Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q29497 (CP17A_SHEEP) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 89. 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
OrganismOvis aries (Sheep) [Complete proteome]
Taxonomic identifier9940 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis

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.

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.

Enzyme regulation

Regulated predominantly by intracellular cAMP levels 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 – 509509Steroid 17-alpha-hydroxylase/17,20 lyase
PRO_0000051942

Sites

Metal binding4421Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict2101G → S in AAA63517. Ref.1
Sequence conflict4641N → Y in AAA63517. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q29497 [UniParc].

Last modified January 4, 2005. Version 2.
Checksum: D498E639D36A5148

FASTA50957,308
        10         20         30         40         50         60 
MWVLLAVFLL TLAYLFWPKT KHSGAKYPRS LPSLPLVGSL PFLPRRGQQH 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 VNDGILEVLG KEVLLDIFPA LKIFPSKAME KMKGCVETRN 

       250        260        270        280        290        300 
ELLSEILEKC QENFTSDSIT NLLHILMQAK VNADNNNTGP EQDSKLLSNR HMLATIADIF 

       310        320        330        340        350        360 
GAGVETTTSV IKWIVAYLLH HPSLKKRIQD SIDQNIGFNR TPTISDRNRL 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]"Cloning and expression of ovine cytochrome P-450 17-alpha hydroxylase/c17-20 lyase."
Murry B.A., Swart P., Mason J.I.
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Adrenal cortex.
[2]"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.
Biochemistry (Mosc.) 68:86-98(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Adrenal gland.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L40335 mRNA. Translation: AAA63517.1.
AF251388 mRNA. Translation: AAF65824.1.
RefSeqNP_001009483.1. NM_001009483.1.
UniGeneOar.399.

3D structure databases

ProteinModelPortalQ29497.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID493968.

Organism-specific databases

CTD1586.

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_SHEEP
AccessionPrimary (citable) accession number: Q29497
Secondary accession number(s): Q9N0U6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 4, 2005
Last modified: April 16, 2014
This is version 89 of the entry and version 2 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