ID Q5ILH2_CHICK Unreviewed; 513 AA.
AC Q5ILH2;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 24-JAN-2024, entry version 125.
DE RecName: Full=Cholesterol 7-alpha-monooxygenase {ECO:0000256|PIRNR:PIRNR000047};
DE EC=1.14.14.23 {ECO:0000256|PIRNR:PIRNR000047};
GN Name=CYP7A1 {ECO:0000313|EMBL:AAW33560.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000313|EMBL:AAW33560.1};
RN [1] {ECO:0000313|EMBL:AAW33560.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15629111; DOI=10.1016/j.abb.2004.10.010;
RA Handschin C., Gnerre C., Fraser D.J., Martinez-Jimenez C., Jover R.,
RA Meyer U.A.;
RT "Species-specific mechanisms for cholesterol 7alpha-hydroxylase (CYP7A1)
RT regulation by drugs and bile acids.";
RL Arch. Biochem. Biophys. 434:75-85(2005).
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:0000256|PIRNR:PIRNR000047};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRNR:PIRNR000047, ECO:0000256|PIRSR:PIRSR000047-1};
CC -!- PATHWAY: Lipid metabolism; bile acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004860, ECO:0000256|PIRNR:PIRNR000047}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|PIRNR:PIRNR000047}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|PIRNR:PIRNR000047}.
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DR EMBL; AY700578; AAW33560.1; -; mRNA.
DR AlphaFoldDB; Q5ILH2; -.
DR VEuPathDB; HostDB:geneid_414834; -.
DR PhylomeDB; Q5ILH2; -.
DR BRENDA; 1.14.14.23; 1306.
DR UniPathway; UPA00221; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008123; F:cholesterol 7-alpha-monooxygenase activity; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniPathway.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:InterPro.
DR GO; GO:0006707; P:cholesterol catabolic process; IEA:InterPro.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:InterPro.
DR CDD; cd20631; CYP7A1; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR030681; Cholesterol_7a_monooxygenase.
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 PANTHER; PTHR24304:SF1; CYTOCHROME P450 7A1; 1.
DR PANTHER; PTHR24304; CYTOCHROME P450 FAMILY 7; 1.
DR Pfam; PF00067; p450; 1.
DR PIRSF; PIRSF500625; Cytochrome_CYP7A1; 1.
DR PIRSF; PIRSF000047; Cytochrome_CYPVIIA1; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 2: Evidence at transcript level;
KW Cholesterol metabolism {ECO:0000256|PIRNR:PIRNR000047};
KW Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR000047};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR000047};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR000047};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000047};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000047};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Steroid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW Sterol metabolism {ECO:0000256|PIRNR:PIRNR000047};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..22
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000047-2"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000047-2"
FT BINDING 453
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:0000256|PIRSR:PIRSR000047-1"
SQ SEQUENCE 513 AA; 59346 MW; 0705B9A7E68AF6AE CRC64;
MITTSWIWGT VIIVCCSFWF LFGRRRRRRQ GEPPLENGFL PYLGCALQFG ANPLKFLREK
QKKHGHIFTC QVAGKYIHFL TDPFSYHSLI RQGKYLDWKK FHFATSAKAF GHGSIDPAEG
NTTENFHHTF IRTLQGNALD ALIKAMMENL QYVMLQSRAS KFQPNTWVTE GLYTFCCQVM
FESGFLTLFG KEFNSNHDKN LSKRETERAR ILNALENFKE FDKIFPALVA GLPIHLFKSA
HSAREKLGEA LLHKNLLKRD NLSELVMLRM FLNDTLSTFD DMEKAKTHVA VLWASQANTI
PATFWSLFTF LRNPEAMRAA TKEVQSVLES AGEKISLDGN YISLNRKQLD NMPVLDSIIK
EAMRLSSASM TFRVAKEDFT LHLENSFYNI RKDDIVALYP QLLHFDPEIY ADPLTFKYDR
YLNENKEEKT DFYRNGRKLK YYYMPFGAGI AKCPGRLFAV HEIKQFLVLI FSYFEIDLVD
SNVQCPSLDQ SRAGLGILQP SNDIDFRYRL KCL
//
