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Reviewed, UniProtKB/Swiss-Prot Q9N0U7 (CP17A_CAPHI)

Last modified January 19, 2010. Version 45. 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
    Cytochrome P450-C17
      Short name=Cytochrome P450c17
Gene names
Name: CYP17A1
Synonyms: CYP17
OrganismCapra hircus (Goat)
Taxonomic identifier9925 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeCapra

Protein attributes

Sequence length509 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. Involved in sexual development during fetal life and at puberty 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 – 509509Steroid 17-alpha-hydroxylase/17,20 lyase
PRO_0000051927

Sites

Metal binding4421Iron (heme axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9N0U7-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: A3C77300622A2EA6

FASTA50957,298
        10         20         30         40         50         60 
MWVLLGVFLL TLAYLFWPKT KHSAAKYPRS LPSLPLVGSL LFLPRRGQQH ENFFKLQEKY 

        70         80         90        100        110        120 
GPIYSFRLGS KTTVMIGHHQ LAREVLLKKG KEFSGRPKVA TLDILSDNQK GIAFADHGAH 

       130        140        150        160        170        180 
WQLHRKLVLN AFALFKDGNL KLEKIINQEA NVLCDFLATQ HGQSIDLSEP LSLAVTNIIS 

       190        200        210        220        230        240 
FICFNFSFKN EDPALKAIQN VNDGILEVLS KEILLDIFPA LKIFPSKAME KMKGCVETRN 

       250        260        270        280        290        300 
ELLNEILEKC QENFTSDSIT NLLHILMQAK VNADNNNAGP DQDSKLLSNR HMLATIADIF 

       310        320        330        340        350        360 
GAGVETTTSV IKWIVAYLLH HPSLKKRIQD SIDQNIGFNR TPTISDRNCL VLLEATIREV 

       370        380        390        400        410        420 
LRIRPVAPML IPHKAIIDSS IGDLTIDKGT DVVVNLWALH HNEKEWQQPD LFMPERFLDP 

       430        440        450        460        470        480 
TGTQLISPSL SYLPFGAGPR SCVGEMLARQ ELFLFMSRLL QRFNLEIPDD GKLPSLEGNP 

       490        500 
SLVLQIKPFK VKIEVRQAWK EAQAEGSTS 

« Hide

References

[1]"Molecular cloning and heterologous expression in E. coli of cytochrome P45017alpha. Comparison of structural and functional properties of substrate-specific cytochromes P450 from different species."
Gilep A.A., Estabrook R.W., Usanov S.A.
Biokhimiia 68:86-98(2003) [PubMed: 12693981] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Adrenal gland.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF251387 mRNA. Translation: AAF65823.1.

3D structure databases

SMRQ9N0U7. Positions 26-492.
ModBaseSearch...

Phylogenomic databases

HOVERGENQ9N0U7.

Enzyme and pathway databases

BRENDA1.14.99.9. 1312.

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_CAPHI
AccessionPrimary (citable) accession number: Q9N0U7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: October 1, 2000
Last modified: January 19, 2010
This is version 45 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