Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P22443 (CP19A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aromatase

EC=1.14.14.14
Alternative name(s):
CYPXIX
Cytochrome P-450AROM
Cytochrome P450 19A1
Estrogen synthase
Gene names
Name:Cyp19a1
Synonyms:Arom, Cyp19
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length508 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the formation of aromatic C18 estrogens from C19 androgens.

Catalytic activity

Testosterone + 3 O2 + 3 reduced flavoproteins = 17-beta-estradiol + formate + 4 H2O + 3 oxidized flavoproteins.

Androst-4-ene-3,17-dione + 3 O2 + 3 reduced flavoproteins = estrone + formate + 4 H2O + 3 oxidized flavoproteins.

Cofactor

Heme group By similarity.

Subcellular location

Membrane; Peripheral membrane protein.

Sequence similarities

Belongs to the cytochrome P450 family.

Ontologies

Keywords
   Cellular componentMembrane
   LigandHeme
Iron
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processC21-steroid hormone metabolic process

Inferred from direct assay PubMed 19190754. Source: RGD

adrenal gland development

Inferred from expression pattern PubMed 8097866. Source: RGD

androgen metabolic process

Inferred from mutant phenotype PubMed 19492405. Source: RGD

bile acid metabolic process

Inferred from expression pattern PubMed 20026603. Source: RGD

biphenyl metabolic process

Inferred from expression pattern PubMed 19464308. Source: RGD

bone development

Inferred from expression pattern PubMed 15012600. Source: RGD

cellular response to fibroblast growth factor stimulus

Inferred from expression pattern PubMed 20434519. Source: RGD

cellular response to follicle-stimulating hormone stimulus

Inferred from expression pattern PubMed 20810564. Source: RGD

cellular response to glucose stimulus

Inferred from expression pattern PubMed 18353182. Source: RGD

cellular response to gonadotropin stimulus

Inferred from expression pattern PubMed 16569475. Source: RGD

cellular response to hydrostatic pressure

Inferred from expression pattern PubMed 21047944. Source: RGD

dibenzo-p-dioxin metabolic process

Inferred from expression pattern PubMed 20059580. Source: RGD

estrogen biosynthetic process

Inferred from direct assay PubMed 19665544. Source: RGD

granulocyte differentiation

Inferred from expression pattern PubMed 18401763. Source: RGD

hippocampus development

Inferred from expression pattern PubMed 21047951. Source: RGD

hypothalamus development

Inferred from expression pattern PubMed 15804399. Source: RGD

luteinization

Inferred from expression pattern PubMed 23183184. Source: RGD

male gonad development

Inferred from expression pattern PubMed 20554652. Source: RGD

melatonin metabolic process

Inferred from expression pattern PubMed 17700567. Source: RGD

negative regulation of bone resorption

Inferred from mutant phenotype PubMed 8694895. Source: RGD

phthalate metabolic process

Inferred from expression pattern PubMed 20920559. Source: RGD

progesterone metabolic process

Inferred from expression pattern PubMed 20810564. Source: RGD

regulation of synapse structure and activity

Inferred from mutant phenotype PubMed 17005180. Source: RGD

response to cesium ion

Inferred from expression pattern PubMed 20451883. Source: RGD

response to drug

Inferred from expression pattern PubMed 19497980. Source: RGD

response to estradiol

Inferred from expression pattern PubMed 21115103. Source: RGD

response to estrogen

Inferred from expression pattern PubMed 19734697. Source: RGD

response to herbicide

Inferred from expression pattern PubMed 21126571. Source: RGD

response to ionizing radiation

Inferred from expression pattern PubMed 18821396. Source: RGD

response to metal ion

Inferred from expression pattern PubMed 20708649. Source: RGD

response to morphine

Inferred from expression pattern PubMed 20977699. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 20821433. Source: RGD

response to testosterone

Inferred from expression pattern PubMed 16569475. Source: RGD

   Cellular_componentaxon terminus

Inferred from direct assay PubMed 14694190. Source: RGD

cytoplasm

Inferred from direct assay PubMed 14694190. Source: RGD

cytosol

Inferred from direct assay PubMed 21114983. Source: RGD

dendritic spine

Inferred from direct assay PubMed 14694190. Source: RGD

endoplasmic reticulum

Inferred from direct assay PubMed 14694190. Source: RGD

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuronal cell body

Inferred from direct assay PubMed 19565659. Source: RGD

synapse

Inferred from direct assay PubMed 20926671. Source: RGD

synaptic vesicle

Inferred from direct assay PubMed 14694190. Source: RGD

terminal bouton

Inferred from direct assay PubMed 20926671. Source: RGD

   Molecular_functionaromatase activity

Inferred from direct assay PubMed 16269516. Source: RGD

heme binding

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: InterPro

oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen

Inferred from direct assay PubMed 11850226. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 508508Aromatase
PRO_0000051962

Sites

Metal binding4371Iron (heme axial ligand)

Experimental info

Sequence conflict3 – 42LE → FQ no nucleotide entry Ref.2
Sequence conflict101H → Q no nucleotide entry Ref.2
Sequence conflict881W → C no nucleotide entry Ref.2
Sequence conflict1011S → L no nucleotide entry Ref.2
Sequence conflict123 – 1297QCIGMHE → VVHGHAR no nucleotide entry Ref.2
Sequence conflict1881V → L no nucleotide entry Ref.2
Sequence conflict2101E → G no nucleotide entry Ref.2
Sequence conflict328 – 3314VETA → WKQ no nucleotide entry Ref.2
Sequence conflict3421D → A no nucleotide entry Ref.2
Sequence conflict364 – 3696LRYQPV → CGISPF no nucleotide entry Ref.2
Sequence conflict4221V → L no nucleotide entry Ref.2
Sequence conflict4251R → T no nucleotide entry Ref.2
Sequence conflict4491V → I no nucleotide entry Ref.2
Sequence conflict4661R → K no nucleotide entry Ref.2
Sequence conflict493 – 4975RHIFN → SPRNS no nucleotide entry Ref.2

Sequences

Sequence LengthMass (Da)Tools
P22443 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: C0ADFB0FD80AB352

FASTA50858,412
        10         20         30         40         50         60 
MFLEMLNPMH YNVTIMVPET VPVSAMPLLL IMGLLLLIRN CESSSSIPGP GYCLGIGPLI 

        70         80         90        100        110        120 
SHGRFLWMGI GSACNYYNKM YGEFMRVWIS GEETLIISKS SSMVHVMKHS NYISRFGSKR 

       130        140        150        160        170        180 
GLQCIGMHEN GIIFNNNPSL WRTVRPFFMK ALTGPGLIRM VEVCVESIKQ HLDRLGDVTD 

       190        200        210        220        230        240 
NSGYVDVVTL MRHIMLDTSN TLFLGIPLDE SSIVKKIQGY FNAWQALLIK PNIFFKISWL 

       250        260        270        280        290        300 
YRKYERSVKD LKDEIEILVE KKRQKVSSAE KLEDCMDFAT DLIFAERRGD LTKENVNQCI 

       310        320        330        340        350        360 
LEMLIAAPDT MSVTLYVMLL LIAEYPEVET AILKEIHTVV GDRDIRIGDV QNLKVVENFI 

       370        380        390        400        410        420 
NESLRYQPVV DLVMRRALED DVIDGYPVKK GTNIILNIGR MHRLEYFPKP NEFTLENFEK 

       430        440        450        460        470        480 
NVPYRYFQPF GFGPRSCAGK YIAMVMMKVV LVTLLKRFHV KTLQKRCIEN MPKNNDLSLH 

       490        500 
LDEDSPIVEI IFRHIFNTPF LQCLYISL 

« Hide

References

[1]"Aromatase cytochrome P450 in rat ovarian granulosa cells before and after luteinization: adenosine 3',5'-monophosphate-dependent and independent regulation. Cloning and sequencing of rat aromatase cDNA and 5' genomic DNA."
Hickey G.J., Krasnow J.S., Beattie W.G., Richards J.S.
Mol. Endocrinol. 4:3-12(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Ovary.
[2]"The structure of cDNA clones encoding the aromatase P-450 isolated from a rat Leydig cell tumor line demonstrates differential processing of aromatase mRNA in rat ovary and a neoplastic cell line."
Lephart E.D., Peterson K.G., Noble J.F., George F.W., McPhaul M.J.
Mol. Cell. Endocrinol. 70:31-40(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M33986 mRNA. Translation: AAA41044.1.
PIRA36121.
UniGeneRn.21402.

3D structure databases

ProteinModelPortalP22443.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000000212.

Chemistry

BindingDBP22443.
ChEMBLCHEMBL3859.

Proteomic databases

PaxDbP22443.
PRIDEP22443.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

RGD2457. Cyp19a1.

Phylogenomic databases

eggNOGCOG2124.
HOGENOMHOG000111912.
HOVERGENHBG050750.
PhylomeDBP22443.

Gene expression databases

GenevestigatorP22443.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR00385. P450.
SUPFAMSSF48264. SSF48264. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP22443.

Entry information

Entry nameCP19A_RAT
AccessionPrimary (citable) accession number: P22443
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: July 9, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families