P79153 (CP11A_CAPHI) 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

Capra hircus (Goat)

Taxonomic identifier

9925 [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 › Ruminantia › Pecora › Bovidae › Caprinae › Capra

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 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.
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
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 By similarity
	Chain	40 – 520	481	Cholesterol side-chain cleavage enzyme, mitochondrial		PRO_0000003583
Sites
	Metal binding	461	1	Iron (heme axial ligand) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P79153 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 4FB09A3C89310317	FASTA	520	60,418
	10 20 30 40 50 60 MLARGLPLRS ALVKACPPLL NTGREGWGHH RVGTGEGAGI STRTPRPYSE IPSPGDNGWI 70 80 90 100 110 120 NLYHFWRKKS SQRIHFRHIE NFQKYGPIYR EKLGNLESVY IIHPEDVAHL FKFEGSYPQR 130 140 150 160 170 180 YDIPPWLAYH QYYQKPIGVL FKKSGAWKKD RVVLNTEVMA PEAIKNFIPL LNPVSQDFVS 190 200 210 220 230 240 LLRKRIQQQG SGKFAGDIKE DLFHFAFESI TNVMFGERLG MLEDTVNTEA QKFIDAVYKM 250 260 270 280 290 300 FHTSVPLLNL PPELYRLFRT KTWRDHVAAW DTIFNKAEKY TEIFYQDLRQ KTEFRNYPGI 310 320 330 340 350 360 LYHLLKSEKM LLEDVKANIT EMLAGGVDTT SMTLQWHLYE MARSLNVQEM LREEVLNARR 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 NFKIEMQQIG DVNTIFNLIL TPDKPIFLVF RPFNQDPPQA

References

[1]

"Molecular cloning and nucleotide sequences of cDNA clones of sheep and goat adrenocortical cytochromes P450scc (CYP11A1)." Okuyama E., Okazaki T., Furukawa A., Wu R.-F., Ichikawa Y. J. Steroid Biochem. Mol. Biol. 57:179-185(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Adrenal cortex.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D50058 mRNA. Translation: BAA08776.1.
3D structure databases
ProteinModelPortal	P79153.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG051098.
Enzyme and pathway databases
UniPathway	UPA00229.
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_CAPHI

Accession

Primary (citable) accession number: P79153

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	May 1, 1997
Last modified:	May 29, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program