Q9N0U7 (CP17A_CAPHI) 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

Capra hircus (Goat)

Taxonomic identifier

9925 [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 › Caprinae › Capra

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 By similarity.
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.
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
Gene Ontology (GO)
Biological_process	hormone biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB progesterone metabolic process Inferred from sequence or structural similarity. Source: UniProtKB steroid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
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 sequence or structural similarity. Source: UniProtKB
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_0000051927
Sites
	Metal binding	442	1	Iron (heme axial ligand) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9N0U7 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: A3C77300622A2EA6	FASTA	509	57,298
	10 20 30 40 50 60 MWVLLGVFLL TLAYLFWPKT KHSAAKYPRS LPSLPLVGSL LFLPRRGQQH 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 VNDGILEVLS KEILLDIFPA LKIFPSKAME KMKGCVETRN 250 260 270 280 290 300 ELLNEILEKC QENFTSDSIT NLLHILMQAK VNADNNNAGP DQDSKLLSNR HMLATIADIF 310 320 330 340 350 360 GAGVETTTSV IKWIVAYLLH HPSLKKRIQD SIDQNIGFNR TPTISDRNCL 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

References

[1]

"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. Biokhimiia 68:86-98(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Adrenal gland.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF251387 mRNA. Translation: AAF65823.1.
3D structure databases
ProteinModelPortal	Q9N0U7.
ModBase	Search...
Proteomic databases
PRIDE	Q9N0U7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG106944.
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...

Entry information

Entry name

CP17A_CAPHI

Accession

Primary (citable) accession number: Q9N0U7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 4, 2005
Last sequence update:	October 1, 2000
Last modified:	May 29, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program