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P11715

- CP17A_RAT

UniProt

P11715 - CP17A_RAT

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Protein

Steroid 17-alpha-hydroxylase/17,20 lyase

Gene

Cyp17a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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.

Pathwayi

Sites

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

GO - Molecular functioni

  1. 17-alpha-hydroxyprogesterone aldolase activity Source: UniProtKB-EC
  2. heme binding Source: UniProtKB
  3. iron ion binding Source: InterPro
  4. steroid 17-alpha-monooxygenase activity Source: RGD

GO - Biological processi

  1. adrenal gland development Source: RGD
  2. androgen biosynthetic process Source: RGD
  3. biphenyl metabolic process Source: RGD
  4. cellular response to antibiotic Source: RGD
  5. cellular response to gonadotropin stimulus Source: RGD
  6. cellular response to lipopolysaccharide Source: RGD
  7. dibenzo-p-dioxin metabolic process Source: RGD
  8. glucocorticoid biosynthetic process Source: Ensembl
  9. hippocampus development Source: RGD
  10. hormone biosynthetic process Source: UniProtKB
  11. Leydig cell differentiation Source: RGD
  12. male gonad development Source: RGD
  13. organic acid metabolic process Source: RGD
  14. ovulation Source: RGD
  15. phenol-containing compound metabolic process Source: RGD
  16. phthalate metabolic process Source: RGD
  17. positive regulation of steroid hormone biosynthetic process Source: RGD
  18. progesterone metabolic process Source: UniProtKB
  19. response to acetate Source: RGD
  20. response to cAMP Source: RGD
  21. response to cytokine Source: RGD
  22. response to drug Source: RGD
  23. response to fungicide Source: RGD
  24. response to gonadotropin Source: RGD
  25. response to herbicide Source: RGD
  26. response to insecticide Source: RGD
  27. response to ionizing radiation Source: RGD
  28. response to methylmercury Source: RGD
  29. response to nutrient levels Source: RGD
  30. response to organic cyclic compound Source: RGD
  31. response to organic substance Source: RGD
  32. response to retinoic acid Source: RGD
  33. response to steroid hormone Source: RGD
  34. response to toxic substance Source: RGD
  35. steroid biosynthetic process Source: RGD
  36. 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_234086. Glucocorticoid biosynthesis.
REACT_243619. Androgen biosynthesis.
REACT_252303. 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: Chromosome 1

Organism-specific databases

RGDi2456. Cyp17a1.

Subcellular locationi

Membrane Curated

GO - Cellular componenti

  1. axon Source: Ensembl
  2. cell projection Source: RGD
  3. endoplasmic reticulum Source: RGD
  4. intracellular membrane-bounded organelle Source: RGD
  5. membrane Source: UniProtKB-KW
  6. mitochondrion Source: Ensembl
  7. 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.
GenevestigatoriP11715.

Interactioni

Protein-protein interaction databases

MINTiMINT-4566010.

Structurei

3D structure databases

ProteinModelPortaliP11715.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Phylogenomic databases

eggNOGiCOG2124.
GeneTreeiENSGT00760000118992.
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

EnsembliENSRNOT00000027160; ENSRNOP00000027160; ENSRNOG00000020035.
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 .
PIRi A31359. A30828.
RefSeqi NP_036885.1. NM_012753.2.
XP_006231496.1. XM_006231434.2.
XP_006231497.1. XM_006231435.2.
UniGenei Rn.10172.

3D structure databases

ProteinModelPortali P11715.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-4566010.

Chemistry

BindingDBi P11715.
ChEMBLi CHEMBL4430.

PTM databases

PhosphoSitei P11715.

Proteomic databases

PaxDbi P11715.
PRIDEi P11715.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000027160 ; ENSRNOP00000027160 ; ENSRNOG00000020035 .
GeneIDi 25146.
KEGGi rno:25146.
UCSCi RGD:2456. rat.

Organism-specific databases

CTDi 1586.
RGDi 2456. Cyp17a1.

Phylogenomic databases

eggNOGi COG2124.
GeneTreei ENSGT00760000118992.
HOGENOMi HOG000036991.
HOVERGENi HBG106944.
InParanoidi P11715.
KOi K00512.
OrthoDBi EOG7RBZ85.
PhylomeDBi P11715.
TreeFami TF105095.

Enzyme and pathway databases

UniPathwayi UPA00062 .
Reactomei REACT_234086. Glucocorticoid biosynthesis.
REACT_243619. Androgen biosynthesis.
REACT_252303. Endogenous sterols.

Miscellaneous databases

NextBioi 605573.
PROi P11715.

Gene expression databases

ExpressionAtlasi P11715. baseline and differential.
Genevestigatori P11715.

Family and domain databases

Gene3Di 1.10.630.10. 1 hit.
InterProi IPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view ]
Pfami PF00067. p450. 1 hit.
[Graphical view ]
PRINTSi PR00463. EP450I.
PR00385. P450.
SUPFAMi SSF48264. SSF48264. 1 hit.
PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: November 26, 2014
This is version 136 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