Q9GLD2 (CP17A_PAPHU) 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

Papio hamadryas ursinus (Chacma baboon)

Taxonomic identifier

36229 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Cercopithecoidea › Cercopithecidae › Cercopithecinae › Papio

Protein attributes

Sequence length	508 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. Has a higher activity for progesterone hydroxylation relative to pregnenolone. Has no 16-alpha-hydroxylase and no lyase activity for 17-alpha-hydroxyprogesterone.
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	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 – 508	508	Steroid 17-alpha-hydroxylase/17,20 lyase		PRO_0000051938
Sites
	Metal binding	442	1	Iron (heme axial ligand) By similarity
Experimental info
	Sequence conflict	331	1	G → E in AAK57726. Ref.2
	Sequence conflict	396	1	L → R in AAK57726. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9GLD2 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 40DF6068D66BAA80	FASTA	508	57,566
	10 20 30 40 50 60 MWELVALLLL TLAYLFWPKR RCPGAKYPKS LLSLPLVGSL PFLPRHGHMH NNFFKLQKKY 70 80 90 100 110 120 GPIYSVRMGT KTTVIVGHHQ LAKEVLIKKG KDFSGRPQVT TLDILSNNRK GIAFADYGAH 130 140 150 160 170 180 WQLHRRLAMA TFALFKDGDQ KLEKIICQEI STLCDMLATH NGQTIDISFP VFVAITNVIS 190 200 210 220 230 240 LICFNISYKN GDPELKIVHN YNEGIIDSLG KESLVDLFPW LKVFPNKTLE KLKRHVKTRN 250 260 270 280 290 300 DLLTKIFENY KEKFRSDSIT NMLDVLMQAK MNSDNGNAGP DQDSELLSDN HILTTIGDIF 310 320 330 340 350 360 GAGVETTTSV VKWIVAFLLH NPQVKKKLYE GIDQNVGFSR TPTISDRNRL LLLEATIREV 370 380 390 400 410 420 LRIRPVAPML IPHKANVDSS IGEFAVDKGT HVIINLWALH HNEKEWHQPD QFMPERFLNP 430 440 450 460 470 480 AGTQLISPSL SYLPFGAGPR SCIGEILARQ ELFLIMAWLL QRFDLEVPDD GQLPSLEGNP 490 500 KVVFLIDSFK VKIKVRQAWR EAQAEGST

References

[1]	"Cloning and expression of baboon cytochrome P-450 17-alpha hydroxylase/c17-20 lyase." Swart A.C., Kolar N.W., Swart P. Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Tissue: Adrenal gland.
[2]	"Baboon cytochrome P450 17alpha-hydroxylase/17,20-lyase (CYP17)." Swart A.C., Kolar N.W., Lombard N., Mason J.I., Swart P. Eur. J. Biochem. 269:5608-5616(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF297650 mRNA. Translation: AAG10599.1. AY034635 Genomic DNA. Translation: AAK57726.1.
3D structure databases
ProteinModelPortal	Q9GLD2.
ModBase	Search...
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_PAPHU

Accession

Primary (citable) accession number: Q9GLD2
Secondary accession number(s): Q95M62

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2003
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program