C11B3_RAT
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 03-AUG-2022, entry version 138.
DE RecName: Full=Cytochrome P450 11B3, mitochondrial;
DE AltName: Full=Aldosterone synthase;
DE AltName: Full=CYPXIB3;
DE AltName: Full=Cytochrome P450-Aldo-2;
DE AltName: Full=Steroid 11-beta-hydroxylase;
DE EC=1.14.15.4;
DE EC=1.14.15.5;
DE Flags: Precursor;
GN Name=Cyp11b3; Synonyms=Cyp11b-3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adrenal gland;
RX 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 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)] and
RT 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 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 P-450
RT in rat adrenal cortex.";
RL FEBS Lett. 263:299-302(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8473352; DOI=10.1016/s0021-9258(18)52987-2;
RA Mukai K., Imai M., Shimada H., Ishimura Y.;
RT "Isolation and characterization of rat CYP11B genes involved in late steps
RT of mineralo- and glucocorticoid syntheses.";
RL J. Biol. Chem. 268:9130-9137(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8468320; DOI=10.1093/oxfordjournals.jbchem.a124018;
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, aldosterone
RT 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 PubMed=2738055; DOI=10.1016/s0021-9258(18)60408-9;
RA Ogishima T., Mitani F., Ishimura Y.;
RT "Isolation of aldosterone synthase cytochrome P-450 from zona glomerulosa
RT 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. Can also catalyze the
CC conversion of 11-deoxycortisol to cortisol, 18-hydroxycortisol and
CC cortisone.
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:P19099};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=corticosterone + 2 H(+) + O2 + 2 reduced [adrenodoxin] = 18-
CC hydroxycorticosterone + H2O + 2 oxidized [adrenodoxin];
CC Xref=Rhea:RHEA:11872, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16485, ChEBI:CHEBI:16827, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738; EC=1.14.15.5;
CC Evidence={ECO:0000250|UniProtKB:P19099};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P19099};
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane.
CC -!- TISSUE SPECIFICITY: Adrenal cortex.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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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 AlphaFoldDB; P30100; -.
DR SMR; P30100; -.
DR STRING; 10116.ENSRNOP00000049722; -.
DR PaxDb; P30100; -.
DR UCSC; RGD:727886; rat.
DR RGD; 727886; Cyp11b3.
DR eggNOG; KOG0159; Eukaryota.
DR InParanoid; P30100; -.
DR Reactome; R-RNO-193993; Mineralocorticoid biosynthesis.
DR Reactome; R-RNO-194002; Glucocorticoid biosynthesis.
DR Reactome; R-RNO-211976; Endogenous sterols.
DR PRO; PR:P30100; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0047783; F:corticosterone 18-monooxygenase activity; IDA:RGD.
DR GO; GO:0020037; F:heme binding; ISO:RGD.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004507; F:steroid 11-beta-monooxygenase activity; IDA:RGD.
DR GO; GO:0030325; P:adrenal gland development; IEP:RGD.
DR GO; GO:0032342; P:aldosterone biosynthetic process; ISO:RGD.
DR GO; GO:0006700; P:C21-steroid hormone biosynthetic process; ISO:RGD.
DR GO; GO:0032870; P:cellular response to hormone stimulus; ISO:RGD.
DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IBA:GO_Central.
DR GO; GO:0035865; P:cellular response to potassium ion; ISO:RGD.
DR GO; GO:0008203; P:cholesterol metabolic process; IBA:GO_Central.
DR GO; GO:0034651; P:cortisol biosynthetic process; ISO:RGD.
DR GO; GO:0034650; P:cortisol metabolic process; IBA:GO_Central.
DR GO; GO:0006704; P:glucocorticoid biosynthetic process; ISO:RGD.
DR GO; GO:0055075; P:potassium ion homeostasis; ISO:RGD.
DR GO; GO:0002017; P:regulation of blood volume by renal aldosterone; ISO:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR GO; GO:0055078; P:sodium ion homeostasis; ISO:RGD.
DR GO; GO:0008202; P:steroid metabolic process; IDA:RGD.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002399; Cyt_P450_mitochondrial.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00408; MITP450.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
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; Reference proteome;
KW Steroidogenesis; Transit peptide.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2738055"
FT CHAIN 25..500
FT /note="Cytochrome P450 11B3, mitochondrial"
FT /id="PRO_0000003605"
FT BINDING 447
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"
FT CONFLICT 310
FT /note="K -> E (in Ref. 3; CAA36978 and 4; BAA03172)"
FT /evidence="ECO:0000305"
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
