ID   C11B2_RAT               Reviewed;         510 AA.
AC   P30099; Q64540;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-NOV-2008, entry version 76.
DE   RecName: Full=Cytochrome P450 11B2, mitochondrial;
DE            EC=1.14.15.4;
DE            EC=1.14.15.5;
DE   AltName: Full=CYPXIB2;
DE   AltName: Full=P450-Aldo-1;
DE   AltName: Full=Aldosterone synthase;
DE   Flags: Precursor;
GN   Name=Cyp11b2; Synonyms=Cyp11b-2;
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 [MRNA].
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   STRAIN=Sprague-Dawley; TISSUE=Adrenal gland;
RX   MEDLINE=93326104; PubMed=8333830; DOI=10.1006/bbrc.1993.1792;
RA   Zhou M., Gomez-Sanchez C.E.;
RT   "Cloning and expression of a rat cytochrome P-450 11 beta-
RT   hydroxylase/aldosterone synthase (CYP11B2) cDNA variant.";
RL   Biochem. Biophys. Res. Commun. 194:112-117(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, AND VARIANT GLY-84.
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   [5]
RP   PROTEIN SEQUENCE OF 35-54.
RC   TISSUE=Adrenal cortex;
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   -!- INDUCTION: A 12-fold increase was seen in the presence of a low
CC       sodium-high potassium diet.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; D00567; BAA00444.1; -; mRNA.
DR   EMBL; U14908; AAB60457.1; -; mRNA.
DR   PIR; A35342; A35342.
DR   PIR; JN0615; JN0615.
DR   UniGene; Rn.144549; -.
DR   HSSP; P00189; 1SCC.
DR   Ensembl; ENSRNOG00000030111; Rattus norvegicus.
DR   RGD; 2454; Cyp11b2.
DR   HOVERGEN; P30099; -.
DR   ArrayExpress; P30099; -.
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     34       Mitochondrion.
FT   CHAIN        35    510       Cytochrome P450 11B2, mitochondrial.
FT                                /FTId=PRO_0000003604.
FT   METAL       457    457       Iron (heme axial ligand) (By similarity).
FT   VARIANT      84     84       E -> G.
FT   VARIANT     146    146       E -> D.
FT   VARIANT     261    261       Q -> R.
FT   VARIANT     509    509       I -> V.
FT   CONFLICT      1     13       MGACDNDFIELHS -> MNKAPAKAL (in Ref. 3).
SQ   SEQUENCE   510 AA;  58241 MW;  2E5129EE513DEA9E CRC64;
     MGACDNDFIE LHSRVTADVW 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 LDAIKANSME LTAGSVDTTA IPLVMTLFEL ARNPDVQQAL RQETLAAEAS
     IAANPQKAMS DLPLLRAALK ETLRLYPVGG FLERILNSDL VLQNYHVPAG TLVLLYLYSM
     GRNPAVFPRP ERYMPQRWLE RKRSFQHLAF GFGVRQCLGR RLAEVEMLLL LHHMLKTFQV
     ETLRQEDVQM AYRFVLMPSS SPVLTFRPIS
//