q12.html";
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DR EMBL; X56088; CAA39568.1; -; mRNA.
DR EMBL; M93133; AAA58435.1; -; mRNA.
DR EMBL; BC101777; AAI01778.1; -; mRNA.
DR EMBL; BC112184; AAI12185.1; -; mRNA.
DR EMBL; L13460; AAA61350.1; -; Genomic_DNA.
DR EMBL; M89647; AAA58423.1; -; Genomic_DNA.
DR CCDS; CCDS6171.1; -.
DR PIR; S29818; JH0659.
DR RefSeq; NP_000771.2; NM_000780.3.
DR PDB; 3DAX; X-ray; 2.15 A; A/B=25-503.
DR PDB; 3SN5; X-ray; 2.75 A; A/B=25-503.
DR PDB; 3V8D; X-ray; 1.90 A; A/B=25-503.
DR PDBsum; 3DAX; -.
DR PDBsum; 3SN5; -.
DR PDBsum; 3V8D; -.
DR AlphaFoldDB; P22680; -.
DR SMR; P22680; -.
DR STRING; 9606.ENSP00000301645; -.
DR ChEMBL; CHEMBL1851; -.
DR GuidetoPHARMACOLOGY; 1354; -.
DR SwissLipids; SLP:000001200; -.
DR iPTMnet; P22680; -.
DR PhosphoSitePlus; P22680; -.
DR BioMuta; CYP7A1; -.
DR DMDM; 544084; -.
DR EPD; P22680; -.
DR jPOST; P22680; -.
DR MassIVE; P22680; -.
DR PaxDb; P22680; -.
DR PeptideAtlas; P22680; -.
DR PRIDE; P22680; -.
DR ProteomicsDB; 54016; -.
DR Antibodypedia; 2602; 160 antibodies from 30 providers.
DR DNASU; 1581; -.
DR Ensembl; ENST00000301645.4; ENSP00000301645.3; ENSG00000167910.4.
DR GeneID; 1581; -.
DR KEGG; hsa:1581; -.
DR MANE-Select; ENST00000301645.4; ENSP00000301645.3; NM_000780.4; NP_000771.2.
DR UCSC; uc003xtm.5; human.
DR CTD; 1581; -.
DR DisGeNET; 1581; -.
DR GeneCards; CYP7A1; -.
DR HGNC; HGNC:2651; CYP7A1.
DR HPA; ENSG00000167910; Tissue enriched (liver).
DR MalaCards; CYP7A1; -.
DR MIM; 118455; gene.
DR neXtProt; NX_P22680; -.
DR OpenTargets; ENSG00000167910; -.
DR Orphanet; 209902; Hypercholesterolemia due to cholesterol 7alpha-hydroxylase deficiency.
DR PharmGKB; PA132; -.
DR VEuPathDB; HostDB:ENSG00000167910; -.
DR eggNOG; KOG0684; Eukaryota.
DR GeneTree; ENSGT00940000153141; -.
DR HOGENOM; CLU_018012_1_3_1; -.
DR InParanoid; P22680; -.
DR OMA; VCCCLWL; -.
DR OrthoDB; 864748at2759; -.
DR PhylomeDB; P22680; -.
DR TreeFam; TF105090; -.
DR BioCyc; MetaCyc:HS09659-MON; -.
DR BRENDA; 1.14.14.23; 2681.
DR PathwayCommons; P22680; -.
DR Reactome; R-HSA-192105; Synthesis of bile acids and bile salts.
DR Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-HSA-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-211976; Endogenous sterols.
DR SABIO-RK; P22680; -.
DR SignaLink; P22680; -.
DR SIGNOR; P22680; -.
DR UniPathway; UPA00221; -.
DR UniPathway; UPA01058; -.
DR BioGRID-ORCS; 1581; 11 hits in 1065 CRISPR screens.
DR EvolutionaryTrace; P22680; -.
DR GeneWiki; Cholesterol_7_alpha-hydroxylase; -.
DR GenomeRNAi; 1581; -.
DR Pharos; P22680; Tchem.
DR PRO; PR:P22680; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P22680; protein.
DR Bgee; ENSG00000167910; Expressed in right lobe of liver and 23 other tissues.
DR Genevisible; P22680; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR GO; GO:0033782; F:24-hydroxycholesterol 7alpha-hydroxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008123; F:cholesterol 7-alpha-monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
DR GO; GO:0015721; P:bile acid and bile salt transport; IEA:Ensembl.
DR GO; GO:0006699; P:bile acid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0038183; P:bile acid signaling pathway; IEA:Ensembl.
DR GO; GO:0071397; P:cellular response to cholesterol; ISS:UniProtKB.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IDA:UniProtKB.
DR GO; GO:0006707; P:cholesterol catabolic process; ISS:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; ISS:UniProtKB.
DR GO; GO:0032966; P:negative regulation of collagen biosynthetic process; IEA:Ensembl.
DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IEA:Ensembl.
DR GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; IEA:Ensembl.
DR GO; GO:0070857; P:regulation of bile acid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0016125; P:sterol metabolic process; TAS:Reactome.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR030681; Cholesterol_7a_monooxygenase.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR024204; Cyt_P450_CYP7A1-type.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24304:SF1; PTHR24304:SF1; 1.
DR Pfam; PF00067; p450; 1.
DR PIRSF; PIRSF500625; Cytochrome_CYP7A1; 1.
DR PIRSF; PIRSF000047; Cytochrome_CYPVIIA1; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cholesterol metabolism; Endoplasmic reticulum; Heme; Iron;
KW Lipid metabolism; Membrane; Metal-binding; Microsome; Monooxygenase;
KW Oxidoreductase; Reference proteome; Steroid metabolism; Sterol metabolism;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..504
FT /note="Cytochrome P450 7A1"
FT /id="PRO_0000051901"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 444
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0007744|PDB:3DAX"
FT VARIANT 86
FT /note="H -> N (in dbSNP:rs62621283)"
FT /id="VAR_059152"
FT VARIANT 100
FT /note="F -> S"
FT /evidence="ECO:0000269|PubMed:1610352"
FT /id="VAR_001259"
FT VARIANT 233
FT /note="N -> S (in dbSNP:rs8192874)"
FT /evidence="ECO:0000269|PubMed:12721789"
FT /id="VAR_018376"
FT VARIANT 347
FT /note="D -> N (in dbSNP:rs8192875)"
FT /evidence="ECO:0000269|PubMed:12721789,
FT ECO:0000269|PubMed:2384150"
FT /id="VAR_018377"
FT CONFLICT 385
FT /note="D -> S (in Ref. 2; CAA39568)"
FT /evidence="ECO:0000305"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:3V8D"
FT TURN 42..45
FT /evidence="ECO:0007829|PDB:3V8D"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:3V8D"
FT HELIX 52..63
FT /evidence="ECO:0007829|PDB:3V8D"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:3V8D"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:3V8D"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:3V8D"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:3V8D"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:3V8D"
FT HELIX 99..109
FT /evidence="ECO:0007829|PDB:3V8D"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:3V8D"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:3V8D"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:3V8D"
FT HELIX 135..153
FT /evidence="ECO:0007829|PDB:3V8D"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:3V8D"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:3V8D"
FT HELIX 171..188
FT /evidence="ECO:0007829|PDB:3V8D"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:3V8D"
FT HELIX 198..220
FT /evidence="ECO:0007829|PDB:3V8D"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:3V8D"
FT HELIX 229..241
FT /evidence="ECO:0007829|PDB:3V8D"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:3V8D"
FT HELIX 255..267
FT /evidence="ECO:0007829|PDB:3V8D"
FT HELIX 272..287
FT /evidence="ECO:0007829|PDB:3V8D"
FT HELIX 290..303
FT /evidence="ECO:0007829|PDB:3V8D"
FT HELIX 305..321
FT /evidence="ECO:0007829|PDB:3V8D"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:3V8D"
FT HELIX 337..341
FT /evidence="ECO:0007829|PDB:3V8D"
FT HELIX 344..357
FT /evidence="ECO:0007829|PDB:3V8D"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:3V8D"
FT STRAND 362..373
FT /evidence="ECO:0007829|PDB:3V8D"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:3V8D"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:3V8D"
FT HELIX 392..395
FT /evidence="ECO:0007829|PDB:3V8D"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:3V8D"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:3V8D"
FT TURN 409..412
FT /evidence="ECO:0007829|PDB:3V8D"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:3V8D"
FT HELIX 447..464
FT /evidence="ECO:0007829|PDB:3V8D"
FT STRAND 465..469
FT /evidence="ECO:0007829|PDB:3V8D"
FT TURN 470..473
FT /evidence="ECO:0007829|PDB:3DAX"
FT HELIX 481..483
FT /evidence="ECO:0007829|PDB:3V8D"
FT STRAND 485..488
FT /evidence="ECO:0007829|PDB:3V8D"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:3V8D"
FT STRAND 496..501
FT /evidence="ECO:0007829|PDB:3V8D"
SQ SEQUENCE 504 AA; 57661 MW; D8067E0FF6342949 CRC64;
MMTTSLIWGI AIAACCCLWL ILGIRRRQTG EPPLENGLIP YLGCALQFGA NPLEFLRANQ
RKHGHVFTCK LMGKYVHFIT NPLSYHKVLC HGKYFDWKKF HFATSAKAFG HRSIDPMDGN
TTENINDTFI KTLQGHALNS LTESMMENLQ RIMRPPVSSN SKTAAWVTEG MYSFCYRVMF
EAGYLTIFGR DLTRRDTQKA HILNNLDNFK QFDKVFPALV AGLPIHMFRT AHNAREKLAE
SLRHENLQKR ESISELISLR MFLNDTLSTF DDLEKAKTHL VVLWASQANT IPATFWSLFQ
MIRNPEAMKA ATEEVKRTLE NAGQKVSLEG NPICLSQAEL NDLPVLDSII KESLRLSSAS
LNIRTAKEDF TLHLEDGSYN IRKDDIIALY PQLMHLDPEI YPDPLTFKYD RYLDENGKTK
TTFYCNGLKL KYYYMPFGSG ATICPGRLFA IHEIKQFLIL MLSYFELELI EGQAKCPPLD
QSRAGLGILP PLNDIEFKYK FKHL
