Steroid 17-alpha-hydroxylase/17,20 lyase

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Reviewed, UniProtKB/Swiss-Prot P19100 (CP17A_PIG)

Last modified June 16, 2009. Version 78. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Steroid 17-alpha-hydroxylase/17,20 lyase
    EC=1.14.99.9
Alternative name(s):
    Cytochrome P450 17A1
    CYPXVII
    P450-C17
      Short name=P450c17

Gene names

Name:	CYP17A1
Synonyms:	CYP17

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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Protein attributes

Sequence length	509 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

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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 steroid + AH₂ + O₂ = a 17-alpha-hydroxysteroid + A + H₂O.
Cofactor	Heme group By similarity.
Enzyme regulation	Regulated predominantly by intracellular cAMP levels.
Pathway	Lipid metabolism; steroid biosynthesis.
Subcellular location	Membrane Potential. Membrane; Single-pass membrane protein.
Sequence similarities	Belongs to the cytochrome P450 family.

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Ontologies

Keywords
Biological process	Steroidogenesis
Cellular component	Membrane
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Gene Ontology (GO)
Biological process	C21-steroid hormone biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
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 steroid 17-alpha-monooxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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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_0000051940

Sites

Metal binding

442

Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict

M → I in CAA77878. Ref.1

Sequence conflict

108 – 116

Missing Ref.1

Sequence conflict

292

M → S in CAA77878. Ref.1

Sequence conflict

319 – 321

LHY → ATLC in CAA77878. Ref.1

Sequence conflict

330

D → E in CAA77878. Ref.1

Sequence conflict

333

D → E in CAA77878. Ref.1

Sequence conflict

407

H → L in AAA31008. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

P19100-1 [UniParc].

Last modified November 1, 1997. Version 3.
Checksum: 9497D185A1B446B4
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FASTA

509

57,447

        10         20         30         40         50         60 
MWVLLVFFLL TLTYLFWPKT KGSGAKYPRS LPVLPVVGSL PFLPRRGHQH MNFFKLQDKY 

        70         80         90        100        110        120 
GPIFSFRLGS KTTVVIGDHQ LAKEVLLKKG KEFSGRPRVM TLDILSDNQK GIAFADHGTS 

       130        140        150        160        170        180 
WQLHRKLALS TFSLFKGGNL KLENIINQEI KVLCDFLATR NGESIDLAQP LSLAMTNIVS 

       190        200        210        220        230        240 
FICFNFSFKK GDPALQAIVN FNDGILDAVG KEILYDMFPG IRILPSQTLE NMKQCVRMRN 

       250        260        270        280        290        300 
ELLREILENR KENYSRNSIT NLLDIMIQAK TNAESNTGGP DHNLKLLSDR HMLATVADIF 

       310        320        330        340        350        360 
GAGVETSASV VKWIVAFLLH YPLLRKKIQD AIDQNIGFNR APSISDRNQL VLLEATIREV 

       370        380        390        400        410        420 
LRFRPVSPTL IPHRAIIDSS IGEFTIDKDT DVVVNLWALH HNEKEWHRPD LFMPERFLDP 

       430        440        450        460        470        480 
TGTQLISPSL SYLPFGAGPR SCVGEMLARQ ELFLFTAGLL QRFDLELPDD GQLPCLVGNP 

       490        500 
SLVLQIDPFK VKIKERQAWK EAHTEGSTS

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References

[1]	"Cytochrome P450c17 (steroid 17 alpha-hydroxylase/17,20 lyase): cloning of human adrenal and testis cDNAs indicates the same gene is expressed in both tissues." Chung B.-C., Picado-Leonard J., Haniu M., Bienkowski M., Hall P.F., Shively J.E., Miller W.L. Proc. Natl. Acad. Sci. U.S.A. 84:407-411(1987) [PubMed: 3025870] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Tissue: Adrenal gland and Testis.
[2]	"Nucleotide sequence of a cDNA encoding porcine testis 17 alpha-hydroxylase cytochrome P-450." Conley A.J., Graham-Lorence S.E., Kagimoto M., Lorence M.C., Murry B.A., Oka K., Sanders D., Mason J.I. Biochim. Biophys. Acta 1130:75-77(1992) [PubMed: 1543750] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis.
[3]	"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: 1627653] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Kidney.
[4]	Conley A.J., Chu X., Corbin C.J. Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.

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Cross-references

Sequence databases
	Z11854, Z11855, Z11856 Genomic DNA. Translation: CAA77878.1. M63507 mRNA. Translation: AAA31008.1. U41525 U41524 Genomic DNA. Translation: AAA84419.1.
PIR	S22339.
RefSeq	NP_999593.1.
UniGene	Ssc.51528
3D structure databases
HSSP	HSSP built from PDB template 1DT6 based on UniProtKB P00179.
ModBase	Search...
Genome annotation databases
GeneID	403330.
KEGG	ssc:403330.
Phylogenomic databases
HOVERGEN	P19100.
Enzyme and pathway databases
BRENDA	1.14.99.9. 249.
Family and domain databases
InterPro	IPR001128. Cyt_P450. IPR017973. Cyt_P450_C. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. [Graphical view]
Gene3D	G3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHER	PTHR19383. Cyt_P450. 1 hit.
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00463. EP450I. PR00385. P450.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

CP17A_PIG

Accession

Primary (citable) accession number: P19100
Secondary accession number(s): Q29553, Q99030

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 78 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents