C11B1_SHEEP
ID C11B1_SHEEP Reviewed; 503 AA.
AC P51663; O19181;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Cytochrome P450 11B1, mitochondrial;
DE AltName: Full=CYPXIB1;
DE AltName: Full=Cytochrome P450C11;
DE AltName: Full=Steroid 11-beta-hydroxylase, CYP11B1 {ECO:0000250|UniProtKB:P15538};
DE EC=1.14.15.4 {ECO:0000250|UniProtKB:P15538};
DE Flags: Precursor;
GN Name=CYP11B1;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Merino; TISSUE=Adrenal cortex;
RX PubMed=7999785; DOI=10.1016/0167-4781(94)00190-e;
RA Boon W.C., Roche P.J., Hammond V.E., Jeyaseelan K., Crawford R.J.,
RA Coghlan J.P.;
RT "Cloning and expression analysis of a cytochrome P-450(11 beta) cDNA in
RT sheep.";
RL Biochim. Biophys. Acta 1260:109-112(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Adrenal gland, and Liver;
RX PubMed=10728821; DOI=10.3109/10425179809020897;
RA Anwar A., Coghlan J.P., Jeyaseelan K.;
RT "Structure of an ovine CYP11B1 gene.";
RL DNA Seq. 8:357-374(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77.
RX PubMed=7804143;
RA Anwar A., Jeyaseelan K., Coghlan J.P.;
RT "Molecular cloning and characterization of the ovine CYP11B1 promoter.";
RL Biochem. Mol. Biol. Int. 33:1169-1178(1994).
CC -!- FUNCTION: A cytochrome P450 monooxygenase involved in the biosynthesis
CC of adrenal corticoids. Catalyzes the hydroxylation of carbon hydrogen
CC bond at 11-beta position of 11-deoxycortisol and 11-
CC deoxycorticosterone/21-hydroxyprogesterone yielding cortisol or
CC corticosterone, respectively. Mechanistically, uses molecular oxygen
CC inserting one oxygen atom into a substrate and reducing the second into
CC a water molecule. Two electrons are provided by NADPH via a two-protein
CC mitochondrial transfer system comprising flavoprotein FDXR
CC (adrenodoxin/ferredoxin reductase) and nonheme iron-sulfur protein FDX1
CC or FDX2 (adrenodoxin/ferredoxin). {ECO:0000250|UniProtKB:P15538}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a steroid + 2 H(+) + O2 + 2 reduced [adrenodoxin] = an 11beta-
CC hydroxysteroid + H2O + 2 oxidized [adrenodoxin];
CC Xref=Rhea:RHEA:15629, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:35341,
CC ChEBI:CHEBI:35346; EC=1.14.15.4;
CC Evidence={ECO:0000250|UniProtKB:P15538};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15630;
CC Evidence={ECO:0000250|UniProtKB:P15538};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11-deoxycortisol + 2 H(+) + O2 + 2 reduced [adrenodoxin] =
CC cortisol + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:46100,
CC Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17650,
CC ChEBI:CHEBI:28324, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738;
CC Evidence={ECO:0000250|UniProtKB:P15538};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46101;
CC Evidence={ECO:0000250|UniProtKB:P15538};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=21-hydroxyprogesterone + 2 H(+) + O2 + 2 reduced [adrenodoxin]
CC = corticosterone + H2O + 2 oxidized [adrenodoxin];
CC Xref=Rhea:RHEA:46104, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16827, ChEBI:CHEBI:16973, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738; Evidence={ECO:0000250|UniProtKB:P15538};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46105;
CC Evidence={ECO:0000250|UniProtKB:P15538};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P19099};
CC -!- PATHWAY: Steroid biosynthesis; glucocorticoid biosynthesis.
CC {ECO:0000250|UniProtKB:P15538}.
CC -!- PATHWAY: Steroid hormone biosynthesis. {ECO:0000250|UniProtKB:P15538}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P14137}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P14137}.
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; L34337; AAA62308.1; -; mRNA.
DR EMBL; L47569; AAA81576.1; -; Genomic_DNA.
DR EMBL; U78478; AAB64249.1; -; Genomic_DNA.
DR EMBL; U78477; AAB64248.1; -; mRNA.
DR EMBL; L28716; AAA83384.1; -; Genomic_DNA.
DR PIR; S52085; S52085.
DR RefSeq; NP_001068568.1; NM_001075100.2.
DR AlphaFoldDB; P51663; -.
DR SMR; P51663; -.
DR STRING; 9940.ENSOARP00000000890; -.
DR Ensembl; ENSOART00020020700; ENSOARP00020017139; ENSOARG00020013254.
DR GeneID; 767576; -.
DR KEGG; oas:767576; -.
DR CTD; 1584; -.
DR eggNOG; KOG0159; Eukaryota.
DR OrthoDB; 481145at2759; -.
DR UniPathway; UPA00788; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004507; F:steroid 11-beta-monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006704; P:glucocorticoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 2: Evidence at transcript level;
KW Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Monooxygenase; Oxidoreductase;
KW Reference proteome; Steroidogenesis; Transit peptide.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT CHAIN 25..503
FT /note="Cytochrome P450 11B1, mitochondrial"
FT /id="PRO_0000003606"
FT BINDING 450
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:P19099"
FT CONFLICT 99
FT /note="R -> S (in Ref. 2; AAB64248/AAB64249)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="A -> G (in Ref. 1; AAA62308)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="P -> R (in Ref. 1; AAA62308)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="R -> G (in Ref. 2; AAB64248/AAB64249)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 503 AA; 57784 MW; 968F2DF6EE7D595B CRC64;
MALWAKARVW MAGPWLSLHR ARPLGTRASA APKAVLPFEA MPRCPGNKWM RVLQIWKEQG
SENMHLDMHQ TFQELGPIFR YDVGGRHMVF VMLPEDVERL QQAESLHPQR MLLEPWLAYR
QARGHKCGVF LLNGPQWRLD RLRLNPDVLS LPALQKYTPL VDGVARDFSQ TLKARVLQNA
RGSLTLDIAP SVFRYTIEAS TLVLYGERLG LLTQQPNPDS LNFIHALEAM FKSTVQLMFV
PRRLSRWTSS SMWREHFEAW DYIFQYANRA IQRIYQELAL GHPWHYSGIV AELLMRADMT
LDTIKANTID LTAGSVDTTA FPLLMTLFEL ARNPEVQQAL RQESLVAEAR ISENPQRATT
ELPLLRAALK ETLRLYPVGI TLERQVSSDL VLQNYHIPAG TLVKVLLYSL GRNPAVFARP
ESYHPQRWLD RQGSGSRFPH LAFGFGMRQC LGRRVAEVEM LLLLHHVLKN FLVETLAQED
IKMVYRFILM PSTLPLFTFR AIQ
