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P79153

- CP11A_CAPHI

UniProt

P79153 - CP11A_CAPHI

Protein

Cholesterol side-chain cleavage enzyme, mitochondrial

Gene

CYP11A1

Organism
Capra hircus (Goat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    Catalyzes the side-chain cleavage reaction of cholesterol to pregnenolone.

    Catalytic activityi

    Cholesterol + 6 reduced adrenodoxin + 3 O2 = pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin + 4 H2O.

    Cofactori

    Heme group.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi461 – 4611Iron (heme axial ligand)By similarity

    GO - Molecular functioni

    1. cholesterol monooxygenase (side-chain-cleaving) activity Source: UniProtKB
    2. heme binding Source: UniProtKB
    3. iron ion binding Source: InterPro

    GO - Biological processi

    1. C21-steroid hormone biosynthetic process Source: UniProtKB
    2. cholesterol metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Steroidogenesis, Sterol metabolism

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00229.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cholesterol side-chain cleavage enzyme, mitochondrial (EC:1.14.15.6)
    Alternative name(s):
    CYPXIA1
    Cholesterol desmolase
    Cytochrome P450 11A1
    Cytochrome P450(scc)
    Gene namesi
    Name:CYP11A1
    OrganismiCapra hircus (Goat)
    Taxonomic identifieri9925 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeCapra

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Membrane, Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3939MitochondrionBy similarityAdd
    BLAST
    Chaini40 – 520481Cholesterol side-chain cleavage enzyme, mitochondrialPRO_0000003583Add
    BLAST

    Interactioni

    Subunit structurei

    Interacts with FDX1/adrenodoxin.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP79153.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    HOVERGENiHBG051098.
    KOiK00498.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P79153-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLARGLPLRS ALVKACPPLL NTGREGWGHH RVGTGEGAGI STRTPRPYSE    50
    IPSPGDNGWI NLYHFWRKKS SQRIHFRHIE NFQKYGPIYR EKLGNLESVY 100
    IIHPEDVAHL FKFEGSYPQR YDIPPWLAYH QYYQKPIGVL FKKSGAWKKD 150
    RVVLNTEVMA PEAIKNFIPL LNPVSQDFVS LLRKRIQQQG SGKFAGDIKE 200
    DLFHFAFESI TNVMFGERLG MLEDTVNTEA QKFIDAVYKM FHTSVPLLNL 250
    PPELYRLFRT KTWRDHVAAW DTIFNKAEKY TEIFYQDLRQ KTEFRNYPGI 300
    LYHLLKSEKM LLEDVKANIT EMLAGGVDTT SMTLQWHLYE MARSLNVQEM 350
    LREEVLNARR QAEGDISKML QMVPLLKASI KETLRLHPIS VTLQRYPESD 400
    LVLQDYLIPA KTLVQVAIYA MGRDPAFFSN PDKFDPTRWL GKDKDLIHFR 450
    NLGFGWGVRQ CVGRRIAELE MTLFLIHILE NFKIEMQQIG DVNTIFNLIL 500
    TPDKPIFLVF RPFNQDPPQA 520
    Length:520
    Mass (Da):60,418
    Last modified:May 1, 1997 - v1
    Checksum:i4FB09A3C89310317
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D50058 mRNA. Translation: BAA08776.1.
    RefSeqiNP_001274503.1. NM_001287574.1.
    UniGeneiChi.38574.

    Genome annotation databases

    GeneIDi102173131.
    KEGGichx:102173131.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D50058 mRNA. Translation: BAA08776.1 .
    RefSeqi NP_001274503.1. NM_001287574.1.
    UniGenei Chi.38574.

    3D structure databases

    ProteinModelPortali P79153.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 102173131.
    KEGGi chx:102173131.

    Phylogenomic databases

    HOVERGENi HBG051098.
    KOi K00498.

    Enzyme and pathway databases

    UniPathwayi UPA00229 .

    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. "Molecular cloning and nucleotide sequences of cDNA clones of sheep and goat adrenocortical cytochromes P450scc (CYP11A1)."
      Okuyama E., Okazaki T., Furukawa A., Wu R.-F., Ichikawa Y.
      J. Steroid Biochem. Mol. Biol. 57:179-185(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Adrenal cortex.

    Entry informationi

    Entry nameiCP11A_CAPHI
    AccessioniPrimary (citable) accession number: P79153
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 84 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

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

    External Data

    Dasty 3