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Reviewed, UniProtKB/Swiss-Prot P70687 (CP17A_MESAU)

Last modified October 13, 2009. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

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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
OrganismMesocricetus auratus (Golden hamster)
Taxonomic identifier10036 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Mesocricetus

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Protein attributes

Sequence length511 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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

Cofactor

Heme group By similarity.

Enzyme regulation

Regulated predominantly by intracellular cAMP levels By similarity.

Pathway

Lipid metabolism; steroid biosynthesis.

Subcellular location

Membrane Potential. Membrane; Single-pass membrane protein.

Sequence similarities

Belongs to the cytochrome P450 family.

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Ontologies

Keywords
   Biological processSteroidogenesis
   Cellular componentMembrane
   LigandHeme
Iron
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   Technical term3D-structure
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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 511511Steroid 17-alpha-hydroxylase/17,20 lyase
PRO_0000051934

Sites

Metal binding4421Iron (heme axial ligand) By similarity

Secondary structure

1 ....................................................................................... 511
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P70687-1 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 896E776A7457546C

FASTA51157,459
        10         20         30         40         50         60 
MWELVALLLL TLAYFFWSKS KTCGAKSPKS LPFLPLVGSL PFIPRHGHPH VNFFKLQEKY 

        70         80         90        100        110        120 
GPIYSLRLGS TTTVIIGQYQ LAKEVLVKKG KEFSGRPHMV TLGLLSDQGK GIAFADSGGS 

       130        140        150        160        170        180 
WQLHRKLALS SFALFRDGNQ KLEKIICQKA SSLCDFLLTH NEESIDLSEP IFNSITNIIC 

       190        200        210        220        230        240 
IICFGISYEN RDPILATIKS FTEGILNSLG NDHLVDIFPW LTIFPNKTVD MIKKNVKIRD 

       250        260        270        280        290        300 
EVLSGILEKC KEKFNSDSIS SLMDLLIQAK TNADNNNTSE GQGSNAFSDM HILATIADIF 

       310        320        330        340        350        360 
GAGIETTASV LSWIIAFLLH NPEVKKKIQK EIDQNIGFSR TPTFNDRNHL LMLEATIREV 

       370        380        390        400        410        420 
LRIRPVAPML IPHRANSDMS IGEFSIPKFT PVIINLWALH HSEKEWDQPD RFMPERFLDP 

       430        440        450        460        470        480 
TGSHLITPSL SYLPFGAGAR SCIGEVLARQ ELFLFMAHLL QRFDLDVPDD EQPPCLKGNA 

       490        500        510 
NVVFLIDPFK VKITVRQAWK DAQAEVNTWR P

« Hide

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References

[1]"Cloning and expression of hamster adrenal cytochrome P450C17 cDNA."
Cloutier M., Fleury A., Courtemanche J., Ducharme L., Mason J.I., Lehoux J.-G.
Ann. N. Y. Acad. Sci. 774:294-296(1995) [PubMed: 8597469] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Adrenal gland.

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Cross-references

Sequence databases

U66494 mRNA. Translation: AAB07494.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1JO9model-A48-501[»]
ModBaseSearch...

Phylogenomic databases

HOVERGENP70687.

Enzyme and pathway databases

BRENDA1.14.99.9. 824.

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...

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Entry information

Entry nameCP17A_MESAU
AccessionPrimary (citable) accession number: P70687
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: October 13, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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