ID   CP7A1_CRIGR             Reviewed;         504 AA.
AC   P46634;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Cholesterol 7-alpha-monooxygenase;
DE            EC=1.14.14.23 {ECO:0000250|UniProtKB:P22680};
DE   AltName: Full=CYPVII;
DE   AltName: Full=Cholesterol 7-alpha-hydroxylase;
DE   AltName: Full=Cytochrome P450 7A1;
GN   Name=CYP7A1; Synonyms=CYP7;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=8105753; DOI=10.1006/abbi.1993.1537;
RA   Crestani M., Galli G., Chiang J.Y.;
RT   "Genomic cloning, sequencing, and analysis of the hamster cholesterol 7
RT   alpha-hydroxylase gene (CYP7).";
RL   Arch. Biochem. Biophys. 306:451-460(1993).
CC   -!- FUNCTION: Catalyzes a rate-limiting step in cholesterol catabolism and
CC       bile acid biosynthesis by introducing a hydrophilic moiety at position
CC       7 of cholesterol. Important for cholesterol homeostasis.
CC       {ECO:0000250|UniProtKB:P22680}.
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:0000250|UniProtKB:P22680};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- PATHWAY: Lipid metabolism; bile acid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein. Microsome membrane; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L04690; AAA03751.1; -; Genomic_DNA.
DR   PIR; S39399; S39399.
DR   RefSeq; NP_001231330.1; NM_001244401.1.
DR   AlphaFoldDB; P46634; -.
DR   SMR; P46634; -.
DR   STRING; 10029.XP_007632636.1; -.
DR   GeneID; 100689275; -.
DR   KEGG; cge:100689275; -.
DR   CTD; 1581; -.
DR   eggNOG; KOG0684; Eukaryota.
DR   OrthoDB; 864748at2759; -.
DR   UniPathway; UPA00221; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR   GO; GO:0008123; F:cholesterol 7-alpha-monooxygenase activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0006699; P:bile acid biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0071397; P:cellular response to cholesterol; ISS:UniProtKB.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; ISS:UniProtKB.
DR   GO; GO:0006707; P:cholesterol catabolic process; ISS:UniProtKB.
DR   GO; GO:0042632; P:cholesterol homeostasis; ISS:UniProtKB.
DR   GO; GO:0070857; P:regulation of bile acid biosynthetic process; ISS:UniProtKB.
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   3: Inferred from homology;
KW   Cholesterol metabolism; Endoplasmic reticulum; Heme; Iron;
KW   Lipid metabolism; Membrane; Metal-binding; Microsome; Monooxygenase;
KW   Oxidoreductase; Steroid metabolism; Sterol metabolism.
FT   CHAIN           1..504
FT                   /note="Cholesterol 7-alpha-monooxygenase"
FT                   /id="PRO_0000051900"
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:0000250"
SQ   SEQUENCE   504 AA;  57447 MW;  BD5E521D0C195257 CRC64;
     MMTISLIWGI AMVVCCCIWV IFDRRRRKAG EPPLENGLIP YLGCALKFGS NPLEFLRANQ
     RKHGHVFTCK LMGKYVHFIT NSLSYHKVLC HGKYFDWKKF HYTTSAKAFG HRSIDPNDGN
     TTENINNTFT KTLQGDALHS LSEAMMQNLQ FVLRPPDLPK SKSDAWVTEG MYAFCYRVMF
     EAGYLTLFGR DTSKPDTQRV LILNNLNSFK QFDQVFPALV AGLPIHLFKA AHKAREQLAE
     GLKHENLSVR DQVSELIRLR MFLNDTLSTF DDMEKAKTHL AILWASQANT IPATFWSLFQ
     MIRSPDALRA ASEEVNGALQ SAGQKLSSEG NAIYLDQIQL NNLPVLDSII KEALRLSSAS
     LNIRTAKEDF TLHLEDGSYN IRKDDIIALY PQLMHLDPAI YPDPLTFKYD RYLDENKKAK
     TSFYSNGNKL KYFYMPFGSG ATICPGRLFA VQEIKQFLIL MLSYFELELV ESHVKCPPLD
     QSRAGLGILP PLNDIEFKYK LKHL