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
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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › 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 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.
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	Lyase Monooxygenase Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Leydig cell differentiation Inferred from expression pattern PubMed 18502897. Source: RGD adrenal gland development Inferred from expression pattern PubMed 17065412. Source: RGD androgen biosynthetic process Traceable author statement Ref.3. Source: RGD biphenyl metabolic process Inferred from expression pattern PubMed 20356859. Source: RGD cellular response to antibiotic Inferred from expression pattern PubMed 18655822. Source: RGD cellular response to gonadotropin stimulus Inferred from expression pattern PubMed 20963569. Source: RGD cellular response to lipopolysaccharide Inferred from expression pattern PubMed 20665543. Source: RGD dibenzo-p-dioxin metabolic process Inferred from expression pattern PubMed 20059580. Source: RGD glucocorticoid biosynthetic process Inferred from electronic annotation. Source: Compara hippocampus development Inferred from expression pattern PubMed 21047951. Source: RGD ovulation Inferred from expression pattern PubMed 19775733. Source: RGD phenol-containing compound metabolic process Inferred from expression pattern PubMed 18191889. Source: RGD phthalate metabolic process Inferred from expression pattern PubMed 16809437. Source: RGD positive regulation of steroid hormone biosynthetic process Inferred from mutant phenotype PubMed 19615041. Source: RGD progesterone metabolic process Inferred from sequence or structural similarity. Source: UniProtKB response to acetate Inferred from expression pattern PubMed 21046364. Source: RGD response to cAMP Inferred from expression pattern PubMed 17291543. Source: RGD response to cytokine stimulus Inferred from expression pattern PubMed 15958400. Source: RGD response to drug Inferred from expression pattern PubMed 19603415. Source: RGD response to fungicide Inferred from expression pattern PubMed 16214947PubMed 17369198. Source: RGD response to herbicide Inferred from expression pattern PubMed 20667998. Source: RGD response to insecticide Inferred from expression pattern PubMed 17569032. Source: RGD response to ionizing radiation Inferred from expression pattern PubMed 18821396. Source: RGD response to methylmercury Inferred from expression pattern PubMed 17869401. Source: RGD response to nutrient levels Inferred from expression pattern PubMed 17936465PubMed 19389810. Source: RGD response to retinoic acid Inferred from expression pattern PubMed 19497980. Source: RGD response to steroid hormone stimulus Inferred from expression pattern PubMed 19961867. Source: RGD
Cellular_component	axon Inferred from electronic annotation. Source: Compara cell projection Inferred from direct assay PubMed 15934942. Source: RGD endoplasmic reticulum Inferred from direct assay PubMed 11691658. Source: RGD membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from electronic annotation. Source: Compara neuronal cell body Inferred from direct assay PubMed 15934942. Source: RGD
Molecular_function	17-alpha-hydroxyprogesterone aldolase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from sequence or structural similarity. Source: UniProtKB iron ion 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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_012753.2.
UniGene	Rn.10172.
3D structure databases
ProteinModelPortal	P11715.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4566010.
PTM databases
PhosphoSite	P11715.
Proteomic databases
PaxDb	P11715.
PRIDE	P11715.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000027160; ENSRNOP00000027160; ENSRNOG00000020035.
GeneID	25146.
KEGG	rno:25146.
UCSC	RGD:2456. rat.
Organism-specific databases
CTD	1586.
RGD	2456. Cyp17a1.
Phylogenomic databases
eggNOG	COG2124.
GeneTree	ENSGT00690000101630.
HOGENOM	HOG000036991.
HOVERGEN	HBG106944.
InParanoid	P11715.
KO	K00512.
OrthoDB	EOG4W9J45.
Enzyme and pathway databases
UniPathway	UPA00062.
Gene expression databases
ArrayExpress	P11715.
Genevestigator	P11715.
GermOnline	ENSRNOG00000020035. Rattus norvegicus.
Family and domain databases
Gene3D	1.10.630.10. 1 hit.
InterPro	IPR001128. Cyt_P450. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. [Graphical view]
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
BindingDB	P11715.
ChEMBL	CHEMBL4430.
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:	May 29, 2013
This is version 123 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program