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P11715 (CP17A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Steroid 17-alpha-hydroxylase/17,20 lyase

EC=1.14.99.9
EC=4.1.2.30
Alternative name(s):
17-alpha-hydroxyprogesterone aldolase
CYPXVII
Cytochrome P450 17A1
Cytochrome P450-C17
Short name=Cytochrome P450c17
Gene names
Name:Cyp17a1
Synonyms:Cyp17
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length507 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione. Catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reaction. Involved in sexual development during fetal life and at puberty.

Catalytic activity

A C(21)-steroid + (reduced NADPH--hemoprotein reductase) + O2 = a 17-alpha-hydroxy-C(21)-steroid + (oxidized NADPH--hemoprotein reductase) + H2O.

17-alpha-hydroxyprogesterone = androst-4-ene-3,17-dione + acetaldehyde.

Cofactor

Heme group By similarity.

Enzyme regulation

Regulated predominantly by intracellular cAMP levels.

Pathway

Lipid metabolism; steroid biosynthesis.

Subcellular location

Membrane Potential.

Sequence similarities

Belongs to the cytochrome P450 family.

Ontologies

Keywords
   Biological processSteroidogenesis
   Cellular componentMembrane
   LigandHeme
Iron
Metal-binding
   Molecular functionLyase
Monooxygenase
Oxidoreductase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processLeydig cell differentiation

Inferred from expression pattern PubMed 18502897. Source: RGD

adrenal gland development

Inferred from expression pattern PubMed 17065412. Source: RGD

androgen biosynthetic process

Traceable author statement Ref.3. Source: RGD

biphenyl metabolic process

Inferred from expression pattern PubMed 20356859. Source: RGD

cellular response to antibiotic

Inferred from expression pattern PubMed 18655822. Source: RGD

cellular response to gonadotropin stimulus

Inferred from expression pattern PubMed 20963569. Source: RGD

cellular response to lipopolysaccharide

Inferred from expression pattern PubMed 20665543. Source: RGD

dibenzo-p-dioxin metabolic process

Inferred from expression pattern PubMed 20059580. Source: RGD

glucocorticoid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

hippocampus development

Inferred from expression pattern PubMed 21047951. Source: RGD

hormone biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

male gonad development

Inferred from expression pattern PubMed 10822021. Source: RGD

organic acid metabolic process

Inferred from expression pattern PubMed 17400581. Source: RGD

ovulation

Inferred from expression pattern PubMed 19775733. Source: RGD

phenol-containing compound metabolic process

Inferred from expression pattern PubMed 18191889. Source: RGD

phthalate metabolic process

Inferred from expression pattern PubMed 16809437. Source: RGD

positive regulation of steroid hormone biosynthetic process

Inferred from mutant phenotype PubMed 19615041. Source: RGD

progesterone metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

response to acetate

Inferred from expression pattern PubMed 21046364. Source: RGD

response to cAMP

Inferred from expression pattern PubMed 17291543. Source: RGD

response to cytokine

Inferred from expression pattern PubMed 15958400. Source: RGD

response to drug

Inferred from expression pattern PubMed 19603415. Source: RGD

response to fungicide

Inferred from expression pattern PubMed 16214947PubMed 17369198. Source: RGD

response to gonadotropin

Inferred from expression pattern PubMed 17291543. Source: RGD

response to herbicide

Inferred from expression pattern PubMed 20667998. Source: RGD

response to insecticide

Inferred from expression pattern PubMed 17569032. Source: RGD

response to ionizing radiation

Inferred from expression pattern PubMed 18821396. Source: RGD

response to methylmercury

Inferred from expression pattern PubMed 17869401. Source: RGD

response to nutrient levels

Inferred from expression pattern PubMed 17936465PubMed 19389810. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 18923996. Source: RGD

response to organic substance

Inferred from expression pattern PubMed 18804513. Source: RGD

response to retinoic acid

Inferred from expression pattern PubMed 19497980. Source: RGD

response to steroid hormone

Inferred from expression pattern PubMed 19961867. Source: RGD

response to toxic substance

Inferred from expression pattern PubMed 17291543. Source: RGD

steroid biosynthetic process

Inferred from mutant phenotype Ref.1. Source: RGD

steroid metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentaxon

Inferred from electronic annotation. Source: Ensembl

cell projection

Inferred from direct assay PubMed 15934942. Source: RGD

endoplasmic reticulum

Inferred from direct assay PubMed 11691658. Source: RGD

intracellular membrane-bounded organelle

Inferred from direct assay PubMed 17936465. Source: RGD

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from direct assay PubMed 15934942. Source: RGD

   Molecular_function17-alpha-hydroxyprogesterone aldolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

heme binding

Inferred from sequence or structural similarity. Source: UniProtKB

iron ion binding

Inferred from electronic annotation. Source: InterPro

steroid 17-alpha-monooxygenase activity

Inferred from direct assay Ref.1. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 507507Steroid 17-alpha-hydroxylase/17,20 lyase
PRO_0000051941

Sites

Metal binding4411Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict1901N → K in AAH78898. Ref.4
Sequence conflict505 – 5062VS → LT in AAA41050. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P11715 [UniParc].

Last modified August 1, 1990. Version 2.
Checksum: A535600F7E6A399B

FASTA50757,250
        10         20         30         40         50         60 
MWELVGLLLL ILAYFFWVKS KTPGAKLPRS LPSLPLVGSL PFLPRRGHMH VNFFKLQEKY 

        70         80         90        100        110        120 
GPIYSLRLGT TTTVIIGHYQ LAREVLIKKG KEFSGRPQMV TQSLLSDQGK GVAFADAGSS 

       130        140        150        160        170        180 
WHLHRKLVFS TFSLFKDGQK LEKLICQEAK SLCDMMLAHD KESIDLSTPI FMSVTNIICA 

       190        200        210        220        230        240 
ICFNISYEKN DPKLTAIKTF TEGIVDATGD RNLVDIFPWL TIFPNKGLEV IKGYAKVRNE 

       250        260        270        280        290        300 
VLTGIFEKCR EKFDSQSISS LTDILIQAKM NSDNNNSCEG RDPDVFSDRH ILATVGDIFG 

       310        320        330        340        350        360 
AGIETTTTVL KWILAFLVHN PEVKKKIQKE IDQYVGFSRT PTFNDRSHLL MLEATIREVL 

       370        380        390        400        410        420 
RIRPVAPMLI PHKANVDSSI GEFTVPKDTH VVVNLWALHH DENEWDQPDQ FMPERFLDPT 

       430        440        450        460        470        480 
GSHLITPTQS YLPFGAGPRS CIGEALARQE LFVFTALLLQ RFDLDVSDDK QLPRLEGDPK 

       490        500 
VVFLIDPFKV KITVRQAWMD AQAEVST 

« Hide

References

« Hide 'large scale' references
[1]"Rat P450(17 alpha) from testis: characterization of a full-length cDNA encoding a unique steroid hydroxylase capable of catalyzing both delta 4- and delta 5-steroid-17,20-lyase reactions."
Fevold H.R., Lorence M.C., McCarthy J.L., Trant J.M., Kagimoto M., Waterman M.R., Mason J.I.
Mol. Endocrinol. 3:968-975(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]"Rat testis P-450(17)alpha cDNA: the deduced amino acid sequence, expression and secondary structural configuration."
Namiki M., Kitamura M., Buczko E., Dufau M.L.
Biochem. Biophys. Res. Commun. 157:705-712(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Tissue: Testis.
[3]"Transcriptional regulation of rat cytochrome P450c17 expression in mouse Leydig MA-10 and adrenal Y-1 cells: identification of a single protein that mediates both basal and cAMP-induced activities."
Givens C.R., Zhang P., Bair S.R., Mellon S.H.
DNA Cell Biol. 13:1087-1098(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Sprague-Dawley.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[5]"Gene for 17 alpha-hydroxylase/C (17-20) lyase P-450: complete nucleotide sequence of the porcine gene and 5' upstream sequence of the rat gene."
Zhang P., Nason T.F., Han X.G., Hall P.F.
Biochim. Biophys. Acta 1131:345-348(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-97.
[6]"Hormonal regulation of rat Leydig cell cytochrome P-45017 alpha mRNA levels and characterization of a partial length rat P-45017 alpha cDNA."
Nishihara M., Winters C.A., Buzko E., Waterman M.R., Dufau M.L.
Biochem. Biophys. Res. Commun. 154:151-158(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 271-507.
[7]"cAMP regulates P450scc gene expression by a cycloheximide-insensitive mechanism in cultured mouse Leydig MA-10 cells."
Mellon S.H., Vaisse C.
Proc. Natl. Acad. Sci. U.S.A. 86:7775-7779(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 273-507.
[8]"Purification and characterization of six cytochromes P-450 from hepatic microsomes of immature female rats."
Imaoka S., Kamataki T., Funae Y.
J. Biochem. 102:843-851(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-16.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14086 mRNA. Translation: CAA32248.1.
X69816 Genomic DNA. Translation: CAA49470.1.
M31681 mRNA. Translation: AAA41777.1.
M22204 mRNA. Translation: AAA41783.1.
BC078898 mRNA. Translation: AAH78898.1.
Z11902 Genomic DNA. Translation: CAA77954.1.
M21208 mRNA. Translation: AAA41050.1.
M27282 mRNA. Translation: AAA41779.1.
PIRA30828. A31359.
RefSeqNP_036885.1. NM_012753.2.
XP_006231496.1. XM_006231434.1.
XP_006231497.1. XM_006231435.1.
UniGeneRn.10172.

3D structure databases

ProteinModelPortalP11715.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4566010.

Chemistry

BindingDBP11715.
ChEMBLCHEMBL4430.

PTM databases

PhosphoSiteP11715.

Proteomic databases

PaxDbP11715.
PRIDEP11715.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000027160; ENSRNOP00000027160; ENSRNOG00000020035.
GeneID25146.
KEGGrno:25146.
UCSCRGD:2456. rat.

Organism-specific databases

CTD1586.
RGD2456. Cyp17a1.

Phylogenomic databases

eggNOGCOG2124.
GeneTreeENSGT00750000117317.
HOGENOMHOG000036991.
HOVERGENHBG106944.
InParanoidP11715.
KOK00512.
OrthoDBEOG7RBZ85.
PhylomeDBP11715.
TreeFamTF105095.

Enzyme and pathway databases

UniPathwayUPA00062.

Gene expression databases

GenevestigatorP11715.

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

NextBio605573.
PROP11715.

Entry information

Entry nameCP17A_RAT
AccessionPrimary (citable) accession number: P11715
Secondary accession number(s): Q68FY2, Q6LAE5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: August 1, 1990
Last modified: April 16, 2014
This is version 132 of the entry and version 2 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

PATHWAY comments

Index of metabolic and biosynthesis pathways