Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P70687

- CP17A_MESAU

UniProt

P70687 - CP17A_MESAU

Protein

Steroid 17-alpha-hydroxylase/17,20 lyase

Gene

CYP17A1

Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.By similarity

    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. hormone biosynthetic process Source: UniProtKB
    2. progesterone metabolic process Source: UniProtKB
    3. steroid biosynthetic process Source: UniProtKB-UniPathway
    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

    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
    OrganismiMesocricetus auratus (Golden hamster)
    Taxonomic identifieri10036 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

    Subcellular locationi

    Membrane Curated

    GO - Cellular componenti

    1. membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 511511Steroid 17-alpha-hydroxylase/17,20 lyasePRO_0000051934Add
    BLAST

    Structurei

    Secondary structure

    1
    511
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi51 – 577
    Beta strandi62 – 654
    Beta strandi74 – 763
    Turni79 – 813
    Beta strandi87 – 893
    Beta strandi91 – 933
    Helixi98 – 1036
    Turni104 – 1074
    Helixi111 – 1133
    Helixi118 – 12710
    Turni128 – 1325
    Beta strandi133 – 14210
    Helixi145 – 15713
    Helixi170 – 18415
    Helixi193 – 20311
    Helixi205 – 2084
    Turni209 – 2135
    Helixi227 – 2337
    Turni234 – 2363
    Helixi237 – 2404
    Turni241 – 2444
    Helixi245 – 2528
    Helixi260 – 27112
    Beta strandi280 – 2834
    Helixi288 – 29912
    Turni300 – 3023
    Helixi303 – 31715
    Helixi318 – 3203
    Helixi322 – 33514
    Helixi343 – 3453
    Beta strandi346 – 3483
    Helixi351 – 36313
    Beta strandi366 – 3705
    Beta strandi373 – 3775
    Beta strandi381 – 3844
    Beta strandi392 – 3943
    Helixi396 – 3994
    Helixi403 – 4053
    Beta strandi407 – 4115
    Helixi414 – 4174
    Beta strandi418 – 4214
    Turni427 – 4304
    Beta strandi434 – 4374
    Helixi444 – 4474
    Helixi449 – 46012
    Beta strandi463 – 4664
    Beta strandi470 – 4723
    Turni473 – 4753
    Beta strandi480 – 4845
    Beta strandi492 – 4954

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JO9model-A48-501[»]
    ProteinModelPortaliP70687.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Curated

    Phylogenomic databases

    HOVERGENiHBG106944.

    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.

    P70687-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWELVALLLL TLAYFFWSKS KTCGAKSPKS LPFLPLVGSL PFIPRHGHPH    50
    VNFFKLQEKY GPIYSLRLGS TTTVIIGQYQ LAKEVLVKKG KEFSGRPHMV 100
    TLGLLSDQGK GIAFADSGGS WQLHRKLALS SFALFRDGNQ KLEKIICQKA 150
    SSLCDFLLTH NEESIDLSEP IFNSITNIIC IICFGISYEN RDPILATIKS 200
    FTEGILNSLG NDHLVDIFPW LTIFPNKTVD MIKKNVKIRD EVLSGILEKC 250
    KEKFNSDSIS SLMDLLIQAK TNADNNNTSE GQGSNAFSDM HILATIADIF 300
    GAGIETTASV LSWIIAFLLH NPEVKKKIQK EIDQNIGFSR TPTFNDRNHL 350
    LMLEATIREV LRIRPVAPML IPHRANSDMS IGEFSIPKFT PVIINLWALH 400
    HSEKEWDQPD RFMPERFLDP TGSHLITPSL SYLPFGAGAR SCIGEVLARQ 450
    ELFLFMAHLL QRFDLDVPDD EQPPCLKGNA NVVFLIDPFK VKITVRQAWK 500
    DAQAEVNTWR P 511
    Length:511
    Mass (Da):57,459
    Last modified:February 1, 1997 - v1
    Checksum:i896E776A7457546C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U66494 mRNA. Translation: AAB07494.1.
    RefSeqiNP_001268860.1. NM_001281931.1.

    Genome annotation databases

    GeneIDi101831170.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U66494 mRNA. Translation: AAB07494.1 .
    RefSeqi NP_001268860.1. NM_001281931.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JO9 model - A 48-501 [» ]
    ProteinModelPortali P70687.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 101831170.

    Organism-specific databases

    CTDi 1586.

    Phylogenomic databases

    HOVERGENi HBG106944.

    Enzyme and pathway databases

    UniPathwayi UPA00062 .

    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. "Cloning and expression of hamster adrenal cytochrome P450C17 cDNA."
      Cloutier M., Fleury A., Courtemanche J., Ducharme L., Mason J.I., Lehoux J.-G.
      Ann. N. Y. Acad. Sci. 774:294-296(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Adrenal gland.

    Entry informationi

    Entry nameiCP17A_MESAU
    AccessioniPrimary (citable) accession number: P70687
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 89 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3