[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Adrenal cortex; DOI=10.1016/0960-0760(95)00263-4; PubMed=8645627 [NCBI, ExPASy, EBI, Israel, Japan] Okuyama E., Okazaki T., Furukawa A., Wu R.-F., Ichikawa Y.; "Molecular cloning and nucleotide sequences of cDNA clones of sheep and goat adrenocortical cytochromes P450scc (CYP11A1)."; J. Steroid Biochem. Mol. Biol. 57:179-185(1996).
[2]	PROTEIN SEQUENCE OF 40-62. TISSUE=Adrenal cortex; DOI=10.1016/0005-2760(94)90108-2; PubMed=7948001 [NCBI, ExPASy, EBI, Israel, Japan] Miyatake A., Tsubaki M., Hori H., Ichikawa Y.; "Purification and comparative characterization of cytochrome P-450scc (CYP XIA1) from sheep adrenocortical mitochondria."; Biochim. Biophys. Acta 1215:176-182(1994).

Comments

FUNCTION: Catalyzes the side-chain cleavage reaction of cholesterol to pregnenolone.
CATALYTIC ACTIVITY: Cholesterol + reduced adrenal ferredoxin + O₂ = pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin + H₂O.
COFACTOR: Heme group (By similarity).
PATHWAY: Lipid metabolism; C21-steroid hormone metabolism .
SUBCELLULAR LOCATION: Mitochondrion membrane.
SIMILARITY: Belongs to the cytochrome P450 family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D50057; BAA08775.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001087258.1; -.

UniGene

Oar.5829

3D structure databases

HSSP

P00189; 1SCC. [HSSP ENTRY / PDB]

ModBase

P79202.

Ontologies

GO:0031966;	Cellular component: mitochondrial membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0008386;	Molecular function: cholesterol monooxygenase (side-chain-cleaving) activity (inferred from electronic annotation from EC).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0006700;	Biological process: C21-steroid hormone biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0008203;	Biological process: cholesterol metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001128; Cyt_P450.
IPR002401; Cyt_P450_E_grp-I.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.630.10; Cyt_P450; 1.

PANTHER

PTHR19383; Cyt_P450; 1.

Pfam

PF00067; p450; 1.
Pfam graphical view of domain structure.

PRINTS

PR00463; EP450I.
PR00385; P450.

PROSITE

PS00086; CYTOCHROME_P450; 1.

ProtoNet

P79202.

Genome annotation databases

GeneID

100048994; -.

Phylogenomic databases

HOVERGEN

P79202; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cholesterol metabolism; Direct protein sequencing; Heme; Iron; Lipid metabolism; Membrane; Metal-binding; Mitochondrion; Monooxygenase; Oxidoreductase; Steroid metabolism; Steroidogenesis; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 39`	`39`	`Mitochondrion.`
`CHAIN`	`40 520`	`481`	`Cytochrome P450 11A1, mitochondrial.`	`PRO_0000003591`
`METAL`	`461 461`		`Iron (heme axial ligand) (By similarity).`

Sequence information

Length: 520 AA [This is the length of the unprocessed precursor]

Molecular weight: 60357 Da [This is the MW of the unprocessed precursor]

CRC64: DF8989FB8A87E8AE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLARGLPFRS ALVKACPPLL NTGREGWGHH RVGTGEGAGI STRTPRPYSE IPSPGDNGWI 

        70         80         90        100        110        120 
NLYHFWRKKG SQRIHFHHIE NFQKYGPIYR EKLGNLESVY IIHPEGVAHL FKFEGSYPQR 

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

       190        200        210        220        230        240 
LLHKRIKQQG SGKFVGDIKE DLFRFAFESI TNVMFGERLG MLEDTVDTEA QKFIDAVYKM 

       250        260        270        280        290        300 
FHTSVPLLNL PPELYRLFRT KTWRDHVAAW DTIFNKAEKY TEIFYQDLRQ KTEFRNYPGI 

       310        320        330        340        350        360 
LYHLLKSEKM LLEDVKANIT EMLAGGVDTT SMTLQWHLYE MARSLNVQEM LRKEVLNARR 

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

       430        440        450        460        470        480 
MGRDPAFFSN PDKFDPTRWL GKDKDLIHFR NLGFGWGVRQ CVGRRIAELE MTLFLIHILE 

       490        500        510        520 
NFRVEMQQIG DVNTIFNLIL TPDKPIFLVF RPFNQGPPQA

P79202 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools