ID   C11B3_RAT               Reviewed;         500 AA.
AC   P30100;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-NOV-2008, entry version 72.
DE   RecName: Full=Cytochrome P450 11B3, mitochondrial;
DE            EC=1.14.15.4;
DE            EC=1.14.15.5;
DE   AltName: Full=CYPXIB3;
DE   AltName: Full=P450-Aldo-2;
DE   AltName: Full=Aldosterone synthase;
DE   Flags: Precursor;
GN   Name=Cyp11b3; Synonyms=Cyp11b-3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Adrenal gland;
RX   MEDLINE=90274674; PubMed=2350348; DOI=10.1016/0006-291X(90)91460-A;
RA   Matsukawa N., Nonaka Y., Ying Z., Higaki J., Ogihara T., Okamoto M.;
RT   "Molecular cloning and expression of cDNAS encoding rat aldosterone
RT   synthase: variants of cytochrome P-450(11 beta).";
RL   Biochem. Biophys. Res. Commun. 169:245-252(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=92222921; PubMed=1562515; DOI=10.1016/0960-0760(92)90367-R;
RA   Okamoto M., Nonaka Y.;
RT   "Molecular biology of rat steroid 11 beta-hydroxylase [P450(11 beta)]
RT   and aldosterone synthase [P450(11 beta, aldo)].";
RL   J. Steroid Biochem. Mol. Biol. 41:415-419(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Adrenal gland;
RX   MEDLINE=90242993; PubMed=2129527; DOI=10.1016/0014-5793(90)81398-8;
RA   Imai M., Shimada H., Okada Y., Matsushima-Hibiya Y., Ogishima T.,
RA   Ishimura Y.;
RT   "Molecular cloning of a cDNA encoding aldosterone synthase cytochrome
RT   P-450 in rat adrenal cortex.";
RL   FEBS Lett. 263:299-302(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=93232080; PubMed=8473352;
RA   Mukai K., Imai M., Shimada H., Ishimura Y.;
RT   "Isolation and characterization of rat CYP11B genes involved in late
RT   steps of mineralo- and glucocorticoid syntheses.";
RL   J. Biol. Chem. 268:9130-9137(1993).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=93224492; PubMed=8468320;
RA   Nomura M., Morohashi K., Kirita S., Nonaka Y., Okamoto M., Nawata H.,
RA   Omura T.;
RT   "Three forms of rat CYP11B genes: 11 beta-hydroxylase gene,
RT   aldosterone synthase gene, and a novel gene.";
RL   J. Biochem. 113:144-152(1993).
RN   [6]
RP   PROTEIN SEQUENCE OF 25-44.
RC   STRAIN=Sprague-Dawley; TISSUE=Adrenal gland;
RX   MEDLINE=89291826; PubMed=2738055;
RA   Ogishima T., Mitani F., Ishimura Y.;
RT   "Isolation of aldosterone synthase cytochrome P-450 from zona
RT   glomerulosa mitochondria of rat adrenal cortex.";
RL   J. Biol. Chem. 264:10935-10938(1989).
CC   -!- FUNCTION: Converts 11-deoxycorticosterone into corticosterone, 18-
CC       hydroxycorticosterone, and aldosterone. Also can catalyze the
CC       conversion of 11-deoxycortisol to cortisol, 18-hydroxycortisol and
CC       cortisone.
CC   -!- CATALYTIC ACTIVITY: A steroid + reduced adrenal ferredoxin + O(2)
CC       = an 11-beta-hydroxysteroid + oxidized adrenal ferredoxin + H(2)O.
CC   -!- CATALYTIC ACTIVITY: Corticosterone + reduced adrenal ferredoxin +
CC       O(2) = 18-hydroxycorticosterone + oxidized adrenal ferredoxin +
CC       H(2)O.
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane.
CC   -!- TISSUE SPECIFICITY: Adrenal cortex.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; D00568; BAA00445.1; -; mRNA.
DR   EMBL; X52766; CAA36978.1; -; mRNA.
DR   EMBL; D14097; BAA03172.1; -; Genomic_DNA.
DR   PIR; JX0252; JX0252.
DR   RefSeq; NP_036670.1; -.
DR   UniGene; Rn.144549; -.
DR   HSSP; P00189; 1SCC.
DR   Ensembl; ENSRNOG00000030111; Rattus norvegicus.
DR   GeneID; 24294; -.
DR   KEGG; rno:24294; -.
DR   RGD; 727886; Cyp11b3.
DR   HOVERGEN; P30100; -.
DR   NextBio; 602896; -.
DR   ArrayExpress; P30100; -.
DR   GermOnline; ENSRNOG00000030111; Rattus norvegicus.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0047783; F:corticosterone 18-monooxygenase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
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:EC.
DR   GO; GO:0006700; P:C21-steroid hormone biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002399; Cyt_P450_mit.
DR   Gene3D; G3DSA:1.10.630.10; Cyt_P450; 1.
DR   PANTHER; PTHR19383; Cyt_P450; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00408; MITP450.
DR   PRINTS; PR00385; P450.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Heme; Iron; Membrane; Metal-binding;
KW   Mitochondrion; Monooxygenase; Oxidoreductase; Steroidogenesis;
KW   Transit peptide.
FT   TRANSIT       1     24       Mitochondrion.
FT   CHAIN        25    500       Cytochrome P450 11B3, mitochondrial.
FT                                /FTId=PRO_0000003605.
FT   METAL       447    447       Iron (heme axial ligand) (By similarity).
FT   CONFLICT    310    310       K -> E (in Ref. 3 and 4).
SQ   SEQUENCE   500 AA;  57122 MW;  040F6ECCA84CDEAD CRC64;
     MALRVTADVW LARPWQCLHR TRALGTTATL APKTLKPFEA IPQYSRNKWL KMIQILREQG
     QENLHLEMHQ AFQELGPIFR HSAGGAQIVS VMLPEDAEKL HQVESILPRR MHLEPWVAHR
     ELRGLRRGVF LLNGAEWRFN RLKLNPNVLS PKAVQNFVPM VDEVARDFLE ALKKKVRQNA
     RGSLTMDVQQ SLFNYTIEAS NFALFGERLG LLGHDLNPGS LKFIHALHSM FKSTTQLLFL
     PRSLTRWTST QVWKEHFDAW DVISEYANRC IWKVHQELRL GSSQTYSGIV AALITQGALP
     LDAIKANSMK LTAGSVDTTA IPLVMTLFEL ARNPDVQQAL RQETLAAEAS IAANPQKAMS
     DLPLLRAALK ETLRLYPVGG FLERILNSDL VLQNYHVPAG TLVLLYLYSM GRNPAVFPRP
     ERYMPQRWLE RKRSFQHLAF GFGVRQCLGR RLAEVEMLLL LHHMLKTFQV ETLRQEDVQM
     AYRFVLMPSS SPVLTFRPIS
//