P05185 (CP17A_BOVIN) 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

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	509 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	steroid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
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 electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 509	509	Steroid 17-alpha-hydroxylase/17,20 lyase		PRO_0000051926
Sites
	Metal binding	442	1	Iron (heme axial ligand) By similarity
Experimental info
	Sequence conflict	240	1	N → K in AAI10170. Ref.3
	Sequence conflict	423	1	T → A no nucleotide entry Ref.2
	Sequence conflict	458	1	R → W no nucleotide entry Ref.2
	Sequence conflict	509	1	P → S no nucleotide entry Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P05185 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: 64B0E5537A474BB7	FASTA	509	57,244
	10 20 30 40 50 60 MWLLLAVFLL TLAYLFWPKT KHSGAKYPRS LPSLPLVGSL PFLPRRGQQH KNFFKLQEKY 70 80 90 100 110 120 GPIYSFRLGS KTTVMIGHHQ LAREVLLKKG KEFSGRPKVA TLDILSDNQK GIAFADHGAH 130 140 150 160 170 180 WQLHRKLALN AFALFKDGNL KLEKIINQEA NVLCDFLATQ HGEAIDLSEP LSLAVTNIIS 190 200 210 220 230 240 FICFNFSFKN EDPALKAIQN VNDGILEVLS KEVLLDIFPV LKIFPSKAME KMKGCVQTRN 250 260 270 280 290 300 ELLNEILEKC QENFSSDSIT NLLHILIQAK VNADNNNAGP DQDSKLLSNR HMLATIGDIF 310 320 330 340 350 360 GAGVETTTSV IKWIVAYLLH HPSLKKRIQD DIDQIIGFNR TPTISDRNRL VLLEATIREV 370 380 390 400 410 420 LRIRPVAPTL IPHKAVIDSS IGDLTIDKGT DVVVNLWALH HSEKEWQHPD LFMPERFLDP 430 440 450 460 470 480 TGTQLISPSL SYLPFGAGPR SCVGEMLARQ ELFLFMSRLL QRFNLEIPDD GKLPSLEGHA 490 500 SLVLQIKPFK VKIEVRQAWK EAQAEGSTP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Bovine adrenocortical cytochrome P-450(17 alpha). Regulation of gene expression by ACTH and elucidation of primary sequence." Zuber M.X., John M.E., Okamura T., Simpson E.R., Waterman M.R. J. Biol. Chem. 261:2475-2482(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structural characterization of the bovine CYP17 (17 alpha-hydroxylase) gene." Bhasker C.R., Adler B.S., Dee A., John M.E., Kagimoto M., Zuber M.X., Ahlgren R., Wang X.D., Simpson E.R., Waterman M.R. Arch. Biochem. Biophys. 271:479-487(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	NIH - Mammalian Gene Collection (MGC) project Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Liver.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M12547 mRNA. Translation: AAA30485.1. BC110169 mRNA. Translation: AAI10170.1.
IPI	IPI00704148.
PIR	S04346.
RefSeq	NP_776729.1. NM_174304.2.
UniGene	Bt.89153.
3D structure databases
ProteinModelPortal	P05185.
ModBase	Search...
Protein-protein interaction databases
STRING	9913.ENSBTAP00000019061.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	281739.
KEGG	bta:281739.
Organism-specific databases
CTD	1586.
Phylogenomic databases
eggNOG	COG2124.
HOGENOM	HOG000036991.
HOVERGEN	HBG106944.
InParanoid	P05185.
KO	K00512.
OrthoDB	EOG4W9J45.
Enzyme and pathway databases
UniPathway	UPA00062.
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	20805659.

Entry information

Entry name

CP17A_BOVIN

Accession

Primary (citable) accession number: P05185
Secondary accession number(s): Q2YDL3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	May 1, 2013
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program