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P10612 (CP11A_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

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 By similarity.

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.3
Chain40 – 520481Cholesterol side-chain cleavage enzyme, mitochondrial
PRO_0000003588

Sites

Metal binding4611Iron (heme axial ligand)

Experimental info

Sequence conflict461R → F AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
P10612 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 6C6D0D6FE34F9C33

FASTA52060,258
        10         20         30         40         50         60 
MLARGLALRS VLVKGCQPFL SAPRECPGHP RVGTGEGACI STKTPRPFSE IPSPGDNGWI 

        70         80         90        100        110        120 
NLYRFWKEKG TQKIHYHHVQ NFQKYGPIYR EKLGNLESVY IIDPEDVALL FKFEGPNPER 

       130        140        150        160        170        180 
YNIPPWVAYH QHYQKPVGVL LKKSGAWKKD RLVLNTEVMA PEAIKNFIPL LDTVSQDFVG 

       190        200        210        220        230        240 
VLHRRIKQQG SGKFSGDIRE DLFRFAFESI TNVIFGERLG MLEEIVDPEA QKFIDAVYQM 

       250        260        270        280        290        300 
FHTSVPMLNL PPDLFRLFRT KTWRDHVAAW DTIFNKAEKY TQNFYWDLRR KREFNNYPGI 

       310        320        330        340        350        360 
LYRLLGNDKL LSEDVKANVT EMLAGGVDTT SMTLQWHLYE MARSLNVQEM LREEVLNARR 

       370        380        390        400        410        420 
QAQGDTSKML QLVPLLKASI KETLRLHPIS VTLQRYLVND LVLRDYMIPA KTLVQVAVYA 

       430        440        450        460        470        480 
MGRDPAFFSN PGQFDPTRWL GKERDLIHFR NLGFGWGVRQ CVGRRIAELE MTLFLIHILE 

       490        500        510        520 
NFKVELQHFS DVDTIFNLIL MPDKPIFLVF RPFNQDPLQA 

« Hide

References

[1]"Nucleotide sequence of cytochrome P-450 cholesterol side-chain cleavage cDNA isolated from porcine testis."
Mulheron G.W., Stone R.T., Miller W.L., Wise T.H.
Nucleic Acids Res. 17:1773-1773(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[2]"Purification and properties of cytochrome P-450 (SCC) from pig testis mitochondria."
Kuwada M., Kitajima R., Suzuki H., Horie S.
Biochem. Biophys. Res. Commun. 176:1501-1508(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 41-61.
Tissue: Testis.
[3]"Purification and comparative characterization of cytochrome P-450scc from porcine adrenocortical mitochondria."
Iwahashi K., Tsubaki M., Miyatake A., Ichikawa Y.
Int. J. Biochem. 23:901-909(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 40-64.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X13768 mRNA. Translation: CAA32018.1.
PIRS03188.
RefSeqNP_999592.1. NM_214427.1.
UniGeneSsc.8776.

3D structure databases

ProteinModelPortalP10612.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID403329.
KEGGssc:403329.

Organism-specific databases

CTD1583.

Phylogenomic databases

HOVERGENHBG051098.
KOK00498.

Enzyme and pathway databases

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...

Entry information

Entry nameCP11A_PIG
AccessionPrimary (citable) accession number: P10612
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 97 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

PATHWAY comments

Index of metabolic and biosynthesis pathways