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Cytochrome P450 11B2, mitochondrial (Aldosterone synthase) (CYPXIB2) (Cytochrome P450-Aldo-1) (Steroid 11-beta-hydroxylase) (EC 1.14.15.4) (EC 1.14.15.5)

 C11B2_RAT               Reviewed;         510 AA.
P30099; Q64540;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
05-JUL-2017, entry version 133.
RecName: Full=Cytochrome P450 11B2, mitochondrial;
AltName: Full=Aldosterone synthase;
AltName: Full=CYPXIB2;
AltName: Full=Cytochrome P450-Aldo-1;
AltName: Full=Steroid 11-beta-hydroxylase;
EC=1.14.15.4;
EC=1.14.15.5;
Flags: Precursor;
Name=Cyp11b2; Synonyms=Cyp11b-2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Adrenal gland;
PubMed=2350348; DOI=10.1016/0006-291X(90)91460-A;
Matsukawa N., Nonaka Y., Ying Z., Higaki J., Ogihara T., Okamoto M.;
"Molecular cloning and expression of cDNAS encoding rat aldosterone
synthase: variants of cytochrome P-450(11 beta).";
Biochem. Biophys. Res. Commun. 169:245-252(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1562515; DOI=10.1016/0960-0760(92)90367-R;
Okamoto M., Nonaka Y.;
"Molecular biology of rat steroid 11 beta-hydroxylase [P450(11 beta)]
and aldosterone synthase [P450(11 beta, aldo)].";
J. Steroid Biochem. Mol. Biol. 41:415-419(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Adrenal gland;
PubMed=8333830; DOI=10.1006/bbrc.1993.1792;
Zhou M., Gomez-Sanchez C.E.;
"Cloning and expression of a rat cytochrome P-450 11 beta-
hydroxylase/aldosterone synthase (CYP11B2) cDNA variant.";
Biochem. Biophys. Res. Commun. 194:112-117(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, AND VARIANT GLY-84.
PubMed=8468320; DOI=10.1093/oxfordjournals.jbchem.a124018;
Nomura M., Morohashi K., Kirita S., Nonaka Y., Okamoto M., Nawata H.,
Omura T.;
"Three forms of rat CYP11B genes: 11 beta-hydroxylase gene,
aldosterone synthase gene, and a novel gene.";
J. Biochem. 113:144-152(1993).
[5]
PROTEIN SEQUENCE OF 35-54.
TISSUE=Adrenal cortex;
PubMed=2738055;
Ogishima T., Mitani F., Ishimura Y.;
"Isolation of aldosterone synthase cytochrome P-450 from zona
glomerulosa mitochondria of rat adrenal cortex.";
J. Biol. Chem. 264:10935-10938(1989).
-!- FUNCTION: Converts 11-deoxycorticosterone into corticosterone, 18-
hydroxycorticosterone, and aldosterone. Also can catalyze the
conversion of 11-deoxycortisol to cortisol, 18-hydroxycortisol and
cortisone.
-!- CATALYTIC ACTIVITY: A steroid + 2 reduced adrenodoxin + O(2) + 2
H(+) = an 11-beta- hydroxysteroid + 2 oxidized adrenodoxin +
H(2)O. {ECO:0000250|UniProtKB:P19099}.
-!- CATALYTIC ACTIVITY: Corticosterone + 2 reduced adrenodoxin + O(2)
+ 2 H(+) = 18-hydroxycorticosterone + 2 oxidized adrenodoxin +
H(2)O. {ECO:0000250|UniProtKB:P19099}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000250|UniProtKB:P19099};
-!- SUBCELLULAR LOCATION: Mitochondrion membrane.
-!- TISSUE SPECIFICITY: Adrenal cortex.
-!- INDUCTION: A 12-fold increase was seen in the presence of a low
sodium-high potassium diet. {ECO:0000269|PubMed:8468320}.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D00567; BAA00444.1; -; mRNA.
EMBL; U14908; AAB60457.1; -; mRNA.
PIR; A35342; A35342.
PIR; JN0615; JN0615.
UniGene; Rn.144549; -.
ProteinModelPortal; P30099; -.
SMR; P30099; -.
BindingDB; P30099; -.
ChEMBL; CHEMBL3237; -.
iPTMnet; P30099; -.
PhosphoSitePlus; P30099; -.
PaxDb; P30099; -.
PRIDE; P30099; -.
UCSC; RGD:2454; rat.
RGD; 2454; Cyp11b2.
eggNOG; KOG0159; Eukaryota.
eggNOG; COG2124; LUCA.
HOGENOM; HOG000013161; -.
HOVERGEN; HBG051098; -.
InParanoid; P30099; -.
PhylomeDB; P30099; -.
PRO; PR:P30099; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0047783; F:corticosterone 18-monooxygenase activity; IDA:RGD.
GO; GO:0020037; F:heme binding; ISS:UniProtKB.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0004507; F:steroid 11-beta-monooxygenase activity; IDA:RGD.
GO; GO:0032342; P:aldosterone biosynthetic process; IDA:RGD.
GO; GO:0006700; P:C21-steroid hormone biosynthetic process; IDA:RGD.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
GO; GO:0031670; P:cellular response to nutrient; IEP:RGD.
GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEP:RGD.
GO; GO:0051365; P:cellular response to potassium ion starvation; IEP:RGD.
GO; GO:0034650; P:cortisol metabolic process; IBA:GO_Central.
GO; GO:0006704; P:glucocorticoid biosynthetic process; IDA:RGD.
GO; GO:0045777; P:positive regulation of blood pressure; IMP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0032868; P:response to insulin; IEP:RGD.
GO; GO:0007584; P:response to nutrient; IEP:RGD.
GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
GO; GO:0009651; P:response to salt stress; IEP:RGD.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002399; Cyt_P450_mitochondrial.
Pfam; PF00067; p450; 1.
PRINTS; PR00408; MITP450.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Heme; Iron; Membrane;
Metal-binding; Mitochondrion; Monooxygenase; Oxidoreductase;
Reference proteome; Steroidogenesis; Transit peptide.
TRANSIT 1 34 Mitochondrion.
{ECO:0000269|PubMed:2738055}.
CHAIN 35 510 Cytochrome P450 11B2, mitochondrial.
/FTId=PRO_0000003604.
METAL 457 457 Iron (heme axial ligand). {ECO:0000250}.
VARIANT 84 84 E -> G. {ECO:0000269|PubMed:8468320}.
VARIANT 146 146 E -> D.
VARIANT 261 261 Q -> R.
VARIANT 509 509 I -> V.
CONFLICT 1 13 MGACDNDFIELHS -> MNKAPAKAL (in Ref. 3;
AAB60457). {ECO:0000305}.
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


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