P11715 (CP17A_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Steroid 17-alpha-hydroxylase/17,20 lyase
EC=1.14.99.9

Alternative name(s):
CYPXVII
Cytochrome P450 17A1
Cytochrome P450-C17
Short name=Cytochrome P450c17

Gene names

Name:	Cyp17a1
Synonyms:	Cyp17

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	507 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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 steroid + AH2 + O2 = a 17-alpha-hydroxysteroid + A + H2O.
Cofactor	Heme group By similarity.
Enzyme regulation	Regulated predominantly by intracellular cAMP levels.
Pathway	Lipid metabolism; steroid biosynthesis.
Subcellular location	Membrane Potential.
Sequence similarities	Belongs to the cytochrome P450 family.

Ontologies

Keywords
Biological process	Steroidogenesis
Cellular component	Membrane
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	Leydig cell differentiation Inferred from expression pattern. Source: RGD adrenal gland development Inferred from expression pattern. Source: RGD androgen biosynthetic process Traceable author statement Ref.3. Source: RGD biphenyl metabolic process Inferred from expression pattern. Source: RGD cellular response to antibiotic Inferred from expression pattern. Source: RGD cellular response to gonadotropin stimulus Inferred from expression pattern. Source: RGD cellular response to lipopolysaccharide Inferred from expression pattern. Source: RGD dibenzo-p-dioxin metabolic process Inferred from expression pattern. Source: RGD hippocampus development Inferred from expression pattern. Source: RGD ovulation Inferred from expression pattern. Source: RGD phenol-containing compound metabolic process Inferred from expression pattern. Source: RGD phthalate metabolic process Inferred from expression pattern. Source: RGD positive regulation of steroid hormone biosynthetic process Inferred from mutant phenotype. Source: RGD response to acetate Inferred from expression pattern. Source: RGD response to cAMP Inferred from expression pattern. Source: RGD response to cytokine stimulus Inferred from expression pattern. Source: RGD response to drug Inferred from expression pattern. Source: RGD response to fungicide Inferred from expression pattern. Source: RGD response to herbicide Inferred from expression pattern. Source: RGD response to insecticide Inferred from expression pattern. Source: RGD response to ionizing radiation Inferred from expression pattern. Source: RGD response to methylmercury Inferred from expression pattern. Source: RGD response to organic cyclic compound Inferred from expression pattern. Source: RGD response to retinoic acid Inferred from expression pattern. Source: RGD response to steroid hormone stimulus Inferred from expression pattern. Source: RGD
Cellular component	cell projection Inferred from direct assay. Source: RGD endoplasmic reticulum Inferred from direct assay. Source: RGD membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Inferred from direct assay. Source: RGD neuronal cell body Inferred from direct assay. Source: RGD
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro steroid 17-alpha-monooxygenase activity Inferred from direct assay Ref.1. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 507	507	Steroid 17-alpha-hydroxylase/17,20 lyase		PRO_0000051941
Sites
	Metal binding	441	1	Iron (heme axial ligand) By similarity
Experimental info
	Sequence conflict	190	1	N → K in AAH78898. Ref.4
	Sequence conflict	505 – 506	2	VS → LT in AAA41050. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P11715 [UniParc]. Last modified August 1, 1990. Version 2. Checksum: A535600F7E6A399B	FASTA	507	57,250
	10 20 30 40 50 60 MWELVGLLLL ILAYFFWVKS KTPGAKLPRS LPSLPLVGSL PFLPRRGHMH VNFFKLQEKY 70 80 90 100 110 120 GPIYSLRLGT TTTVIIGHYQ LAREVLIKKG KEFSGRPQMV TQSLLSDQGK GVAFADAGSS 130 140 150 160 170 180 WHLHRKLVFS TFSLFKDGQK LEKLICQEAK SLCDMMLAHD KESIDLSTPI FMSVTNIICA 190 200 210 220 230 240 ICFNISYEKN DPKLTAIKTF TEGIVDATGD RNLVDIFPWL TIFPNKGLEV IKGYAKVRNE 250 260 270 280 290 300 VLTGIFEKCR EKFDSQSISS LTDILIQAKM NSDNNNSCEG RDPDVFSDRH ILATVGDIFG 310 320 330 340 350 360 AGIETTTTVL KWILAFLVHN PEVKKKIQKE IDQYVGFSRT PTFNDRSHLL MLEATIREVL 370 380 390 400 410 420 RIRPVAPMLI PHKANVDSSI GEFTVPKDTH VVVNLWALHH DENEWDQPDQ FMPERFLDPT 430 440 450 460 470 480 GSHLITPTQS YLPFGAGPRS CIGEALARQE LFVFTALLLQ RFDLDVSDDK QLPRLEGDPK 490 500 VVFLIDPFKV KITVRQAWMD AQAEVST

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Rat P450(17 alpha) from testis: characterization of a full-length cDNA encoding a unique steroid hydroxylase capable of catalyzing both delta 4- and delta 5-steroid-17,20-lyase reactions." Fevold H.R., Lorence M.C., McCarthy J.L., Trant J.M., Kagimoto M., Waterman M.R., Mason J.I. Mol. Endocrinol. 3:968-975(1989) [PubMed: 2786990] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	"Rat testis P-450(17)alpha cDNA: the deduced amino acid sequence, expression and secondary structural configuration." Namiki M., Kitamura M., Buczko E., Dufau M.L. Biochem. Biophys. Res. Commun. 157:705-712(1988) [PubMed: 3264499] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Tissue: Testis.
[3]	"Transcriptional regulation of rat cytochrome P450c17 expression in mouse Leydig MA-10 and adrenal Y-1 cells: identification of a single protein that mediates both basal and cAMP-induced activities." Givens C.R., Zhang P., Bair S.R., Mellon S.H. DNA Cell Biol. 13:1087-1098(1994) [PubMed: 7702752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Sprague-Dawley.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[5]	"Gene for 17 alpha-hydroxylase/C (17-20) lyase P-450: complete nucleotide sequence of the porcine gene and 5' upstream sequence of the rat gene." Zhang P., Nason T.F., Han X.G., Hall P.F. Biochim. Biophys. Acta 1131:345-348(1992) [PubMed: 1627653] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-97.
[6]	"Hormonal regulation of rat Leydig cell cytochrome P-45017 alpha mRNA levels and characterization of a partial length rat P-45017 alpha cDNA." Nishihara M., Winters C.A., Buzko E., Waterman M.R., Dufau M.L. Biochem. Biophys. Res. Commun. 154:151-158(1988) [PubMed: 3260774] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 271-507.
[7]	"cAMP regulates P450scc gene expression by a cycloheximide-insensitive mechanism in cultured mouse Leydig MA-10 cells." Mellon S.H., Vaisse C. Proc. Natl. Acad. Sci. U.S.A. 86:7775-7779(1989) [PubMed: 2554289] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 273-507.
[8]	"Purification and characterization of six cytochromes P-450 from hepatic microsomes of immature female rats." Imaoka S., Kamataki T., Funae Y. J. Biochem. 102:843-851(1987) [PubMed: 3436956] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-16.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X14086 mRNA. Translation: CAA32248.1. X69816 Genomic DNA. Translation: CAA49470.1. M31681 mRNA. Translation: AAA41777.1. M22204 mRNA. Translation: AAA41783.1. BC078898 mRNA. Translation: AAH78898.1. Z11902 Genomic DNA. Translation: CAA77954.1. M21208 mRNA. Translation: AAA41050.1. M27282 mRNA. Translation: AAA41779.1.
IPI	IPI00196701.
PIR	A30828. A31359.
RefSeq	NP_036885.1. NM_012753.1.
UniGene	Rn.10172.
3D structure databases
ProteinModelPortal	P11715.
ModBase	Search...
Protein-protein interaction databases
STRING	P11715.
PTM databases
PhosphoSite	P11715.
Proteomic databases
PRIDE	P11715.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000027160; ENSRNOP00000027160; ENSRNOG00000020035.
GeneID	25146.
KEGG	rno:25146.
UCSC	NM_012753. rat.
Organism-specific databases
CTD	1586.
RGD	2456. Cyp17a1.
Phylogenomic databases
eggNOG	roNOG05560.
HOVERGEN	HBG106944.
InParanoid	P11715.
OrthoDB	EOG4W9J45.
PhylomeDB	P11715.
Gene expression databases
ArrayExpress	P11715.
Genevestigator	P11715.
GermOnline	ENSRNOG00000020035. Rattus norvegicus.
Family and domain databases
InterPro	IPR001128. Cyt_P450. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. [Graphical view]
Gene3D	G3DSA:1.10.630.10. Cyt_P450. 1 hit.
KO	K00512.
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00463. EP450I. PR00385. P450.
SUPFAM	SSF48264. Cytochrome_P450. 1 hit.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	605573.

Entry information

Entry name

CP17A_RAT

Accession

Primary (citable) accession number: P11715
Secondary accession number(s): Q68FY2, Q6LAE5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	August 1, 1990
Last modified:	November 16, 2011
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program