CP7B1_MOUSE
ID CP7B1_MOUSE Reviewed; 507 AA.
AC Q60991; Q9CZ39;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Cytochrome P450 7B1;
DE AltName: Full=24-hydroxycholesterol 7-alpha-hydroxylase {ECO:0000305|PubMed:11067870};
DE EC=1.14.14.26 {ECO:0000269|PubMed:11067870};
DE AltName: Full=25/26-hydroxycholesterol 7-alpha-hydroxylase {ECO:0000305|PubMed:9295351};
DE EC=1.14.14.29 {ECO:0000269|PubMed:9295351};
DE AltName: Full=3-hydroxysteroid 7-alpha hydroxylase;
DE AltName: Full=Hippocampal transcript 1 protein {ECO:0000303|PubMed:8530364};
DE Short=HCT-1 {ECO:0000303|PubMed:8530364};
DE AltName: Full=Oxysterol 7-alpha-hydroxylase {ECO:0000303|PubMed:9295351};
GN Name=Cyp7b1 {ECO:0000303|PubMed:10748047, ECO:0000312|MGI:MGI:104978};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain, and Liver;
RX PubMed=8530364; DOI=10.1074/jbc.270.50.29739;
RA Stapleton G., Steel M., Richardson M., Mason J.O., Rose K.A., Morris R.G.,
RA Lathe R.;
RT "A novel cytochrome P450 expressed primarily in brain.";
RL J. Biol. Chem. 270:29739-29745(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=9295351; DOI=10.1074/jbc.272.38.23995;
RA Schwarz M., Lund E.G., Lathe R., Bjoerkhem I., Russell D.W.;
RT "Identification and characterization of a mouse oxysterol 7alpha-
RT hydroxylase cDNA.";
RL J. Biol. Chem. 272:23995-24001(1997).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=9144166; DOI=10.1073/pnas.94.10.4925;
RA Rose K.A., Stapleton G., Dott K., Kieny M.P., Best R., Schwarz M.,
RA Russell D.W., Bjoerkhem I., Seckl J., Lathe R.;
RT "Cyp7b, a novel brain cytochrome P450, catalyzes the synthesis of
RT neurosteroids 7alpha-hydroxy dehydroepiandrosterone and 7alpha-hydroxy
RT pregnenolone.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:4925-4930(1997).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=10748047; DOI=10.1074/jbc.m001810200;
RA Li-Hawkins J., Lund E.G., Bronson A.D., Russell D.W.;
RT "Expression cloning of an oxysterol 7alpha-hydroxylase selective for 24-
RT hydroxycholesterol.";
RL J. Biol. Chem. 275:16543-16549(2000).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=11067870; DOI=10.1172/jci10902;
RA Schwarz M., Wright A.C., Davis D.L., Nazer H., Bjorkhem I., Russell D.W.;
RT "The bile acid synthetic gene 3beta-hydroxy-delta(5)-C(27)-steroid
RT oxidoreductase is mutated in progressive intrahepatic cholestasis.";
RL J. Clin. Invest. 106:1175-1184(2000).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22999953; DOI=10.1016/j.immuni.2012.06.015;
RA Yi T., Wang X., Kelly L.M., An J., Xu Y., Sailer A.W., Gustafsson J.A.,
RA Russell D.W., Cyster J.G.;
RT "Oxysterol gradient generation by lymphoid stromal cells guides activated B
RT cell movement during humoral responses.";
RL Immunity 37:535-548(2012).
CC -!- FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of
CC endogenous oxysterols and steroid hormones, including neurosteroids
CC (PubMed:9295351, PubMed:9144166, PubMed:10748047, PubMed:11067870).
CC Mechanistically, uses molecular oxygen inserting one oxygen atom into a
CC substrate, and reducing the second into a water molecule, with two
CC electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-
CC ferrihemoprotein reductase). Catalyzes the hydroxylation of carbon
CC hydrogen bonds of steroids with a preference for 7-alpha position.
CC Usually metabolizes steroids carrying a hydroxy group at position 3,
CC functioning as a 3-hydroxy steroid 7-alpha hydroxylase (PubMed:9295351,
CC PubMed:9144166, PubMed:10748047, PubMed:11067870). Hydroxylates
CC oxysterols, including 25-hydroxycholesterol and (25R)-cholest-5-ene-
CC 3beta,26-diol toward 7-alpha hydroxy derivatives, which may be
CC transported to the liver and converted to bile acids (PubMed:9295351,
CC PubMed:9144166, PubMed:10748047, PubMed:11067870). Via its product 7-
CC alpha,25-dihydroxycholesterol, a ligand for the chemotactic G protein-
CC coupled receptor GPR183/EBI2, regulates B cell migration in germinal
CC centers of lymphoid organs, thus guiding efficient maturation of plasma
CC B cells and overall antigen-specific humoral immune response
CC (PubMed:22999953). 7-alpha hydroxylates neurosteroids, including 3beta-
CC hydroxyandrost-5-en-17-one (dehydroepiandrosterone) and pregnenolone,
CC both involved in hippocampus-associated memory and learning
CC (PubMed:9144166). Metabolizes androstanoids toward 6- or 7-alpha
CC hydroxy derivatives (By similarity). {ECO:0000250|UniProtKB:O75881,
CC ECO:0000269|PubMed:10748047, ECO:0000269|PubMed:11067870,
CC ECO:0000269|PubMed:22999953, ECO:0000269|PubMed:9144166,
CC ECO:0000269|PubMed:9295351}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=25-hydroxycholesterol + O2 + reduced [NADPH--hemoprotein
CC reductase] = 7alpha,25-dihydroxycholesterol + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:24308, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:37623,
CC ChEBI:CHEBI:42977, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC EC=1.14.14.29; Evidence={ECO:0000269|PubMed:10748047,
CC ECO:0000269|PubMed:11067870, ECO:0000269|PubMed:9144166,
CC ECO:0000269|PubMed:9295351};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24309;
CC Evidence={ECO:0000305|PubMed:9295351};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(25R)-cholest-5-ene-3beta,26-diol + O2 + reduced [NADPH--
CC hemoprotein reductase] = (25R)-cholest-5-en-3beta,7alpha,26-triol +
CC H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:19041, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76591,
CC ChEBI:CHEBI:76592; EC=1.14.14.29;
CC Evidence={ECO:0000269|PubMed:10748047, ECO:0000269|PubMed:11067870,
CC ECO:0000269|PubMed:9295351};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19042;
CC Evidence={ECO:0000305|PubMed:9295351};
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:11067870};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46125;
CC Evidence={ECO:0000305|PubMed:11067870};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(24S)-25-epoxycholesterol + O2 + reduced [NADPH--hemoprotein
CC reductase] = (24S,25)-epoxy-7alpha-hydroxycholesterol + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46464,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:41633,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:86146;
CC Evidence={ECO:0000269|PubMed:10748047};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46465;
CC Evidence={ECO:0000305|PubMed:10748047};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(22R)-hydroxycholesterol + O2 + reduced [NADPH--hemoprotein
CC reductase] = (22R,7alpha)-dihydroxycholesterol + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46460,
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:67237, ChEBI:CHEBI:86145;
CC Evidence={ECO:0000269|PubMed:10748047};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46461;
CC Evidence={ECO:0000305|PubMed:10748047};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=androst-5-en-3beta,17beta-diol + O2 + reduced [NADPH--
CC hemoprotein reductase] = androst-5-en-3beta,7alpha,17beta-triol +
CC H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:46204, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:2710, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:85810; Evidence={ECO:0000250|UniProtKB:O75881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46205;
CC Evidence={ECO:0000250|UniProtKB:O75881};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5alpha-androstane-3beta,17beta-diol + O2 + reduced [NADPH--
CC hemoprotein reductase] = 5alpha-androstane-3beta,6alpha,17beta-triol
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:46200, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:18329, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:85809; Evidence={ECO:0000250|UniProtKB:O75881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46201;
CC Evidence={ECO:0000250|UniProtKB:O75881};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3beta-hydroxyandrost-5-en-17-one + O2 + reduced [NADPH--
CC hemoprotein reductase] = 3beta,7alpha-dihydroxyandrost-5-en-17-one +
CC H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:46192, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:28689, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:81471; Evidence={ECO:0000269|PubMed:9144166};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46193;
CC Evidence={ECO:0000305|PubMed:9144166};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3beta-hydroxy-5alpha-androstan-17-one + O2 + reduced [NADPH--
CC hemoprotein reductase] = 3beta,7alpha-dihydroxy-5alpha-androstan-17-
CC one + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:43896, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:85816,
CC ChEBI:CHEBI:541975; Evidence={ECO:0000250|UniProtKB:O75881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43897;
CC Evidence={ECO:0000250|UniProtKB:O75881};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + pregnenolone + reduced [NADPH--hemoprotein reductase] =
CC 7alpha-hydroxypregnenolone + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:46196, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16581, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:81467;
CC Evidence={ECO:0000269|PubMed:9144166};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46197;
CC Evidence={ECO:0000305|PubMed:9144166};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P22680};
CC -!- ACTIVITY REGULATION: Inhibited by drugs voriconazole and metyrapone.
CC {ECO:0000250|UniProtKB:O75881}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13.6 uM for 3beta-hydroxyandrost-5-en-17-one
CC (dehydroepiandrosterone) {ECO:0000269|PubMed:9144166};
CC KM=4 uM for pregnenolone {ECO:0000269|PubMed:9144166};
CC -!- PATHWAY: Lipid metabolism; bile acid biosynthesis.
CC {ECO:0000269|PubMed:10748047, ECO:0000269|PubMed:11067870,
CC ECO:0000269|PubMed:9144166, ECO:0000269|PubMed:9295351}.
CC -!- PATHWAY: Steroid hormone biosynthesis. {ECO:0000269|PubMed:9144166}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O75881}; Multi-pass membrane protein
CC {ECO:0000305}. Microsome membrane {ECO:0000250|UniProtKB:O75881};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain structures including the
CC corpus callosum, the anterior commissure and fornix (PubMed:8530364).
CC The hippocampal expression is particularly prominent in the dentate
CC gyrus (PubMed:8530364). Expressed in liver and kidney. The hepatic
CC expression is sexually dimorphic, predominantly detected in male liver
CC while barely detectable in females (PubMed:8530364). Expressed in lymph
CC nodes and spleens, in both lymphoid and stromal compartments
CC (PubMed:22999953). Higher expression is detected in fibroblastic
CC reticular cells, a type of stromal cells in the lymph nodes
CC (PubMed:22999953). Also expressed at high levels in the outer follicle
CC and at the B cell-T cell boundary of splenic germinal centers
CC (PubMed:22999953). Expressed in dendritic cells (DCs) subpopulations
CC being most abundant in CD8-positive DCs (PubMed:22999953).
CC {ECO:0000269|PubMed:22999953, ECO:0000269|PubMed:8530364}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice exhibit impaired generation of
CC plasma cells and overall deficient antigen-specific humoral immune
CC response. {ECO:0000269|PubMed:22999953}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; U36993; AAA92615.1; -; mRNA.
DR EMBL; AK013034; BAB28613.1; -; mRNA.
DR CCDS; CCDS17254.1; -.
DR RefSeq; NP_031851.3; NM_007825.4.
DR RefSeq; XP_006535446.1; XM_006535383.3.
DR AlphaFoldDB; Q60991; -.
DR SMR; Q60991; -.
DR BioGRID; 199039; 1.
DR STRING; 10090.ENSMUSP00000037487; -.
DR SwissLipids; SLP:000001208; -.
DR iPTMnet; Q60991; -.
DR PhosphoSitePlus; Q60991; -.
DR SwissPalm; Q60991; -.
DR jPOST; Q60991; -.
DR MaxQB; Q60991; -.
DR PaxDb; Q60991; -.
DR PeptideAtlas; Q60991; -.
DR PRIDE; Q60991; -.
DR ProteomicsDB; 283934; -.
DR Antibodypedia; 3058; 302 antibodies from 35 providers.
DR DNASU; 13123; -.
DR Ensembl; ENSMUST00000035625; ENSMUSP00000037487; ENSMUSG00000039519.
DR GeneID; 13123; -.
DR KEGG; mmu:13123; -.
DR UCSC; uc008orm.2; mouse.
DR CTD; 9420; -.
DR MGI; MGI:104978; Cyp7b1.
DR VEuPathDB; HostDB:ENSMUSG00000039519; -.
DR eggNOG; KOG0684; Eukaryota.
DR GeneTree; ENSGT00940000153141; -.
DR HOGENOM; CLU_018012_1_2_1; -.
DR InParanoid; Q60991; -.
DR OMA; FIMDPFQ; -.
DR OrthoDB; 614788at2759; -.
DR PhylomeDB; Q60991; -.
DR TreeFam; TF105090; -.
DR BRENDA; 1.14.14.29; 3474.
DR Reactome; R-MMU-192105; Synthesis of bile acids and bile salts.
DR Reactome; R-MMU-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-MMU-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
DR Reactome; R-MMU-211976; Endogenous sterols.
DR UniPathway; UPA00221; -.
DR BioGRID-ORCS; 13123; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Cyp7b1; mouse.
DR PRO; PR:Q60991; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q60991; protein.
DR Bgee; ENSMUSG00000039519; Expressed in left lobe of liver and 244 other tissues.
DR Genevisible; Q60991; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; TAS:UniProtKB.
DR GO; GO:0033782; F:24-hydroxycholesterol 7alpha-hydroxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0033783; F:25-hydroxycholesterol 7alpha-hydroxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0047092; F:27-hydroxycholesterol 7-alpha-monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0008396; F:oxysterol 7-alpha-hydroxylase activity; IDA:UniProtKB.
DR GO; GO:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
DR GO; GO:0035754; P:B cell chemotaxis; IMP:UniProtKB.
DR GO; GO:0006699; P:bile acid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; IBA:GO_Central.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007623; P:circadian rhythm; ISO:MGI.
DR GO; GO:0007586; P:digestion; TAS:UniProtKB.
DR GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IMP:MGI.
DR GO; GO:0007613; P:memory; ISO:MGI.
DR GO; GO:0033147; P:negative regulation of intracellular estrogen receptor signaling pathway; IMP:MGI.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:0060740; P:prostate gland epithelium morphogenesis; IMP:MGI.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR024204; Cyt_P450_CYP7A1-type.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PIRSF; PIRSF000047; Cytochrome_CYPVIIA1; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 1: Evidence at protein level;
KW Cholesterol metabolism; Endoplasmic reticulum; Heme; Iron;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding; Microsome;
KW Monooxygenase; Oxidoreductase; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..507
FT /note="Cytochrome P450 7B1"
FT /id="PRO_0000051907"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 447
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:0000250|UniProtKB:P22680"
FT CONFLICT 265
FT /note="R -> S (in Ref. 1; AAA92615)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="P -> S (in Ref. 1; AAA92615)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="K -> R (in Ref. 1; AAA92615)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="M -> E (in Ref. 1; AAA92615)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 507 AA; 58470 MW; 628A0D3270C04DA4 CRC64;
MQGATTLDAA SPGPLALLGL LFAATLLLSA LFLLTRRTRR PREPPLIKGW LPYLGMALKF
FKDPLTFLKT LQRQHGDTFT VFLVGKYITF VLNPFQYQYV TKNPKQLSFQ KFSSRLSAKA
FSVKKLLTDD DLNEDVHRAY LLLQGKPLDA LLETMIQEVK ELFESQLLKI TDWNTERIFA
FCGSLVFEIT FATLYGKILA GNKKQIISEL RDDFFKFDDM FPYLVSDIPI QLLRNEESMQ
KKIIKCLTSE KVAQMQGQSK IVQERQDLLK RYYRHDDPEI GAHHLGFLWA SLANTIPAMF
WAMYYILRHP EAMEALRDEI DSFLQSTGQK KGPGISVHFT REQLDSLVCL ESTILEVLRL
CSYSSIIREV QEDMNLSLES KSFSLRKGDF VALFPPLIHN DPEIFDAPKE FRFDRFIEDG
KKKSTFFKGG KKLKTYVMPF GLGTSKCPGR YFAVNEMKLL LIMLLTYFDL EIIDRKPIGL
NHSRMFLGIQ HPDSAVSFRY KAKSWRS
