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Protein

Steroid 17-alpha-hydroxylase/17,20 lyase

Gene

Cyp17a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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.

Cofactori

hemeBy similarity

Enzyme regulationi

Regulated predominantly by intracellular cAMP levels.

Pathway:isteroid biosynthesis

This protein is involved in the pathway steroid biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway steroid biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi441 – 4411Iron (heme axial ligand)By similarity

GO - Molecular functioni

GO - Biological processi

  • adrenal gland development Source: RGD
  • androgen biosynthetic process Source: RGD
  • biphenyl metabolic process Source: RGD
  • cellular response to antibiotic Source: RGD
  • cellular response to gonadotropin stimulus Source: RGD
  • cellular response to lipopolysaccharide Source: RGD
  • dibenzo-p-dioxin metabolic process Source: RGD
  • hippocampus development Source: RGD
  • hormone biosynthetic process Source: UniProtKB
  • Leydig cell differentiation Source: RGD
  • male gonad development Source: RGD
  • organic acid metabolic process Source: RGD
  • ovulation Source: RGD
  • phenol-containing compound metabolic process Source: RGD
  • phthalate metabolic process Source: RGD
  • positive regulation of steroid hormone biosynthetic process Source: RGD
  • progesterone metabolic process Source: UniProtKB
  • response to acetate Source: RGD
  • response to cAMP Source: RGD
  • response to cytokine Source: RGD
  • response to drug Source: RGD
  • response to fungicide Source: RGD
  • response to gonadotropin Source: RGD
  • response to herbicide Source: RGD
  • response to insecticide Source: RGD
  • response to ionizing radiation Source: RGD
  • response to methylmercury Source: RGD
  • response to nutrient levels Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to organic substance Source: RGD
  • response to retinoic acid Source: RGD
  • response to steroid hormone Source: RGD
  • response to toxic substance Source: RGD
  • steroid biosynthetic process Source: RGD
  • steroid metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Steroidogenesis

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_281422. Androgen biosynthesis.
REACT_326910. Glucocorticoid biosynthesis.
REACT_350068. Endogenous sterols.
UniPathwayiUPA00062.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Cyp17a1
Synonyms:Cyp17
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2456. Cyp17a1.

Subcellular locationi

GO - Cellular componenti

  • cell projection Source: RGD
  • endoplasmic reticulum Source: RGD
  • intracellular membrane-bounded organelle Source: RGD
  • membrane Source: UniProtKB-SubCell
  • neuronal cell body Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 507507Steroid 17-alpha-hydroxylase/17,20 lyasePRO_0000051941Add
BLAST

Proteomic databases

PaxDbiP11715.
PRIDEiP11715.

PTM databases

PhosphoSiteiP11715.

Expressioni

Gene expression databases

ExpressionAtlasiP11715. baseline and differential.
GenevisibleiP11715. RN.

Interactioni

Protein-protein interaction databases

MINTiMINT-4566010.
STRINGi10116.ENSRNOP00000027160.

Structurei

3D structure databases

ProteinModelPortaliP11715.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Phylogenomic databases

eggNOGiCOG2124.
HOGENOMiHOG000036991.
HOVERGENiHBG106944.
InParanoidiP11715.
KOiK00512.
OrthoDBiEOG7RBZ85.
PhylomeDBiP11715.
TreeFamiTF105095.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11715-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWELVGLLLL ILAYFFWVKS KTPGAKLPRS LPSLPLVGSL PFLPRRGHMH
60 70 80 90 100
VNFFKLQEKY GPIYSLRLGT TTTVIIGHYQ LAREVLIKKG KEFSGRPQMV
110 120 130 140 150
TQSLLSDQGK GVAFADAGSS WHLHRKLVFS TFSLFKDGQK LEKLICQEAK
160 170 180 190 200
SLCDMMLAHD KESIDLSTPI FMSVTNIICA ICFNISYEKN DPKLTAIKTF
210 220 230 240 250
TEGIVDATGD RNLVDIFPWL TIFPNKGLEV IKGYAKVRNE VLTGIFEKCR
260 270 280 290 300
EKFDSQSISS LTDILIQAKM NSDNNNSCEG RDPDVFSDRH ILATVGDIFG
310 320 330 340 350
AGIETTTTVL KWILAFLVHN PEVKKKIQKE IDQYVGFSRT PTFNDRSHLL
360 370 380 390 400
MLEATIREVL RIRPVAPMLI PHKANVDSSI GEFTVPKDTH VVVNLWALHH
410 420 430 440 450
DENEWDQPDQ FMPERFLDPT GSHLITPTQS YLPFGAGPRS CIGEALARQE
460 470 480 490 500
LFVFTALLLQ RFDLDVSDDK QLPRLEGDPK VVFLIDPFKV KITVRQAWMD

AQAEVST
Length:507
Mass (Da):57,250
Last modified:August 1, 1990 - v2
Checksum:iA535600F7E6A399B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti190 – 1901N → K in AAH78898 (PubMed:15489334).Curated
Sequence conflicti505 – 5062VS → LT in AAA41050 (PubMed:3260774).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14086 mRNA. Translation: CAA32248.1.
X69816 Genomic DNA. Translation: CAA49470.1.
M31681 mRNA. Translation: AAA41777.1.
M22204 mRNA. Translation: AAA41783.1.
BC078898 mRNA. Translation: AAH78898.1.
Z11902 Genomic DNA. Translation: CAA77954.1.
M21208 mRNA. Translation: AAA41050.1.
M27282 mRNA. Translation: AAA41779.1.
PIRiA31359. A30828.
RefSeqiNP_036885.1. NM_012753.2.
XP_006231496.1. XM_006231434.2.
XP_006231497.1. XM_006231435.2.
UniGeneiRn.10172.

Genome annotation databases

GeneIDi25146.
KEGGirno:25146.
UCSCiRGD:2456. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14086 mRNA. Translation: CAA32248.1.
X69816 Genomic DNA. Translation: CAA49470.1.
M31681 mRNA. Translation: AAA41777.1.
M22204 mRNA. Translation: AAA41783.1.
BC078898 mRNA. Translation: AAH78898.1.
Z11902 Genomic DNA. Translation: CAA77954.1.
M21208 mRNA. Translation: AAA41050.1.
M27282 mRNA. Translation: AAA41779.1.
PIRiA31359. A30828.
RefSeqiNP_036885.1. NM_012753.2.
XP_006231496.1. XM_006231434.2.
XP_006231497.1. XM_006231435.2.
UniGeneiRn.10172.

3D structure databases

ProteinModelPortaliP11715.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4566010.
STRINGi10116.ENSRNOP00000027160.

Chemistry

BindingDBiP11715.
ChEMBLiCHEMBL4430.

PTM databases

PhosphoSiteiP11715.

Proteomic databases

PaxDbiP11715.
PRIDEiP11715.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25146.
KEGGirno:25146.
UCSCiRGD:2456. rat.

Organism-specific databases

CTDi1586.
RGDi2456. Cyp17a1.

Phylogenomic databases

eggNOGiCOG2124.
HOGENOMiHOG000036991.
HOVERGENiHBG106944.
InParanoidiP11715.
KOiK00512.
OrthoDBiEOG7RBZ85.
PhylomeDBiP11715.
TreeFamiTF105095.

Enzyme and pathway databases

UniPathwayiUPA00062.
ReactomeiREACT_281422. Androgen biosynthesis.
REACT_326910. Glucocorticoid biosynthesis.
REACT_350068. Endogenous sterols.

Miscellaneous databases

NextBioi605573.
PROiP11715.

Gene expression databases

ExpressionAtlasiP11715. baseline and differential.
GenevisibleiP11715. RN.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Rat P450(17 alpha) from testis: characterization of a full-length cDNA encoding a unique steroid hydroxylase capable of catalyzing both delta 4- and delta 5-steroid-17,20-lyase reactions."
    Fevold H.R., Lorence M.C., McCarthy J.L., Trant J.M., Kagimoto M., Waterman M.R., Mason J.I.
    Mol. Endocrinol. 3:968-975(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Rat testis P-450(17)alpha cDNA: the deduced amino acid sequence, expression and secondary structural configuration."
    Namiki M., Kitamura M., Buczko E., Dufau M.L.
    Biochem. Biophys. Res. Commun. 157:705-712(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: Testis.
  3. "Transcriptional regulation of rat cytochrome P450c17 expression in mouse Leydig MA-10 and adrenal Y-1 cells: identification of a single protein that mediates both basal and cAMP-induced activities."
    Givens C.R., Zhang P., Bair S.R., Mellon S.H.
    DNA Cell Biol. 13:1087-1098(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Sprague-Dawley.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  5. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-97.
  6. "Hormonal regulation of rat Leydig cell cytochrome P-45017 alpha mRNA levels and characterization of a partial length rat P-45017 alpha cDNA."
    Nishihara M., Winters C.A., Buzko E., Waterman M.R., Dufau M.L.
    Biochem. Biophys. Res. Commun. 154:151-158(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 271-507.
  7. "cAMP regulates P450scc gene expression by a cycloheximide-insensitive mechanism in cultured mouse Leydig MA-10 cells."
    Mellon S.H., Vaisse C.
    Proc. Natl. Acad. Sci. U.S.A. 86:7775-7779(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 273-507.
  8. "Purification and characterization of six cytochromes P-450 from hepatic microsomes of immature female rats."
    Imaoka S., Kamataki T., Funae Y.
    J. Biochem. 102:843-851(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-16.

Entry informationi

Entry nameiCP17A_RAT
AccessioniPrimary (citable) accession number: P11715
Secondary accession number(s): Q68FY2, Q6LAE5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: August 1, 1990
Last modified: July 22, 2015
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.