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Protein

Cytochrome P450 11B2, mitochondrial

Gene

CYP11B2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Preferentially catalyzes the conversion of 11-deoxycorticosterone to aldosterone via corticosterone and 18-hydroxycorticosterone.1 Publication

Catalytic activityi

A steroid + 2 reduced adrenodoxin + O2 + 2 H+ = an 11-beta- hydroxysteroid + 2 oxidized adrenodoxin + H2O.1 Publication
Corticosterone + 2 reduced adrenodoxin + O2 + 2 H+ = 18-hydroxycorticosterone + 2 oxidized adrenodoxin + H2O.1 Publication

Cofactori

heme1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi450Iron (heme axial ligand)1

GO - Molecular functioni

GO - Biological processi

  • aldosterone biosynthetic process Source: UniProtKB
  • C21-steroid hormone biosynthetic process Source: BHF-UCL
  • cellular response to hormone stimulus Source: UniProtKB
  • cellular response to peptide hormone stimulus Source: GO_Central
  • cellular response to potassium ion Source: UniProtKB
  • cholesterol metabolic process Source: GO_Central
  • cortisol biosynthetic process Source: UniProtKB
  • mineralocorticoid biosynthetic process Source: Reactome
  • potassium ion homeostasis Source: BHF-UCL
  • regulation of blood volume by renal aldosterone Source: BHF-UCL
  • renal water homeostasis Source: BHF-UCL
  • secondary metabolite biosynthetic process Source: GO_Central
  • sodium ion homeostasis Source: BHF-UCL
  • sterol metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Lipid metabolism, Steroid metabolism, Steroidogenesis

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS11355-MONOMER.
ZFISH:HS11355-MONOMER.
BRENDAi1.14.15.4. 2681.
ReactomeiR-HSA-193993. Mineralocorticoid biosynthesis.
R-HSA-194002. Glucocorticoid biosynthesis.
R-HSA-211976. Endogenous sterols.

Chemistry databases

SwissLipidsiSLP:000001198.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome P450 11B2, mitochondrial
Alternative name(s):
Aldosterone synthase (EC:1.14.15.4, EC:1.14.15.5)
Short name:
ALDOS
Aldosterone-synthesizing enzyme
CYPXIB2
Cytochrome P-450Aldo
Cytochrome P-450C18
Steroid 18-hydroxylase
Gene namesi
Name:CYP11B2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:2592. CYP11B2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: BHF-UCL
  • mitochondrion Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Corticosterone methyloxidase 1 deficiency (CMO-1 deficiency)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal 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.
See also OMIM:203400
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_018470140N → NRL in CMO-1 deficiency; the enzyme is inactive. 1
Natural variantiVAR_018472461L → P in CMO-1 deficiency; abolishes the 18-hydroxylase activity required for conversion of 11-deoxycorticosterone to aldosterone. 1 PublicationCorresponds to variant rs72554627dbSNPEnsembl.1
Corticosterone methyloxidase 2 deficiency (CMO-2 deficiency)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal 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.
See also OMIM:610600
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_001267181R → W in CMO-2 deficiency; reduces 18-hydroxylase and abolishes 18-oxidase activities; leaves 11 beta-hydroxylase activity intact. 2 PublicationsCorresponds to variant rs28931609dbSNPEnsembl.1
Natural variantiVAR_018471185T → I in CMO-2 deficiency. 2 PublicationsCorresponds to variant rs121912978dbSNPEnsembl.1
Natural variantiVAR_001268198E → D in CMO-2 deficiency. 1 PublicationCorresponds to variant rs104894072dbSNPEnsembl.1
Natural variantiVAR_001269386V → A in CMO-2 deficiency; small but consistent reduction in the production of 18-hydroxycorticosterone. 5 PublicationsCorresponds to variant rs61757294dbSNPEnsembl.1
Natural variantiVAR_018473498T → A in CMO-2 deficiency. 1 PublicationCorresponds to variant rs72554626dbSNPEnsembl.1
Hyperaldosteronism, familial, 1 (HALD1)
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.
Disease descriptionA 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.
See also OMIM:103900

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi1585.
MalaCardsiCYP11B2.
MIMi103900. phenotype.
203400. phenotype.
610600. phenotype.
OpenTargetsiENSG00000179142.
Orphaneti403. Familial hyperaldosteronism type I.
99763. Familial hyperreninemic hypoaldosteronism type 1.
PharmGKBiPA134.

Chemistry databases

ChEMBLiCHEMBL2722.
DrugBankiDB00700. Eplerenone.
DB00292. Etomidate.
DB00741. Hydrocortisone.
DB01233. Metoclopramide.
DB01011. Metyrapone.
DB00421. Spironolactone.
GuidetoPHARMACOLOGYi1360.

Polymorphism and mutation databases

BioMutaiCYP11B2.
DMDMi3041666.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 24MitochondrionAdd BLAST24
ChainiPRO_000000359725 – 503Cytochrome P450 11B2, mitochondrialAdd BLAST479

Proteomic databases

PaxDbiP19099.
PeptideAtlasiP19099.
PRIDEiP19099.

PTM databases

iPTMnetiP19099.
PhosphoSitePlusiP19099.

Expressioni

Gene expression databases

BgeeiENSG00000179142.
CleanExiHS_CYP11B2.
GenevisibleiP19099. HS.

Organism-specific databases

HPAiHPA049171.
HPA056348.
HPA057752.

Interactioni

Protein-protein interaction databases

BioGridi107957. 1 interactor.
STRINGi9606.ENSP00000325822.

Chemistry databases

BindingDBiP19099.

Structurei

Secondary structure

1503
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi38 – 40Combined sources3
Helixi48 – 58Combined sources11
Helixi64 – 75Combined sources12
Beta strandi77 – 80Combined sources4
Beta strandi84 – 86Combined sources3
Beta strandi88 – 91Combined sources4
Helixi94 – 103Combined sources10
Helixi114 – 123Combined sources10
Helixi129 – 131Combined sources3
Helixi134 – 142Combined sources9
Helixi145 – 148Combined sources4
Helixi151 – 178Combined sources28
Beta strandi182 – 186Combined sources5
Helixi189 – 205Combined sources17
Beta strandi212 – 214Combined sources3
Helixi218 – 238Combined sources21
Helixi242 – 248Combined sources7
Helixi250 – 280Combined sources31
Helixi289 – 296Combined sources8
Helixi301 – 313Combined sources13
Helixi317 – 332Combined sources16
Helixi334 – 353Combined sources20
Helixi355 – 357Combined sources3
Helixi358 – 361Combined sources4
Helixi363 – 375Combined sources13
Beta strandi381 – 385Combined sources5
Beta strandi390 – 392Combined sources3
Beta strandi395 – 397Combined sources3
Beta strandi402 – 406Combined sources5
Helixi407 – 410Combined sources4
Turni414 – 416Combined sources3
Beta strandi417 – 419Combined sources3
Helixi427 – 430Combined sources4
Helixi446 – 448Combined sources3
Helixi453 – 470Combined sources18
Beta strandi471 – 474Combined sources4
Beta strandi483 – 493Combined sources11
Beta strandi497 – 501Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4DVQX-ray2.49A/B/C/D/E/F/G/H/I/J/K/L34-503[»]
4FDHX-ray2.71A/B/C/D/E/F/G/H/I/J/K/L34-503[»]
4ZGXX-ray3.20A/B/C/D/E/F/G/H/I/J/K/L28-503[»]
ProteinModelPortaliP19099.
SMRiP19099.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0159. Eukaryota.
COG2124. LUCA.
GeneTreeiENSGT00760000119243.
HOGENOMiHOG000013161.
HOVERGENiHBG051098.
InParanoidiP19099.
KOiK07433.
OMAiPFEAMPQ.
OrthoDBiEOG091G0B8F.
PhylomeDBiP19099.
TreeFamiTF105094.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002399. Cyt_P450_mitochondrial.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00408. MITP450.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P19099-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALRAKAEVC VAAPWLSLQR ARALGTRAAR APRTVLPFEA MPQHPGNRWL
60 70 80 90 100
RLLQIWREQG YEHLHLEMHQ TFQELGPIFR YNLGGPRMVC VMLPEDVEKL
110 120 130 140 150
QQVDSLHPCR MILEPWVAYR QHRGHKCGVF LLNGPEWRFN RLRLNPDVLS
160 170 180 190 200
PKAVQRFLPM VDAVARDFSQ ALKKKVLQNA RGSLTLDVQP SIFHYTIEAS
210 220 230 240 250
NLALFGERLG LVGHSPSSAS LNFLHALEVM FKSTVQLMFM PRSLSRWISP
260 270 280 290 300
KVWKEHFEAW DCIFQYGDNC IQKIYQELAF NRPQHYTGIV AELLLKAELS
310 320 330 340 350
LEAIKANSME LTAGSVDTTA FPLLMTLFEL ARNPDVQQIL RQESLAAAAS
360 370 380 390 400
ISEHPQKATT ELPLLRAALK ETLRLYPVGL FLERVVSSDL VLQNYHIPAG
410 420 430 440 450
TLVQVFLYSL GRNAALFPRP ERYNPQRWLD IRGSGRNFHH VPFGFGMRQC
460 470 480 490 500
LGRRLAEAEM LLLLHHVLKH FLVETLTQED IKMVYSFILR PGTSPLLTFR

AIN
Length:503
Mass (Da):57,560
Last modified:July 15, 1998 - v3
Checksum:i42BA671704CEE35D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti17S → C in AAA35741 (PubMed:2592361).Curated1
Sequence conflicti55I → M in AAA35741 (PubMed:2592361).Curated1
Sequence conflicti119Y → I in AAA35741 (PubMed:2592361).Curated1
Sequence conflicti249S → R in CAA38539 (PubMed:2256920).Curated1
Sequence conflicti342Q → K in AAA35741 (PubMed:2592361).Curated1
Sequence conflicti438F → L in AAA35741 (PubMed:2592361).Curated1
Sequence conflicti470H → R in AAA35741 (PubMed:2592361).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01415129A → T.1 PublicationCorresponds to variant rs6438dbSNPEnsembl.1
Natural variantiVAR_01415230R → Q.1 PublicationCorresponds to variant rs6441dbSNPEnsembl.1
Natural variantiVAR_018470140N → NRL in CMO-1 deficiency; the enzyme is inactive. 1
Natural variantiVAR_001266173K → R.3 PublicationsCorresponds to variant rs4539dbSNPEnsembl.1
Natural variantiVAR_001267181R → W in CMO-2 deficiency; reduces 18-hydroxylase and abolishes 18-oxidase activities; leaves 11 beta-hydroxylase activity intact. 2 PublicationsCorresponds to variant rs28931609dbSNPEnsembl.1
Natural variantiVAR_018471185T → I in CMO-2 deficiency. 2 PublicationsCorresponds to variant rs121912978dbSNPEnsembl.1
Natural variantiVAR_001268198E → D in CMO-2 deficiency. 1 PublicationCorresponds to variant rs104894072dbSNPEnsembl.1
Natural variantiVAR_014643222N → T.Corresponds to variant rs5308dbSNPEnsembl.1
Natural variantiVAR_014153248I → T.2 PublicationsCorresponds to variant rs4547dbSNPEnsembl.1
Natural variantiVAR_014154281N → S.2 PublicationsCorresponds to variant rs4537dbSNPEnsembl.1
Natural variantiVAR_014155339I → T.2 PublicationsCorresponds to variant rs4544dbSNPEnsembl.1
Natural variantiVAR_014644383E → V.Corresponds to variant rs5312dbSNPEnsembl.1
Natural variantiVAR_001269386V → A in CMO-2 deficiency; small but consistent reduction in the production of 18-hydroxycorticosterone. 5 PublicationsCorresponds to variant rs61757294dbSNPEnsembl.1
Natural variantiVAR_014645403V → E.Corresponds to variant rs5315dbSNPEnsembl.1
Natural variantiVAR_014156435G → S.2 PublicationsCorresponds to variant rs4545dbSNPEnsembl.1
Natural variantiVAR_018472461L → P in CMO-1 deficiency; abolishes the 18-hydroxylase activity required for conversion of 11-deoxycorticosterone to aldosterone. 1 PublicationCorresponds to variant rs72554627dbSNPEnsembl.1
Natural variantiVAR_014646487F → V.Corresponds to variant rs5317dbSNPEnsembl.1
Natural variantiVAR_018473498T → A in CMO-2 deficiency. 1 PublicationCorresponds to variant rs72554626dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6393.1.
PIRiB34181.
RefSeqiNP_000489.3. NM_000498.3.
UniGeneiHs.632054.

Genome annotation databases

EnsembliENST00000323110; ENSP00000325822; ENSG00000179142.
GeneIDi1585.
KEGGihsa:1585.
UCSCiuc003yxk.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

CYP11B2 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6393.1.
PIRiB34181.
RefSeqiNP_000489.3. NM_000498.3.
UniGeneiHs.632054.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4DVQX-ray2.49A/B/C/D/E/F/G/H/I/J/K/L34-503[»]
4FDHX-ray2.71A/B/C/D/E/F/G/H/I/J/K/L34-503[»]
4ZGXX-ray3.20A/B/C/D/E/F/G/H/I/J/K/L28-503[»]
ProteinModelPortaliP19099.
SMRiP19099.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107957. 1 interactor.
STRINGi9606.ENSP00000325822.

Chemistry databases

BindingDBiP19099.
ChEMBLiCHEMBL2722.
DrugBankiDB00700. Eplerenone.
DB00292. Etomidate.
DB00741. Hydrocortisone.
DB01233. Metoclopramide.
DB01011. Metyrapone.
DB00421. Spironolactone.
GuidetoPHARMACOLOGYi1360.
SwissLipidsiSLP:000001198.

PTM databases

iPTMnetiP19099.
PhosphoSitePlusiP19099.

Polymorphism and mutation databases

BioMutaiCYP11B2.
DMDMi3041666.

Proteomic databases

PaxDbiP19099.
PeptideAtlasiP19099.
PRIDEiP19099.

Protocols and materials databases

DNASUi1585.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000323110; ENSP00000325822; ENSG00000179142.
GeneIDi1585.
KEGGihsa:1585.
UCSCiuc003yxk.1. human.

Organism-specific databases

CTDi1585.
DisGeNETi1585.
GeneCardsiCYP11B2.
H-InvDBHIX0034383.
HGNCiHGNC:2592. CYP11B2.
HPAiHPA049171.
HPA056348.
HPA057752.
MalaCardsiCYP11B2.
MIMi103900. phenotype.
124080. gene.
203400. phenotype.
610600. phenotype.
neXtProtiNX_P19099.
OpenTargetsiENSG00000179142.
Orphaneti403. Familial hyperaldosteronism type I.
99763. Familial hyperreninemic hypoaldosteronism type 1.
PharmGKBiPA134.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0159. Eukaryota.
COG2124. LUCA.
GeneTreeiENSGT00760000119243.
HOGENOMiHOG000013161.
HOVERGENiHBG051098.
InParanoidiP19099.
KOiK07433.
OMAiPFEAMPQ.
OrthoDBiEOG091G0B8F.
PhylomeDBiP19099.
TreeFamiTF105094.

Enzyme and pathway databases

BioCyciMetaCyc:HS11355-MONOMER.
ZFISH:HS11355-MONOMER.
BRENDAi1.14.15.4. 2681.
ReactomeiR-HSA-193993. Mineralocorticoid biosynthesis.
R-HSA-194002. Glucocorticoid biosynthesis.
R-HSA-211976. Endogenous sterols.

Miscellaneous databases

GeneWikiiAldosterone_synthase.
GenomeRNAii1585.
PROiP19099.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000179142.
CleanExiHS_CYP11B2.
GenevisibleiP19099. HS.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002399. Cyt_P450_mitochondrial.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00408. MITP450.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiC11B2_HUMAN
AccessioniPrimary (citable) accession number: P19099
Secondary accession number(s): B0ZBE4, Q16726
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: July 15, 1998
Last modified: November 30, 2016
This is version 182 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.