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P00189

- CP11A_BOVIN

UniProt

P00189 - CP11A_BOVIN

Protein

Cholesterol side-chain cleavage enzyme, mitochondrial

Gene

CYP11A1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      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.1 Publication

    Pathwayi

    Sites

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

    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
    3. vitamin D 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

    SABIO-RKP00189.
    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
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial membrane Source: UniProtKB-SubCell
    2. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Membrane, Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3939Mitochondrion2 PublicationsAdd
    BLAST
    Chaini40 – 520481Cholesterol side-chain cleavage enzyme, mitochondrialPRO_0000003582Add
    BLAST

    Proteomic databases

    PRIDEiP00189.

    Interactioni

    Subunit structurei

    Interacts with FDX1/adrenodoxin.By similarity

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000009106.

    Structurei

    Secondary structure

    1
    520
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi48 – 503
    Helixi58 – 6811
    Helixi70 – 723
    Helixi74 – 8512
    Beta strandi87 – 904
    Beta strandi99 – 1013
    Helixi104 – 1129
    Helixi124 – 13310
    Turni139 – 1413
    Helixi145 – 15814
    Turni161 – 1677
    Helixi168 – 18922
    Beta strandi190 – 1923
    Beta strandi194 – 1963
    Helixi199 – 21517
    Beta strandi223 – 2253
    Helixi229 – 24214
    Helixi243 – 2475
    Helixi252 – 2543
    Helixi255 – 2584
    Helixi260 – 28930
    Helixi300 – 3067
    Helixi312 – 34332
    Helixi345 – 35511
    Turni356 – 3627
    Helixi366 – 3694
    Helixi374 – 38613
    Beta strandi389 – 3913
    Beta strandi393 – 3953
    Beta strandi401 – 4088
    Beta strandi414 – 4163
    Helixi418 – 4236
    Turni425 – 4273
    Beta strandi428 – 4303
    Helixi436 – 4405
    Beta strandi446 – 4494
    Helixi457 – 4593
    Helixi464 – 47916
    Beta strandi485 – 4884
    Beta strandi494 – 50411
    Beta strandi508 – 5103

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SCCmodel-A40-520[»]
    2ASAmodel-A87-516[»]
    3MZSX-ray2.50A/B/C/D41-520[»]
    ProteinModelPortaliP00189.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG2124.
    HOGENOMiHOG000013161.
    HOVERGENiHBG051098.
    InParanoidiP00189.
    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.

    P00189-1 [UniParc]FASTAAdd to Basket

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    MLARGLPLRS ALVKACPPIL STVGEGWGHH RVGTGEGAGI STKTPRPYSE    50
    IPSPGDNGWL NLYHFWREKG SQRIHFRHIE NFQKYGPIYR EKLGNLESVY 100
    IIHPEDVAHL FKFEGSYPER YDIPPWLAYH RYYQKPIGVL FKKSGTWKKD 150
    RVVLNTEVMA PEAIKNFIPL LNPVSQDFVS LLHKRIKQQG SGKFVGDIKE 200
    DLFHFAFESI TNVMFGERLG MLEETVNPEA QKFIDAVYKM FHTSVPLLNV 250
    PPELYRLFRT KTWRDHVAAW DTIFNKAEKY TEIFYQDLRR KTEFRNYPGI 300
    LYCLLKSEKM LLEDVKANIT EMLAGGVNTT SMTLQWHLYE MARSLNVQEM 350
    LREEVLNARR QAEGDISKML QMVPLLKASI KETLRLHPIS VTLQRYPESD 400
    LVLQDYLIPA KTLVQVAIYA MGRDPAFFSS PDKFDPTRWL SKDKDLIHFR 450
    NLGFGWGVRQ CVGRRIAELE MTLFLIHILE NFKVEMQHIG DVDTIFNLIL 500
    TPDKPIFLVF RPFNQDPPQA 520
    Length:520
    Mass (Da):60,333
    Last modified:July 21, 1986 - v1
    Checksum:i81C84B4AE0E70418
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 221T → S in AAA30681. (PubMed:2154474)Curated
    Sequence conflicti57 – 571N → D AA sequence (PubMed:3518802)Curated
    Sequence conflicti106 – 1061D → N AA sequence (PubMed:3518802)Curated
    Sequence conflicti197 – 1971D → N AA sequence (PubMed:3518802)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02130 mRNA. Translation: AAA30488.1.
    J05245 Genomic DNA. Translation: AAA30681.1.
    PIRiA00189. O4BOM.
    RefSeqiNP_788817.1. NM_176644.2.
    UniGeneiBt.104995.

    Genome annotation databases

    GeneIDi338048.
    KEGGibta:338048.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02130 mRNA. Translation: AAA30488.1 .
    J05245 Genomic DNA. Translation: AAA30681.1 .
    PIRi A00189. O4BOM.
    RefSeqi NP_788817.1. NM_176644.2.
    UniGenei Bt.104995.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SCC model - A 40-520 [» ]
    2ASA model - A 87-516 [» ]
    3MZS X-ray 2.50 A/B/C/D 41-520 [» ]
    ProteinModelPortali P00189.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000009106.

    Chemistry

    BindingDBi P00189.
    ChEMBLi CHEMBL4813.

    Proteomic databases

    PRIDEi P00189.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 338048.
    KEGGi bta:338048.

    Organism-specific databases

    CTDi 1583.

    Phylogenomic databases

    eggNOGi COG2124.
    HOGENOMi HOG000013161.
    HOVERGENi HBG051098.
    InParanoidi P00189.
    KOi K00498.

    Enzyme and pathway databases

    UniPathwayi UPA00229 .
    SABIO-RK P00189.

    Miscellaneous databases

    NextBioi 20812499.

    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 sequence of cDNA for mRNA of mitochondrial cytochrome P-450(SCC) of bovine adrenal cortex."
      Morohashi K., Fujii-Kuriyama Y., Okada Y., Sogawa K., Hirose T., Inayama S., Omura T.
      Proc. Natl. Acad. Sci. U.S.A. 81:4647-4651(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Adrenal cortex.
    2. "Primary structure of the cholesterol side-chain cleavage cytochrome P-450 from bovine adrenocortical mitochondria and some aspects of its functioning on a structural level."
      Chashchin V.L., Lapko V.N., Adamovich T.B., Lapko A.G., Kuprina N.S., Akhrem A.A.
      Biochim. Biophys. Acta 871:217-223(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 40-520.
    3. "Partial amino acid sequences of two mitochondrial and two microsomal cytochrome P-450's from adrenal cortex."
      Ogishima T., Okada Y., Kominami S., Takemori S., Omura T.
      J. Biochem. 94:1711-1714(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 40-54.
    4. "Characterization of the promoter/regulatory region of the bovine CYP11A (P-450scc) gene. Basal and cAMP-dependent expression."
      Ahlgren R., Simpson E.R., Waterman M.R., Lund J.
      J. Biol. Chem. 265:3313-3319(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-90.
    5. "Molecular modeling of the 3-D structure of cytochrome P-450scc."
      Vijayakumar S., Salerno J.C.
      Biochim. Biophys. Acta 1160:281-286(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF 40-520.
    6. "Structural basis for three-step sequential catalysis by the cholesterol side chain cleavage enzyme CYP11A1."
      Mast N., Annalora A.J., Lodowski D.T., Palczewski K., Stout C.D., Pikuleva I.A.
      J. Biol. Chem. 286:5607-5613(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 41-520 IN COMPLEX WITH HEME AND 22R-HYDROXYCHOLESTEROL, COFACTOR.

    Entry informationi

    Entry nameiCP11A_BOVIN
    AccessioniPrimary (citable) accession number: P00189
    Secondary accession number(s): Q28152
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 116 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, Complete proteome, Direct protein sequencing, Reference proteome

    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