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Q64410 (CP17A_CAVPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. 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
OrganismCavia porcellus (Guinea pig) [Reference proteome]
Taxonomic identifier10141 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia

Protein attributes

Sequence length508 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.

Pathway

Lipid metabolism; steroid biosynthesis.

Subcellular location

Membrane Potential.

Sequence similarities

Belongs to the cytochrome P450 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 508508Steroid 17-alpha-hydroxylase/17,20 lyase
PRO_0000051928

Sites

Metal binding4421Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict621P → S in AAB33048. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q64410 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 5F7D6EBFB5B5CC8E

FASTA50857,026
        10         20         30         40         50         60 
MWELVTLLGL ILAYLFWPRQ GSSGTKYPKS LPSLPVVGSL PFLPKSGHMH VNFFKLQKKY 

        70         80         90        100        110        120 
GPIYSFRLGS TTTVVIGHHQ LARELLIKKG KEFSGRPLTT TVALLSDNGK GIAFADSSAT 

       130        140        150        160        170        180 
WQLHRRLVLS SFSLFRDGEQ KLENIICQEL SALCDFLATC DGQVKDLSSS IFMTVVNIIC 

       190        200        210        220        230        240 
MICFSVSYKE GDMELVTIRR FTTGFVNSLS DDNLVDIFPW LKIFPNKTLE MIRKYTEIRG 

       250        260        270        280        290        300 
AMLSKILKEC KEKFRSDSVS NLIDLLIQAK VNENNNNSSL DQDSNLFSDK HILTTLGDIF 

       310        320        330        340        350        360 
GAGVETSSSV VLWVIAFLLH NPQVKKKIQE EIDHNVGFSR TPTFSDRNHL LMLEATIREV 

       370        380        390        400        410        420 
LRIRPVAPIL IPHKANTDSS IGEFAIDKDT NVLVNLWALH HNEQEWDRPD QFMPERFLDP 

       430        440        450        460        470        480 
TGSQIIVPSS SYLPFGAGPR SCVGEALARQ EIFLITAWLL QKFDLEVPEG GQLPSLEGIP 

       490        500 
KIVFLIDPFK VKITVRPAWK EAQAEGSA 

« Hide

References

[1]"cDNA cloning of guinea pig adrenal CYP17."
Huang Y., Voigt J.M., Colby H.D.
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: English short hair.
Tissue: Adrenal cortex.
[2]"Molecular cloning and expression of guinea pig cytochrome P450c17 cDNA (steroid 17 alpha-hydroxylase/17,20 lyase): tissue distribution, regulation, and substrate specificity of the expressed enzyme."
Tremblay Y., Fleury A., Beaudoin C., Vallee M., Belanger A.
DNA Cell Biol. 13:1199-1212(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Adrenal gland.
[3]"Partial amino acid sequences of two mitochondrial and two microsomal cytochrome P-450's from adrenal cortex."
Ogishima T., Okada Y., Kominami S., Takemori S., Omura T.
J. Biochem. 94:1711-1714(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-15.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X82878 Genomic DNA. Translation: CAA58059.1.
S75277 mRNA. Translation: AAB33048.1.
PIRI53018.
S52756.
RefSeqXP_003475015.1. XM_003474967.1.

3D structure databases

ProteinModelPortalQ64410.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10141.ENSCPOP00000013107.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSCPOT00000014691; ENSCPOP00000013107; ENSCPOG00000014546.
GeneID100729670.

Phylogenomic databases

eggNOGCOG2124.
GeneTreeENSGT00750000117317.
HOGENOMHOG000036991.
HOVERGENHBG106944.
InParanoidQ64410.
OrthoDBEOG7RBZ85.
TreeFamTF105095.

Enzyme and pathway databases

BRENDA1.14.99.9. 1225.
UniPathwayUPA00062.

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...

Entry information

Entry nameCP17A_CAVPO
AccessionPrimary (citable) accession number: Q64410
Secondary accession number(s): Q64659
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 96 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

PATHWAY comments

Index of metabolic and biosynthesis pathways