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O57525 (CP17A_RANDY) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 79. 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
OrganismRana dybowskii (Dybovsky's frog) (Korean brown frog)
Taxonomic identifier71582 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaRanoideaRanidaeRanaRana

Protein attributes

Sequence length519 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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.

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.

Ontologies

Keywords
   Biological processSteroidogenesis
   Cellular componentMembrane
   LigandHeme
Iron
Metal-binding
   Molecular functionLyase
Monooxygenase
Oxidoreductase
Gene Ontology (GO)
   Biological_processsteroid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmembrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function17-alpha-hydroxyprogesterone aldolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

heme binding

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: InterPro

steroid 17-alpha-monooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 519519Steroid 17-alpha-hydroxylase/17,20 lyase
PRO_0000051948

Sites

Metal binding4551Iron (heme axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
O57525 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: FDF866CF15593A2E

FASTA51958,948
        10         20         30         40         50         60 
MKLCFFLLIF IRSFLLFKIK LVRTSEKKWR MGSRSHGDVK HPKSLPSLPV IGSLLHLGKK 

        70         80         90        100        110        120 
LPPHILFCNL QKKYGSLYSF MMGSHYVVVV NNHEDAREVL LKKGKTFGGR PRTVTTDILT 

       130        140        150        160        170        180 
RDGKDIAFAD YSPTWKFHRK MVHSALCMFG EGTVAIEQII SREAASLCQT LTSFQRIPLD 

       190        200        210        220        230        240 
MAPELIRAVT NVVCSLCFNT RYKRGDAEFE TMLKYSKGIV DTVAKDSLVD IFPWLQIFPN 

       250        260        270        280        290        300 
KDLDILRQSV AARDQLLQKK INEHKDAFCG ETVKDLVDAL LKAKLNMENN NSNVSQDVGL 

       310        320        330        340        350        360 
TEDHILMTVG DIFGAGVETT STVLKWAVAY LLHYPEVQKK IQEELDVKVG FGRYPLLSDR 

       370        380        390        400        410        420 
KILHYTEAAI SEVLRIRPVS PLLIPHVALK ESSIGEYTIP KEARVVINLW SLHHDEKEWV 

       430        440        450        460        470        480 
NPHLFSPDRF LDENGNRVYS PSPSFLPFGA GIRVCLGEAL AKMEVFLFLS WILQRFTLEV 

       490        500        510 
PEGDPLPDLE GKFGVVIQVK PFKVIAKLRE VWKNIEIVT 

« Hide

References

[1]"Cloning and characterization of cDNA encoding 17-alpha-hydroxylase/17,20 lyase (P450c17) in amphibia (Rana dybowskii)."
Choi H.H., Kang H.M., Choi H.S., Kwon H.B.
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF042278 mRNA. Translation: AAB97686.1.

3D structure databases

ProteinModelPortalO57525.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG106944.

Enzyme and pathway databases

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_RANDY
AccessionPrimary (citable) accession number: O57525
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: December 11, 2013
This is version 79 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