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Reviewed, UniProtKB/Swiss-Prot Q8HYN0 (CP17A_PAPCY)

Last modified October 13, 2009. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Steroid 17-alpha-hydroxylase/17,20 lyase
    EC=1.14.99.9
Alternative name(s):
    Cytochrome P450 17A1
    CYPXVII
    P450-C17
      Short name=P450c17
Gene names
Name: CYP17A1
Synonyms: CYP17
OrganismPapio cynocephalus (Yellow baboon)
Taxonomic identifier9556 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaePapio

Protein attributes

Sequence length508 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 By similarity.

Catalytic activity

A steroid + AH2 + O2 = a 17-alpha-hydroxysteroid + A + H2O.

Cofactor

Heme group By similarity.

Pathway

Lipid metabolism; steroid biosynthesis.

Subcellular location

Membrane Potential. Membrane; Single-pass membrane protein.

Sequence similarities

Belongs to the cytochrome P450 family.

Ontologies

Keywords
   Biological processSteroidogenesis
   Cellular componentMembrane
   LigandHeme
Iron
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

steroid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionelectron carrier activity

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

steroid 17-alpha-monooxygenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 508508Steroid 17-alpha-hydroxylase/17,20 lyase
PRO_0000051937

Sites

Metal binding4421Iron (heme axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8HYN0-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 92DEEDDF813F7263

FASTA50857,638
        10         20         30         40         50         60 
MWELVALLLL TLAYLFWPKR RCPGAKYPKS LLSLPLVGSL PFLPRHGHMH NNFFKLQKKY 

        70         80         90        100        110        120 
GPIYSVRMGT KTTVIVGHHQ LAKEVLIKKG KDFSGRPQVT TLDILSNNRK GIAFADYGAH 

       130        140        150        160        170        180 
WQLHRRLAMA TFALFKDGDQ KLEKIICQEI STLCDMLATH NGQTIDISFP VFVAITNVIS 

       190        200        210        220        230        240 
LICFNISYKN GDPELKIVHN YNEGIIDSLG KESLVDLFPW LKVFPNKTLE KLKRHVKTRN 

       250        260        270        280        290        300 
DLLTKIFENY KEKFRSDSIT NMLDVLMQAK MNSDNGNAGP DQDSELLSDN HILTTIGDIF 

       310        320        330        340        350        360 
GAGVETTTSV VKWIVAFLLH NPQVKKKLYE EIDQNVGFSR TPTISDRNRL LLLEATIREV 

       370        380        390        400        410        420 
LRIRPVAPML IPHKANVDSS IGEFAVDKGT HVIINLWALH HNEKEWHQPD QFMPERFLNP 

       430        440        450        460        470        480 
AGTQLISPSL SYLPFGAGPR SCIGEILARQ ELFLIMAWLL QRFDLEVPDD GQLPSLEGNP 

       490        500 
KVVFLIDSFK VKIKVRQAWR EAQAEGST 

« Hide

References

[1]"Molecular evolution of adrenarche: structural and functional analysis of p450c17 from four primate species."
Arlt W., Martens J.W., Song M., Wang J.T., Auchus R.J., Miller W.L.
Endocrinology 143:4665-4672(2002) [PubMed: 12446594] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

AF458331 mRNA. Translation: AAN86252.1.

3D structure databases

HSSPHSSP built from PDB template 1DT6 based on UniProtKB P00179.
ModBaseSearch...

Phylogenomic databases

HOVERGENQ8HYN0.

Enzyme and pathway databases

BRENDA1.14.99.9. 74251.

Family and domain databases

InterProIPR001128. Cyt_P450.
IPR017973. Cyt_P450_C.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
Gene3DG3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHERPTHR19383. Cyt_P450. 1 hit.
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR00385. P450.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCP17A_PAPCY
AccessionPrimary (citable) accession number: Q8HYN0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 21, 2003
Last sequence update: March 1, 2003
Last modified: October 13, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents