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P19100

- CP17A_PIG

UniProt

P19100 - CP17A_PIG

Protein

Steroid 17-alpha-hydroxylase/17,20 lyase

Gene

CYP17A1

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 3 (01 Nov 1997)
      Previous versions | rss
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    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

    Heme group.By similarity

    Enzyme regulationi

    Regulated predominantly by intracellular cAMP levels.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi442 – 4421Iron (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: UniProtKB

    GO - Biological processi

    1. glucocorticoid biosynthetic process Source: Ensembl
    2. hormone biosynthetic process Source: UniProtKB
    3. progesterone metabolic process Source: UniProtKB
    4. steroid metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Lyase, Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Steroidogenesis

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_210511. Glucocorticoid biosynthesis.
    REACT_211636. Endogenous sterols.
    REACT_221517. Androgen biosynthesis.
    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
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Chromosome 14

    Subcellular locationi

    Membrane Curated

    GO - Cellular componenti

    1. axon Source: Ensembl
    2. membrane Source: UniProtKB-SubCell
    3. mitochondrion Source: Ensembl
    4. neuronal cell body Source: Ensembl

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 509509Steroid 17-alpha-hydroxylase/17,20 lyasePRO_0000051940Add
    BLAST

    Proteomic databases

    PaxDbiP19100.

    Structurei

    3D structure databases

    ProteinModelPortaliP19100.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Curated

    Phylogenomic databases

    eggNOGiCOG2124.
    GeneTreeiENSGT00750000117317.
    HOGENOMiHOG000036991.
    HOVERGENiHBG106944.
    KOiK00512.
    OrthoDBiEOG7RBZ85.
    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.

    P19100-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWVLLVFFLL TLTYLFWPKT KGSGAKYPRS LPVLPVVGSL PFLPRRGHQH    50
    MNFFKLQDKY GPIFSFRLGS KTTVVIGDHQ LAKEVLLKKG KEFSGRPRVM 100
    TLDILSDNQK GIAFADHGTS WQLHRKLALS TFSLFKGGNL KLENIINQEI 150
    KVLCDFLATR NGESIDLAQP LSLAMTNIVS FICFNFSFKK GDPALQAIVN 200
    FNDGILDAVG KEILYDMFPG IRILPSQTLE NMKQCVRMRN ELLREILENR 250
    KENYSRNSIT NLLDIMIQAK TNAESNTGGP DHNLKLLSDR HMLATVADIF 300
    GAGVETSASV VKWIVAFLLH YPLLRKKIQD AIDQNIGFNR APSISDRNQL 350
    VLLEATIREV LRFRPVSPTL IPHRAIIDSS IGEFTIDKDT DVVVNLWALH 400
    HNEKEWHRPD LFMPERFLDP TGTQLISPSL SYLPFGAGPR SCVGEMLARQ 450
    ELFLFTAGLL QRFDLELPDD GQLPCLVGNP SLVLQIDPFK VKIKERQAWK 500
    EAHTEGSTS 509
    Length:509
    Mass (Da):57,447
    Last modified:November 1, 1997 - v3
    Checksum:i9497D185A1B446B4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti46 – 538RGHQHMNF → FL no nucleotide entry (PubMed:3025870)Curated
    Sequence conflicti51 – 511M → I in CAA77878. (PubMed:1627653)Curated
    Sequence conflicti70 – 701S → D no nucleotide entry (PubMed:3025870)Curated
    Sequence conflicti98 – 981R → K no nucleotide entry (PubMed:3025870)Curated
    Sequence conflicti108 – 1169Missing in CAA77878. (PubMed:1627653)Curated
    Sequence conflicti117 – 1171H → E no nucleotide entry (PubMed:3025870)Curated
    Sequence conflicti126 – 14015KLALS…KGGNL → SLF no nucleotide entry (PubMed:3025870)CuratedAdd
    BLAST
    Sequence conflicti161 – 19131NGESI…SFKKG → VIQNACEMDRLKEI no nucleotide entry (PubMed:3025870)CuratedAdd
    BLAST
    Sequence conflicti196 – 1961Q → D no nucleotide entry (PubMed:3025870)Curated
    Sequence conflicti201 – 21010FNDGILDAVG → IEEGELT no nucleotide entry (PubMed:3025870)Curated
    Sequence conflicti238 – 2381M → E no nucleotide entry (PubMed:3025870)Curated
    Sequence conflicti257 – 26610NSITNLLDIM → IL no nucleotide entry (PubMed:3025870)Curated
    Sequence conflicti270 – 28415Missing no nucleotide entry (PubMed:3025870)CuratedAdd
    BLAST
    Sequence conflicti291 – 30313HMLAT…IFGAG → AC no nucleotide entry (PubMed:3025870)CuratedAdd
    BLAST
    Sequence conflicti292 – 2921M → S in CAA77878. (PubMed:1627653)Curated
    Sequence conflicti308 – 3081A → V no nucleotide entry (PubMed:3025870)Curated
    Sequence conflicti311 – 33323VKWIV…QDAID → FIWIQEAIE no nucleotide entry (PubMed:3025870)CuratedAdd
    BLAST
    Sequence conflicti319 – 3213LHY → ATLC in CAA77878. (PubMed:1627653)Curated
    Sequence conflicti330 – 3301D → E in CAA77878. (PubMed:1627653)Curated
    Sequence conflicti333 – 3331D → E in CAA77878. (PubMed:1627653)Curated
    Sequence conflicti389 – 3891D → A no nucleotide entry (PubMed:3025870)Curated
    Sequence conflicti395 – 3973NLW → SLF no nucleotide entry (PubMed:3025870)Curated
    Sequence conflicti407 – 4071H → L in AAA31008. (PubMed:1543750)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63507 mRNA. Translation: AAA31008.1.
    U41525
    , U41519, U41520, U41521, U41522, U41523, U41524 Genomic DNA. Translation: AAA84419.1.
    Z11854, Z11855, Z11856 Genomic DNA. Translation: CAA77878.1.
    PIRiS22339.
    RefSeqiNP_999593.1. NM_214428.1.
    UniGeneiSsc.51528.

    Genome annotation databases

    EnsembliENSSSCT00000011585; ENSSSCP00000011283; ENSSSCG00000010591.
    GeneIDi403330.
    KEGGissc:403330.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63507 mRNA. Translation: AAA31008.1 .
    U41525
    , U41519 , U41520 , U41521 , U41522 , U41523 , U41524 Genomic DNA. Translation: AAA84419.1 .
    Z11854 , Z11855 , Z11856 Genomic DNA. Translation: CAA77878.1 .
    PIRi S22339.
    RefSeqi NP_999593.1. NM_214428.1.
    UniGenei Ssc.51528.

    3D structure databases

    ProteinModelPortali P19100.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PaxDbi P19100.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSSSCT00000011585 ; ENSSSCP00000011283 ; ENSSSCG00000010591 .
    GeneIDi 403330.
    KEGGi ssc:403330.

    Organism-specific databases

    CTDi 1586.

    Phylogenomic databases

    eggNOGi COG2124.
    GeneTreei ENSGT00750000117317.
    HOGENOMi HOG000036991.
    HOVERGENi HBG106944.
    KOi K00512.
    OrthoDBi EOG7RBZ85.
    TreeFami TF105095.

    Enzyme and pathway databases

    UniPathwayi UPA00062 .
    Reactomei REACT_210511. Glucocorticoid biosynthesis.
    REACT_211636. Endogenous sterols.
    REACT_221517. Androgen biosynthesis.

    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

    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      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] [Europe PMC] [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] [Europe PMC] [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.

    Entry informationi

    Entry nameiCP17A_PIG
    AccessioniPrimary (citable) accession number: P19100
    Secondary accession number(s): Q29553, Q99030
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 117 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, 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