P10612 (CP11A_PIG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Sus scrofa (Pig) [Reference proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › 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 + 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.

Ontologies

Keywords
Biological process	Cholesterol metabolism Lipid metabolism Steroid metabolism Steroidogenesis Sterol metabolism
Cellular component	Membrane Mitochondrion
Domain	Transit peptide
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	C21-steroid hormone biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB cholesterol metabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	mitochondrial membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cholesterol monooxygenase (side-chain-cleaving) activity Inferred from sequence or structural similarity. Source: UniProtKB electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from sequence or structural similarity. Source: UniProtKB iron ion 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 [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] [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.
PIR	S03188.
RefSeq	NP_999592.1. NM_214427.1.
UniGene	Ssc.8776.
3D structure databases
ProteinModelPortal	P10612.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	403329.
KEGG	ssc:403329.
Organism-specific databases
CTD	1583.
Phylogenomic databases
HOVERGEN	HBG051098.
KO	K00498.
Enzyme and pathway databases
UniPathway	UPA00229.
Gene expression databases
ArrayExpress	P10612.
Family and domain databases
Gene3D	1.10.630.10. 1 hit.
InterPro	IPR001128. Cyt_P450. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. [Graphical view]
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00463. EP450I. PR00385. P450.
SUPFAM	SSF48264. Cytochrome_P450. 1 hit.
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 29, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program