[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Adrenal cortex; PubMed=6589615 [NCBI, ExPASy, EBI, Israel, Japan] Morohashi K., Fujii-Kuriyama Y., Okada Y., Sogawa K., Hirose T., Inayama S., Omura T.; "Molecular cloning and nucleotide sequence of cDNA for mRNA of mitochondrial cytochrome P-450(SCC) of bovine adrenal cortex."; Proc. Natl. Acad. Sci. U.S.A. 81:4647-4651(1984).
[2]	PROTEIN SEQUENCE OF 40-520. DOI=10.1016/0167-4838(86)90176-7; PubMed=3518802 [NCBI, ExPASy, EBI, Israel, Japan] Chashchin V.L., Lapko V.N., Adamovich T.B., Lapko A.G., Kuprina N.S., Akhrem A.A.; "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."; Biochim. Biophys. Acta 871:217-223(1986).
[3]	PROTEIN SEQUENCE OF 40-54. PubMed=6654880 [NCBI, ExPASy, EBI, Israel, Japan] Ogishima T., Okada Y., Kominami S., Takemori S., Omura T.; "Partial amino acid sequences of two mitochondrial and two microsomal cytochrome P-450's from adrenal cortex."; J. Biochem. 94:1711-1714(1983).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-90. PubMed=2154474 [NCBI, ExPASy, EBI, Israel, Japan] Ahlgren R., Simpson E.R., Waterman M.R., Lund J.; "Characterization of the promoter/regulatory region of the bovine CYP11A (P-450scc) gene. Basal and cAMP-dependent expression."; J. Biol. Chem. 265:3313-3319(1990).
[5]	3D-STRUCTURE MODELING OF 40-520. DOI=10.1016/0167-4838(92)90089-V; PubMed=1477100 [NCBI, ExPASy, EBI, Israel, Japan] Vijayakumar S., Salerno J.C.; "Molecular modeling of the 3-D structure of cytochrome P-450scc."; Biochim. Biophys. Acta 1160:281-286(1992).

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.
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

K02130; AAA30488.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J05245; AAA30681.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A00189; O4BOM.

NP_788817.1; -.

3D structure databases

PDB

1SCC; Model; -; A=40-520.	[ExPASy / RCSB / EBI]
2ASA; Model; -; A=87-516.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1SCC; -.
2ASA; -.

ModBase

P00189.

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 direct assay from UniProtKB).
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 direct assay from UniProtKB).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0042359;	Biological process: vitamin D metabolic process (inferred from direct assay from UniProtKB).
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

P00189.

Genome annotation databases

Ensembl

ENSBTAG00000006934; Bos taurus. [Contig view]

GeneID

338048; -.

KEGG

bta:338048; -.

Phylogenomic databases

HOVERGEN

P00189; -.

Other

UniRef

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

Keywords

3D-structure; 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_0000003582`
`METAL`	`461 461`		`Iron (heme axial ligand).`
`CONFLICT`	`22 22`		`T -> S (in Ref. 4; AAA30681).`
`CONFLICT`	`57 57`		`N -> D (in Ref. 2; AA sequence).`
`CONFLICT`	`106 106`		`D -> N (in Ref. 2; AA sequence).`
`CONFLICT`	`197 197`		`D -> N (in Ref. 2; AA sequence).`
`HELIX`	`46 48`	`3`
`HELIX`	`58 68`	`11`
`HELIX`	`73 76`	`4`
`TURN`	`77 81`	`5`
`HELIX`	`89 91`	`3`
`HELIX`	`95 99`	`5`
`HELIX`	`100 102`	`3`
`STRAND`	`109 111`	`3`
`STRAND`	`119 121`	`3`
`TURN`	`132 134`	`3`
`HELIX`	`137 139`	`3`
`STRAND`	`141 143`	`3`
`HELIX`	`144 149`	`6`
`TURN`	`150 153`	`4`
`HELIX`	`154 157`	`4`
`HELIX`	`163 175`	`13`
`HELIX`	`178 181`	`4`
`HELIX`	`183 198`	`16`
`STRAND`	`201 204`	`4`
`HELIX`	`209 219`	`11`
`HELIX`	`223 225`	`3`
`HELIX`	`230 239`	`10`
`HELIX`	`241 247`	`7`
`STRAND`	`250 252`	`3`
`HELIX`	`253 262`	`10`
`STRAND`	`266 268`	`3`
`HELIX`	`270 290`	`21`
`STRAND`	`294 296`	`3`
`HELIX`	`297 301`	`5`
`HELIX`	`312 327`	`16`
`HELIX`	`330 342`	`13`
`HELIX`	`345 360`	`16`
`STRAND`	`364 366`	`3`
`TURN`	`372 374`	`3`
`HELIX`	`377 386`	`10`
`STRAND`	`392 395`	`4`
`STRAND`	`401 403`	`3`
`STRAND`	`406 408`	`3`
`STRAND`	`414 417`	`4`
`HELIX`	`418 423`	`6`
`TURN`	`425 427`	`3`
`STRAND`	`428 430`	`3`
`HELIX`	`445 448`	`4`
`HELIX`	`457 459`	`3`
`HELIX`	`464 481`	`18`
`STRAND`	`498 500`	`3`
`STRAND`	`507 509`	`3`
`HELIX`	`512 514`	`3`

Sequence information

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

Molecular weight: 60333 Da [This is the MW of the unprocessed precursor]

CRC64: 81C84B4AE0E70418 [This is a checksum on the sequence]

        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

P00189 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