P14137 (CP11A_RAT) 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
Synonyms:	Cyp11a, Cyp11a-1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	526 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.
Tissue specificity	Expressed in ovary, adrenal and testis. Ref.4
Induction	Induced by FSH or pregnant mare's serum gonadotropin in ovaries of estrogen-treated immature rats in vivo.
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 Reference proteome
Gene Ontology (GO)
Biological_process	Leydig cell differentiation Inferred from expression pattern PubMed 18502897. Source: RGD Schwann cell differentiation Inferred from expression pattern PubMed 18373277. Source: RGD biphenyl metabolic process Inferred from expression pattern PubMed 19071209PubMed 20356859. Source: RGD cellular response to antibiotic Inferred from expression pattern PubMed 18655822. Source: RGD cellular response to cAMP Inferred from expression pattern PubMed 17719163. Source: RGD cellular response to cadmium ion Inferred from expression pattern PubMed 17719163. Source: RGD cellular response to fibroblast growth factor stimulus Inferred from expression pattern PubMed 17494997. Source: RGD cellular response to follicle-stimulating hormone stimulus Inferred from expression pattern PubMed 20810564. Source: RGD cellular response to interleukin-1 Inferred from expression pattern PubMed 9397943PubMed 9582502. Source: RGD cellular response to lipopolysaccharide Inferred from expression pattern PubMed 20665543. Source: RGD cellular response to peptide hormone stimulus Inferred from expression pattern PubMed 19416745. Source: RGD cellular response to transforming growth factor beta stimulus Inferred from expression pattern PubMed 18511507. Source: RGD cellular response to tumor necrosis factor Inferred from expression pattern PubMed 9397943. Source: RGD cerebellum development Inferred from expression pattern PubMed 16329132. Source: RGD cholesterol metabolic process Inferred from electronic annotation. Source: UniProtKB-KW dibenzo-p-dioxin metabolic process Inferred from expression pattern PubMed 18637154. Source: RGD estrogen biosynthetic process Inferred from expression pattern PubMed 20810564. Source: RGD fractalkine metabolic process Inferred from expression pattern PubMed 18292196. Source: RGD granulosa cell differentiation Inferred from expression pattern Ref.2. Source: RGD hippocampus development Inferred from expression pattern PubMed 21047951. Source: RGD maternal process involved in female pregnancy Inferred from expression pattern PubMed 17726144. Source: RGD mating behavior Inferred from mutant phenotype PubMed 16101892. Source: RGD phenol-containing compound metabolic process Inferred from expression pattern PubMed 18191889. Source: RGD phthalate metabolic process Inferred from expression pattern PubMed 18923996. Source: RGD progesterone biosynthetic process Inferred from expression pattern PubMed 20810564. Source: RGD response to L-ascorbic acid Inferred from expression pattern PubMed 17280759. Source: RGD response to acid Inferred from expression pattern PubMed 18040670. Source: RGD response to alkaloid Inferred from expression pattern PubMed 18772241. Source: RGD response to corticosterone stimulus Inferred from expression pattern PubMed 18335507. Source: RGD response to drug Inferred from expression pattern PubMed 20144211. Source: RGD response to fungicide Inferred from expression pattern PubMed 14967917. Source: RGD response to gamma radiation Inferred from expression pattern PubMed 18046538. Source: RGD response to genistein Inferred from expression pattern PubMed 16214947. Source: RGD response to hydrogen peroxide Inferred from mutant phenotype PubMed 14635199. Source: RGD response to insecticide Inferred from expression pattern PubMed 19892000. Source: RGD response to salt stress Inferred from expression pattern PubMed 7678819. Source: RGD response to vitamin E Inferred from expression pattern PubMed 17280759. Source: RGD testosterone biosynthetic process Inferred from expression pattern PubMed 19883722. Source: RGD
Cellular_component	mitochondrial crista Inferred from direct assay PubMed 11691658. Source: RGD perikaryon Inferred from direct assay PubMed 16632873. Source: RGD
Molecular_function	cholesterol binding Inferred from mutant phenotype PubMed 16226009. Source: RGD cholesterol monooxygenase (side-chain-cleaving) activity Inferred from mutant phenotype PubMed 16226009. Source: RGD electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro 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 – 36	36	Mitochondrion
	Chain	37 – 526	490	Cholesterol side-chain cleavage enzyme, mitochondrial		PRO_0000003590
Sites
	Metal binding	459	1	Iron (heme axial ligand) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P14137 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: B2930E40018DC1EE	FASTA	526	60,586
	10 20 30 40 50 60 MLAKGLCLRS VLVKSCQPFL SPVWQGPGLA TGNGAGISST NSPRSFNEIP SPGDNGWINL 70 80 90 100 110 120 YHFLRENGTH RIHYHHMQNF QKYGPIYREK LGNMESVYIL DPKDAATLFS CEGPNPERYL 130 140 150 160 170 180 VPPWVAYHQY YQRPIGVLFK SSDAWRKDRI VLNQEVMAPD SIKNFVPLLE GVAQDFIKVL 190 200 210 220 230 240 HRRIKQQNSG KFSGDISDDL FRFAFESITS VVFGERLGML EEIVDPESQR FIDAVYQMFH 250 260 270 280 290 300 TSVPMLNMPP DLFRLFRTKT WKDHAAAWDV IFSKADEYTQ NFYWDLRQKR DFSKYPGVLY 310 320 330 340 350 360 SLLGGNKLPF KNIQANITEM LAGGVDTTSM TLQWNLYEMA HNLKVQEMLR AEVLAARRQA 370 380 390 400 410 420 QGDMAKMVQL VPLLKASIKE TLRLHPISVT LQRYIVNDLV LRNYKIPAKT LVQVASYAMG 430 440 450 460 470 480 RESSFFPNPN KFDPTRWLEK SQNTTHFRYL GFGWGVRQCL GRRIAELEMT IFLINVLENF 490 500 510 520 RIEVQSIRDV GTKFNLILMP EKPIFFNFQP LKQDLGSTMP RKGDTV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cyclic AMP-dependent and -independent regulation of cholesterol side chain cleavage cytochrome P-450 (P-450scc) in rat ovarian granulosa cells and corpora lutea. cDNA and deduced amino acid sequence of rat P-450scc." Oonk R.B., Krasnow J.S., Beattie W.G., Richards J.S. J. Biol. Chem. 264:21934-21942(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Rat cholesterol side-chain cleavage cytochrome P-450 (P-450scc) gene. Structure and regulation by cAMP in vitro." Oonk R.B., Parker K.L., Gibson J.L., Richards J.S. J. Biol. Chem. 265:22392-22401(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Ovary.
[4]	"Rat cholesterol side-chain cleavage enzyme (P-450scc): use of a cDNA probe to study the hormonal regulation of P-450scc mRNA levels in ovarian granulosa cells." McMasters K.M., Dickson L.A., Shamy R.V., Robischon K., Macdonald G.J., Moyle W.R. Gene 57:1-9(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 344-526, TISSUE SPECIFICITY. Strain: Sprague-Dawley. Tissue: Ovary.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J05156 mRNA. Translation: AAA40989.1. M63133 , M63125, M63126, M63127, M63128, M63129, M63130, M63131, M63132 Genomic DNA. Translation: AAA40958.1. BC089100 mRNA. Translation: AAH89100.1. M22615 mRNA. Translation: AAA62267.1.
IPI	IPI00325713.
PIR	A34164.
RefSeq	NP_058982.1. NM_017286.2.
UniGene	Rn.1401.
3D structure databases
ProteinModelPortal	P14137.
ModBase	Search...
Proteomic databases
PRIDE	P14137.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000010831; ENSRNOP00000010831; ENSRNOG00000008074.
GeneID	29680.
KEGG	rno:29680.
UCSC	RGD:69325. rat.
Organism-specific databases
CTD	1583.
RGD	69325. Cyp11a1.
Phylogenomic databases
eggNOG	COG2124.
GeneTree	ENSGT00550000074304.
HOGENOM	HOG000013161.
HOVERGEN	HBG051098.
InParanoid	P14137.
KO	K00498.
OrthoDB	EOG4GXFMF.
Enzyme and pathway databases
SABIO-RK	P14137.
UniPathway	UPA00229.
Gene expression databases
ArrayExpress	P14137.
Genevestigator	P14137.
GermOnline	ENSRNOG00000008074. Rattus norvegicus.
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...
Other
BindingDB	P14137.
ChEMBL	CHEMBL5246.
NextBio	610031.

Entry information

Entry name

CP11A_RAT

Accession

Primary (citable) accession number: P14137
Secondary accession number(s): Q5FWY8, Q6LDR9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	May 1, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program