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P00189 (CP11A_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:CYP11A1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

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

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Heme group. Ref.6

Pathway

Lipid metabolism; C21-steroid hormone metabolism.

Subunit structure

Interacts with FDX1/adrenodoxin By similarity.

Subcellular location

Mitochondrion membrane.

Sequence similarities

Belongs to the cytochrome P450 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3939Mitochondrion Ref.2 Ref.3
Chain40 – 520481Cholesterol side-chain cleavage enzyme, mitochondrial
PRO_0000003582

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

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P00189 [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

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] [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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K02130 mRNA. Translation: AAA30488.1.
J05245 Genomic DNA. Translation: AAA30681.1.
PIRO4BOM. A00189.
RefSeqNP_788817.1. NM_176644.2.
UniGeneBt.104995.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SCCmodel-A40-520[»]
2ASAmodel-A87-516[»]
3MZSX-ray2.50A/B/C/D41-520[»]
ProteinModelPortalP00189.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000009106.

Chemistry

BindingDBP00189.
ChEMBLCHEMBL4813.

Proteomic databases

PRIDEP00189.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID338048.
KEGGbta:338048.

Organism-specific databases

CTD1583.

Phylogenomic databases

eggNOGCOG2124.
HOGENOMHOG000013161.
HOVERGENHBG051098.
InParanoidP00189.
KOK00498.

Enzyme and pathway databases

SABIO-RKP00189.
UniPathwayUPA00229.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR00385. P450.
SUPFAMSSF48264. SSF48264. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20812499.

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: January 22, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways