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Reviewed, UniProtKB/Swiss-Prot P00189 (CP11A_BOVIN)

Last modified July 22, 2008. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Cytochrome P450 11A1, mitochondrial
    EC=1.14.15.6
Alternative name(s):
    CYPXIA1
    Cholesterol side-chain cleavage enzyme
    P450(scc)
    Cholesterol desmolase
Gene names
Name: CYP11A1
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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

Catalytic activity

Cholesterol + reduced adrenal ferredoxin + O(2) = pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin + H(2)O.

Cofactor

Heme group.

Pathway

Lipid metabolism; C21-steroid hormone metabolism.

Subcellular location

Mitochondrion membrane.

Sequence similarities

Belongs to the cytochrome P450 family.

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Ontologies

Keywords

   Biological processCholesterol metabolism
Lipid metabolism
Steroid metabolism
Steroidogenesis
   Cellular componentMembrane
Mitochondrion
   DomainTransit peptide
   LigandHeme
Iron
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   Technical term3D-structure
Direct protein sequencing

Gene Ontology (GO)

   Biological processcholesterol metabolic process

Inferred from direct assay. Source: UniProtKB

vitamin D metabolic process

Inferred from direct assay. Source: UniProtKB

   Cellular componentmitochondrion

Inferred from direct assay. Source: UniProtKB

   Molecular functioncholesterol monooxygenase (side-chain-cleaving) activity

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Transit peptide1 – 3939Mitochondrion
Chain40 – 520481Cytochrome P450 11A1, mitochondrial

Sites

Metal binding4611Iron (heme axial ligand)

Experimental info

Sequence conflict221T → S in AAA30681. Ref.4
Sequence conflict571N → D AA sequence Ref.2
Sequence conflict1061D → N AA sequence Ref.2
Sequence conflict1971D → N AA sequence Ref.2

Secondary structure

1 ........................................................................................ 520
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P00189-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 81C84B4AE0E70418

FASTA52060,333
        10         20         30         40         50         60 
MLARGLPLRS ALVKACPPIL STVGEGWGHH RVGTGEGAGI STKTPRPYSE IPSPGDNGWL 

        70         80         90        100        110        120 
NLYHFWREKG SQRIHFRHIE NFQKYGPIYR EKLGNLESVY IIHPEDVAHL FKFEGSYPER 

       130        140        150        160        170        180 
YDIPPWLAYH RYYQKPIGVL FKKSGTWKKD RVVLNTEVMA PEAIKNFIPL LNPVSQDFVS 

       190        200        210        220        230        240 
LLHKRIKQQG SGKFVGDIKE DLFHFAFESI TNVMFGERLG MLEETVNPEA QKFIDAVYKM 

       250        260        270        280        290        300 
FHTSVPLLNV PPELYRLFRT KTWRDHVAAW DTIFNKAEKY TEIFYQDLRR KTEFRNYPGI 

       310        320        330        340        350        360 
LYCLLKSEKM LLEDVKANIT EMLAGGVNTT SMTLQWHLYE MARSLNVQEM LREEVLNARR 

       370        380        390        400        410        420 
QAEGDISKML QMVPLLKASI KETLRLHPIS VTLQRYPESD LVLQDYLIPA KTLVQVAIYA 

       430        440        450        460        470        480 
MGRDPAFFSS PDKFDPTRWL SKDKDLIHFR NLGFGWGVRQ CVGRRIAELE MTLFLIHILE 

       490        500        510        520 
NFKVEMQHIG DVDTIFNLIL TPDKPIFLVF RPFNQDPPQA

« Hide

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References

[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: 6589615] [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: 3518802] [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: 6654880] [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: 2154474] [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: 1477100] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF 40-520.

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Cross-references

Sequence databases

K02130 mRNA. Translation: AAA30488.1.
J05245 Genomic DNA. Translation: AAA30681.1.
PIRO4BOM. A00189.
RefSeqNP_788817.1.
UniGeneBt.7190

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1SCCmodel-A40-520[»]
2ASAmodel-A87-516[»]
ModBaseSearch...

Genome annotation databases

EnsemblENSBTAG00000006934. Bos taurus. [Contig view]
GeneID338048.
KEGGbta:338048.

Phylogenomic databases

HOVERGENP00189.

Family and domain databases

InterProIPR001128. Cyt_P450.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
Gene3DG3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHERPTHR19383. Cyt_P450. 1 hit.
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR00385. P450.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProDomP00189.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

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Entry information

Entry nameCP11A_BOVIN
AccessionPrimary (citable) accession number: P00189
Secondary accession number(s): Q28152
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 22, 2008
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents