Reviewed, UniProtKB/Swiss-Prot P10612 (CP11A_PIG)

Names and origin

Protein names

Recommended name:
    Cholesterol side-chain cleavage enzyme, mitochondrial
    EC=1.14.15.6
Alternative name(s):
    Cytochrome P450 11A1
    CYPXIA1
    P450(scc)
    Cholesterol desmolase

Gene names

Name:

CYP11A1

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	520 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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.
Sequence similarities	Belongs to the cytochrome P450 family.

Ontologies

Keywords
Biological process	Cholesterol metabolism Lipid metabolism Steroid metabolism Steroidogenesis
Cellular component	Membrane Mitochondrion
Domain	Transit peptide
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	C21-steroid hormone biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW cholesterol metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cholesterol monooxygenase (side-chain-cleaving) activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 39	39	Mitochondrion Ref.3
	Chain	40 – 520	481	Cholesterol side-chain cleavage enzyme, mitochondrial		PRO_0000003588
Sites
	Metal binding	461	1	Iron (heme axial ligand)
Experimental info
	Sequence conflict	46	1	R → F AA sequence Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P10612-1 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 6C6D0D6FE34F9C33	FASTA	520	60,258
	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

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: 2922297] [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: 2039527] [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: 1773895] [Abstract] Cited for: PROTEIN SEQUENCE OF 40-64.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X13768 mRNA. Translation: CAA32018.1.
PIR	S03188.
RefSeq	NP_999592.1.
UniGene	Ssc.8776
3D structure databases
HSSP	HSSP built from PDB template 1SCC based on UniProtKB P00189.
ModBase	Search...
Genome annotation databases
GeneID	403329.
KEGG	ssc:403329.
Phylogenomic databases
HOVERGEN	P10612.
Enzyme and pathway databases
BRENDA	1.14.15.6. 249.
Family and domain databases
InterPro	IPR001128. Cyt_P450. IPR017973. Cyt_P450_C. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. [Graphical view]
Gene3D	G3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHER	PTHR19383. Cyt_P450. 1 hit.
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00463. EP450I. PR00385. P450.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CP11A_PIG

Accession

Primary (citable) accession number: P10612

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	May 26, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)