P27786 (CP17A_MOUSE) 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

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [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 › Mus › Mus

Protein attributes

Sequence length	507 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
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 Reference proteome
Gene Ontology (GO)
Biological_process	Leydig cell differentiation Inferred from electronic annotation. Source: Compara adrenal gland development Inferred from electronic annotation. Source: Compara biphenyl metabolic process Inferred from electronic annotation. Source: Compara cellular response to antibiotic Inferred from electronic annotation. Source: Compara cellular response to gonadotropin stimulus Inferred from electronic annotation. Source: Compara cellular response to lipopolysaccharide Inferred from electronic annotation. Source: Compara dibenzo-p-dioxin metabolic process Inferred from electronic annotation. Source: Compara glucocorticoid biosynthetic process Inferred from direct assay PubMed 7588219. Source: MGI hippocampus development Inferred from electronic annotation. Source: Compara ovulation Inferred from electronic annotation. Source: Compara phenol-containing compound metabolic process Inferred from electronic annotation. Source: Compara phthalate metabolic process Inferred from electronic annotation. Source: Compara positive regulation of steroid hormone biosynthetic process Inferred from electronic annotation. Source: Compara response to acetate Inferred from electronic annotation. Source: Compara response to cAMP Inferred from electronic annotation. Source: Compara response to cytokine stimulus Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to fungicide Inferred from electronic annotation. Source: Compara response to herbicide Inferred from electronic annotation. Source: Compara response to insecticide Inferred from electronic annotation. Source: Compara response to ionizing radiation Inferred from electronic annotation. Source: Compara response to methylmercury Inferred from electronic annotation. Source: Compara response to nutrient levels Inferred from electronic annotation. Source: Compara response to retinoic acid Inferred from electronic annotation. Source: Compara response to steroid hormone stimulus Inferred from electronic annotation. Source: Compara
Cellular_component	axon Inferred from direct assay PubMed 7588260. Source: MGI endoplasmic reticulum Inferred from electronic annotation. Source: Compara membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay PubMed 14651853. Source: MGI neuronal cell body Inferred from direct assay PubMed 7588260. Source: MGI
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro steroid 17-alpha-monooxygenase activity Inferred from direct assay PubMed 7588219. Source: MGI
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_0000051935
Sites
	Metal binding	441	1	Iron (heme axial ligand) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P27786 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: C0916193356EFEBD	FASTA	507	57,638
	10 20 30 40 50 60 MWELVGLLLL ILAYFFWPKS KTPNAKFPRS LPFLPLVGSL PFLPRRGHMH ANFFKLQEKY 70 80 90 100 110 120 GPIYSLRLGT TTAVIVGHYQ LAREVLVKKG KEFSGRPQMV TLGLLSDQGK GVAFADSSSS 130 140 150 160 170 180 WQLHRKLVFS TFSLFRDDQK LEKMICQEAN SLCDLILTYD GESRDLSTLI FKSVINIICT 190 200 210 220 230 240 ICFNISFENK DPILTTIQTF TEGIVDVLGH SDLVDIFPWL KIFPNKNLEM IKEHTKIREK 250 260 270 280 290 300 TLVEMFEKCK EKFNSESLSS LTDILIQAKM NAENNNTGEG QDPSVFSDKH ILVTVGDIFG 310 320 330 340 350 360 AGIETTSSVL NWILAFLVHN PEVKRKIQKE IDQYVGFSRT PSFNDRTHLL MLEATIREVL 370 380 390 400 410 420 RIRPVAPLLI PHKANIDSSI GEFAIPKDTH VIINLWALHH DKNEWDQPDR FMPERFLDPT 430 440 450 460 470 480 GSHLITPTPS YLPFGAGPRS CIGEALARQE LFIFMALLLQ RFDFDVSDDK QLPCLVGDPK 490 500 VVFLIDPFKV KITVRQAWKD AQVEVST

References

[1]	"Isolation, characterization, and chromosomal mapping of mouse P450 17 alpha-hydroxylase/C17-20 lyase." Youngblood G.L., Sartorius C., Taylor B.A., Payne A.H. Genomics 10:270-275(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M64863 mRNA. Translation: AAA39877.1.
IPI	IPI00119940.
PIR	A39072.
RefSeq	NP_031835.3. NM_007809.3.
UniGene	Mm.1262.
3D structure databases
ProteinModelPortal	P27786.
SMR	P27786. Positions 34-502.
ModBase	Search...
PTM databases
PhosphoSite	P27786.
Proteomic databases
PaxDb	P27786.
PRIDE	P27786.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000026012; ENSMUSP00000026012; ENSMUSG00000003555.
GeneID	13074.
KEGG	mmu:13074.
Organism-specific databases
CTD	1586.
MGI	MGI:88586. Cyp17a1.
Phylogenomic databases
eggNOG	COG2124.
HOGENOM	HOG000036991.
HOVERGEN	HBG106944.
InParanoid	P27786.
KO	K00512.
OMA	ILAYFFW.
OrthoDB	EOG4W9J45.
Enzyme and pathway databases
UniPathway	UPA00062.
Gene expression databases
ArrayExpress	P27786.
Bgee	P27786.
Genevestigator	P27786.
GermOnline	ENSMUSG00000003555. Mus musculus.
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
NextBio	283012.
SOURCE	Search...

Entry information

Entry name

CP17A_MOUSE

Accession

Primary (citable) accession number: P27786

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	May 1, 2013
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program