P19099 (C11B2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytochrome P450 11B2, mitochondrial

Alternative name(s):
Aldosterone synthase
Short name=ALDOS
EC=1.14.15.4
EC=1.14.15.5
Aldosterone-synthesizing enzyme
CYPXIB2
Cytochrome P-450Aldo
Cytochrome P-450C18
Steroid 18-hydroxylase

Gene names

Name:

CYP11B2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	503 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Preferentially catalyzes the conversion of 11-deoxycorticosterone to aldosterone via corticosterone and 18-hydroxycorticosterone. Ref.6
Catalytic activity	A steroid + reduced adrenal ferredoxin + O2 = an 11-beta-hydroxysteroid + oxidized adrenal ferredoxin + H2O. Ref.6 Corticosterone + reduced adrenal ferredoxin + O2 = 18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O. Ref.6
Cofactor	Heme group. Ref.6
Subcellular location	Mitochondrion membrane.
Involvement in disease	Corticosterone methyloxidase 1 deficiency (CMO-1 deficiency) [MIM:203400]: Autosomal recessive disorder of aldosterone biosynthesis. There are two biochemically different forms of selective aldosterone deficiency be termed corticosterone methyloxidase (CMO) deficiency type 1 and type 2. In CMO-1 deficiency, aldosterone is undetectable in plasma, while its immediate precursor, 18-hydroxycorticosterone, is low or normal. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Corticosterone methyloxidase 2 deficiency (CMO-2 deficiency) [MIM:610600]: Autosomal recessive disorder of aldosterone biosynthesis. In CMO-2 deficiency, aldosterone can be low or normal, but at the expense of increased secretion of 18-hydroxycorticosterone. Consequently, patients have a greatly increased ratio of 18-hydroxycorticosterone to aldosterone and a low ratio of corticosterone to 18-hydroxycorticosterone in serum. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Familial hyperaldosteronism 1 (FH1) [MIM:103900]: A disorder characterized by hypertension, variable hyperaldosteronism, and abnormal adrenal steroid production, including 18-oxocortisol and 18-hydroxycortisol. There is significant phenotypic heterogeneity, and some individuals never develop hypertension. Note: The disease is caused by mutations affecting the gene represented in this entry. The molecular defect causing hyperaldosteronism familial 1 is an anti-Lepore-type fusion of the CYP11B1 and CYP11B2 genes. The hybrid gene has the promoting part of CYP11B1, ACTH-sensitive, and the coding part of CYP11B2. Ref.10
Sequence similarities	Belongs to the cytochrome P450 family.

Ontologies

Keywords
Biological process	Lipid metabolism Steroid metabolism Steroidogenesis
Cellular component	Membrane Mitochondrion
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Transit peptide
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aldosterone biosynthetic process Inferred from mutant phenotype PubMed 19342457. Source: UniProtKB cellular response to hormone stimulus Inferred from expression pattern PubMed 19342457. Source: UniProtKB cellular response to potassium ion Inferred from expression pattern PubMed 19342457. Source: UniProtKB cortisol biosynthetic process Inferred from mutant phenotype PubMed 19342457. Source: UniProtKB potassium ion homeostasis Inferred from mutant phenotype PubMed 9838244. Source: BHF-UCL regulation of blood volume by renal aldosterone Inferred from mutant phenotype PubMed 14614232. Source: BHF-UCL renal water homeostasis Inferred by curator Ref.2. Source: BHF-UCL sodium ion homeostasis Inferred from mutant phenotype PubMed 9838244. Source: BHF-UCL xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular_component	mitochondrial inner membrane Inferred by curator Ref.2. Source: BHF-UCL
Molecular_function	corticosterone 18-monooxygenase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred by curator Ref.2. Source: BHF-UCL iron ion binding Inferred from electronic annotation. Source: InterPro steroid 11-beta-monooxygenase activity Inferred from direct assay PubMed 1741400Ref.2. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 24

24

Mitochondrion

Chain

25 – 503

479

Cytochrome P450 11B2, mitochondrial

PRO_0000003597

Sites

Metal binding

450

1

Iron (heme axial ligand)

Natural variations

Natural variant

29

1

A → T. Ref.15
Corresponds to variant rs6438 [ dbSNP | Ensembl ].

VAR_014151

Natural variant

30

1

R → Q. Ref.15
Corresponds to variant rs6441 [ dbSNP | Ensembl ].

VAR_014152

Natural variant

140

1

N → NRL in CMO-1 deficiency; the enzyme is inactive.

VAR_018470

Natural variant

173

1

K → R. Ref.14 Ref.15 Ref.17
Corresponds to variant rs4539 [ dbSNP | Ensembl ].

VAR_001266

Natural variant

181

1

R → W in CMO-2 deficiency; reduces 18-hydroxylase and abolishes 18-oxidase activities; leaves 11 beta-hydroxylase activity intact. Ref.7 Ref.8
Corresponds to variant rs28931609 [ dbSNP | Ensembl ].

VAR_001267

Natural variant

185

1

T → I in CMO-2 deficiency. Ref.12 Ref.19

VAR_018471

Natural variant

198

1

E → D in CMO-2 deficiency. Ref.13

VAR_001268

Natural variant

222

1

N → T.
Corresponds to variant rs5308 [ dbSNP | Ensembl ].

VAR_014643

Natural variant

248

1

I → T. Ref.15 Ref.17
Corresponds to variant rs4547 [ dbSNP | Ensembl ].

VAR_014153

Natural variant

281

1

N → S. Ref.15 Ref.17
Corresponds to variant rs4537 [ dbSNP | Ensembl ].

VAR_014154

Natural variant

339

1

I → T. Ref.15 Ref.17
Corresponds to variant rs4544 [ dbSNP | Ensembl ].

VAR_014155

Natural variant

383

1

E → V.
Corresponds to variant rs5312 [ dbSNP | Ensembl ].

VAR_014644

Natural variant

386

1

V → A in CMO-2 deficiency; small but consistent reduction in the production of 18-hydroxycorticosterone. Ref.7 Ref.8 Ref.13 Ref.15 Ref.17
Corresponds to variant rs4541 [ dbSNP | Ensembl ].

VAR_001269

Natural variant

403

1

V → E.
Corresponds to variant rs5315 [ dbSNP | Ensembl ].

VAR_014645

Natural variant

435

1

G → S. Ref.15 Ref.17
Corresponds to variant rs4545 [ dbSNP | Ensembl ].

VAR_014156

Natural variant

461

1

L → P in CMO-1 deficiency; abolishes the 18-hydroxylase activity required for conversion of 11-deoxycorticosterone to aldosterone. Ref.11

VAR_018472

Natural variant

487

1

F → V.
Corresponds to variant rs5317 [ dbSNP | Ensembl ].

VAR_014646

Natural variant

498

1

T → A in CMO-2 deficiency. Ref.19

VAR_018473

Experimental info

Sequence conflict

17

1

S → C in AAA35741. Ref.1

Sequence conflict

55

1

I → M in AAA35741. Ref.1

Sequence conflict

119

1

Y → I in AAA35741. Ref.1

Sequence conflict

249

1

S → R in CAA38539. Ref.2

Sequence conflict

342

1

Q → K in AAA35741. Ref.1

Sequence conflict

438

1

F → L in AAA35741. Ref.1

Sequence conflict

470

1

H → R in AAA35741. Ref.1

Secondary structure

1

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503

Helix Strand Turn

Details...

Helix

38 – 40

3

Helix

48 – 58

11

Helix

64 – 75

12

Beta strand

77 – 80

4

Beta strand

84 – 86

3

Beta strand

88 – 91

4

Helix

94 – 103

10

Helix

114 – 123

10

Helix

129 – 131

3

Helix

134 – 142

9

Helix

145 – 148

4

Helix

151 – 178

28

Beta strand

182 – 186

5

Helix

189 – 205

17

Beta strand

212 – 214

3

Helix

218 – 238

21

Helix

242 – 248

7

Helix

250 – 280

31

Helix

289 – 296

8

Helix

301 – 313

13

Helix

317 – 332

16

Helix

334 – 353

20

Helix

355 – 357

3

Helix

358 – 361

4

Helix

363 – 375

13

Beta strand

381 – 385

5

Beta strand

390 – 392

3

Beta strand

395 – 397

3

Beta strand

402 – 406

5

Helix

407 – 410

4

Turn

414 – 416

3

Beta strand

417 – 419

3

Helix

427 – 430

4

Helix

446 – 448

3

Helix

453 – 470

18

Beta strand

471 – 474

4

Beta strand

483 – 493

11

Beta strand

497 – 501

5

Sequences

	Sequence		Length	Mass (Da)
	P19099 [UniParc]. Last modified July 15, 1998. Version 3. Checksum: 42BA671704CEE35D	FASTA	503	57,560
	10 20 30 40 50 60 MALRAKAEVC VAAPWLSLQR ARALGTRAAR APRTVLPFEA MPQHPGNRWL RLLQIWREQG 70 80 90 100 110 120 YEHLHLEMHQ TFQELGPIFR YNLGGPRMVC VMLPEDVEKL QQVDSLHPCR MILEPWVAYR 130 140 150 160 170 180 QHRGHKCGVF LLNGPEWRFN RLRLNPDVLS PKAVQRFLPM VDAVARDFSQ ALKKKVLQNA 190 200 210 220 230 240 RGSLTLDVQP SIFHYTIEAS NLALFGERLG LVGHSPSSAS LNFLHALEVM FKSTVQLMFM 250 260 270 280 290 300 PRSLSRWISP KVWKEHFEAW DCIFQYGDNC IQKIYQELAF NRPQHYTGIV AELLLKAELS 310 320 330 340 350 360 LEAIKANSME LTAGSVDTTA FPLLMTLFEL ARNPDVQQIL RQESLAAAAS ISEHPQKATT 370 380 390 400 410 420 ELPLLRAALK ETLRLYPVGL FLERVVSSDL VLQNYHIPAG TLVQVFLYSL GRNAALFPRP 430 440 450 460 470 480 ERYNPQRWLD IRGSGRNFHH VPFGFGMRQC LGRRLAEAEM LLLLHHVLKH FLVETLTQED 490 500 IKMVYSFILR PGTSPLLTFR AIN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of two genes encoding human steroid 11 beta-hydroxylase (P-450(11) beta)." Mornet E., Dupont J., Vitek A., White P.C. J. Biol. Chem. 264:20961-20967(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Cloning and expression of a cDNA for human cytochrome P-450aldo as related to primary aldosteronism." Kawamoto T., Mitsuuchi Y., Ohnishi T., Ichikawa Y., Yokoyama Y., Sumimoto H., Toda K., Miyahara K., Kuribayashi I., Nakao K., Hosoda K., Yamamoto Y., Imura H., Shizuta Y. Biochem. Biophys. Res. Commun. 173:309-316(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Adrenal gland.
[3]	Kawamoto T., Miyahara K., Mitsuuchi Y., Ulick S., Shizuta Y. Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Blood.
[4]	NHLBI resequencing and genotyping service (RS&G) Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"Structural insights into aldosterone synthase substrate specificity and targeted inhibition." Strushkevich N., Gilep A.A., Shen L., Arrowsmith C.H., Edwards A.M., Usanov S.A., Park H.W. Mol. Endocrinol. 27:315-324(2013) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 34-503 IN COMPLEXES WITH HEME; DESOXYCORTICOSTERONE AND SYNTHETIC INHIBITOR FADROZOLE, CATALYTIC ACTIVITY, COFACTOR, FUNCTION.
[7]	"Mutations in the human CYP11B2 (aldosterone synthase) gene causing corticosterone methyloxidase II deficiency." Pascoe L., Curnow K.M., Slutsker L., Roesler A., White P.C. Proc. Natl. Acad. Sci. U.S.A. 89:4996-5000(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CMO-2 DEFICIENCY TRP-181 AND ALA-386.
[8]	"Congenitally defective aldosterone biosynthesis in humans: the involvement of point mutations of the P-450C18 gene (CYP11B2) in CMO II deficient patients." Mitsuuchi Y., Kawamoto T., Naiki Y., Miyahara K., Toda K., Kuribayashi I., Orii T., Yasuda K., Miura K., Nakao K., Imura H., Ulick S., Shizuta Y. Biochem. Biophys. Res. Commun. 182:974-979(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CMO-2 DEFICIENCY TRP-181 AND ALA-386.
[9]	Erratum Mitsuuchi Y., Kawamoto T., Naiki Y., Miyahara K., Toda K., Kuribayashi I., Orii T., Yasuda K., Miura K., Nakao K., Imura H., Ulick S., Shizuta Y. Biochem. Biophys. Res. Commun. 184:1529-1530(1992)
[10]	"Congenitally defective aldosterone biosynthesis in humans: inactivation of the P-450(C18) gene (CYP11B2) due to nucleotide deletion in CMO I deficient patients." Mitsuuchi Y., Kawamoto T., Miyahara K., Ulick S., Morton D.H., Naiki Y., Kuribayashi I., Toda K., Hara T., Orii T., Yasuda K., Miura K., Yamamoto Y., Imura H., Shizuta Y. Biochem. Biophys. Res. Commun. 190:864-869(1993) [PubMed] [Europe PMC] [Abstract] Cited for: DISEASE.
[11]	"CMO I deficiency caused by a point mutation in exon 8 of the human CYP11B2 gene encoding steroid 18-hydroxylase (P450C18)." Nomoto S., Massa G., Mitani F., Ishimura Y., Miyahara K., Toda K., Nagano I., Yamashiro T., Ogoshi S., Fukata J., Onishi S., Hashimoto K., Doi Y., Imura H., Shizuta Y. Biochem. Biophys. Res. Commun. 234:382-385(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CMO-1 DEFICIENCY PRO-461.
[12]	"Mutation THR-185 ILE is associated with corticosterone methyl oxidase deficiency type II." Peter M., Buenger K., Solyom J., Sippell W.G. Eur. J. Pediatr. 157:378-381(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CMO-2 DEFICIENCY ILE-185.
[13]	"Isolated aldosterone synthase deficiency caused by simultaneous E198D and V386A mutations in the CYP11B2 gene." Portrat-Doyen S., Tourniaire J., Richard O., Mulatero P., Aupetit-Faisant B., Curnow K.M., Pascoe L., Morel Y. J. Clin. Endocrinol. Metab. 83:4156-4161(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CMO-2 DEFICIENCY ASP-198 AND ALA-386.
[14]	"Genetic polymorphism of CYP11B2 gene and hypertension in Japanese." Tamaki S., Iwai N., Tsujita Y., Kinoshita M. Hypertension 33:266-270(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ARG-173.
[15]	"Characterization of single-nucleotide polymorphisms in coding regions of human genes." Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS THR-29; GLN-30; ARG-173; THR-248; SER-281; THR-339; ALA-386 AND SER-435.
[16]	Erratum Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 23:373-373(1999)
[17]	"Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis." Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A., Cooper R., Lipshutz R., Chakravarti A. Nat. Genet. 22:239-247(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ARG-173; THR-248; SER-281; THR-339; ALA-386 AND SER-435.
[18]	"Type 1 aldosterone synthase deficiency presenting in a middle-aged man." Kayes-Wandover K.M., Schindler R.E.L., Taylor H.C., White P.C. J. Clin. Endocrinol. Metab. 86:1008-1012(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CMO-1 DEFICIENCY ARG-LEU-140 INS.
[19]	"A compound heterozygote case of type II aldosterone synthase deficiency." Dunlop F.M., Crock P.A., Montalto J., Funder J.W., Curnow K.M. J. Clin. Endocrinol. Metab. 88:2518-2526(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CMO-2 DEFICIENCY ILE-185 AND ALA-498.
+	Additional computationally mapped references.

Web resources

GeneReviews

Wikipedia

CYP11B2 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M32881, M32864, M32880 Genomic DNA. Translation: AAA35741.1.
X54741 mRNA. Translation: CAA38539.1.
D13752 Genomic DNA. Translation: BAA02899.1.
EU326306 Genomic DNA. Translation: ACA05912.1.
CH471162 Genomic DNA. Translation: EAW82292.1.

IPI

IPI00290116.

PIR

B34181.

RefSeq

NP_000489.3. NM_000498.3.

UniGene

Hs.632054.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4DVQ	X-ray	2.49	A/B/C/D/E/F/G/H/I/J/K/L	34-503	[»]
4FDH	X-ray	2.71	A/B/C/D/E/F/G/H/I/J/K/L	34-503	[»]

ProteinModelPortal

P19099.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000325822.

Polymorphism databases

DMDM

3041666.

Proteomic databases

PaxDb

P19099.

PRIDE

P19099.

Protocols and materials databases

DNASU

1585.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000323110; ENSP00000325822; ENSG00000179142.

GeneID

1585.

KEGG

hsa:1585.

UCSC

uc003yxk.1. human.

Organism-specific databases

CTD

1585.

GeneCards

GC08M143988.

H-InvDB

HIX0034383.

HGNC

HGNC:2592. CYP11B2.

HPA

HPA049171.

MIM

103900. phenotype.
124080. gene.
203400. phenotype.
610600. phenotype.

neXtProt

NX_P19099.

Orphanet

403. Familial hyperaldosteronism type 1.
99763. Familial hyperreninemic hypoaldosteronism type 1.
99764. Familial hyperreninemic hypoaldosteronism type 2.

PharmGKB

PA134.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2124.

HOGENOM

HOG000013161.

HOVERGEN

HBG051098.

InParanoid

P19099.

KO

K07433.

OMA

QVFLYSL.

OrthoDB

EOG4B2SWV.

PhylomeDB

P19099.

Enzyme and pathway databases

BioCyc

MetaCyc:HS11355-MONOMER.

Reactome

REACT_111217. Metabolism.
REACT_15493. Steroid hormones.

Gene expression databases

ArrayExpress

P19099.

Bgee

P19099.

CleanEx

HS_CYP11B2.

Genevestigator

P19099.

GermOnline

ENSG00000179142. Homo sapiens.

Family and domain databases

Gene3D

1.10.630.10. 1 hit.

InterPro

IPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002399. Cyt_P450_mitochondrial.
[Graphical view]

Pfam

PF00067. p450. 1 hit.
[Graphical view]

PRINTS

PR00408. MITP450.
PR00385. P450.

SUPFAM

SSF48264. Cytochrome_P450. 1 hit.

PROSITE

PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P19099.

ChEMBL

CHEMBL2722.

DrugBank

DB00796. Candesartan.
DB01011. Metyrapone.

GenomeRNAi

1585.

NextBio

6515.

SOURCE

Search...

Entry information

Entry name

C11B2_HUMAN

Accession

Primary (citable) accession number: P19099
Secondary accession number(s): B0ZBE4, Q16726

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	July 15, 1998
Last modified:	May 1, 2013
This is version 149 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.