P00189 (CP11A_BOVIN) 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

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [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 › Bovinae › Bos

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.
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	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	C21-steroid hormone metabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway cholesterol metabolic process Inferred from direct assay PubMed 14657394. Source: UniProtKB steroid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW vitamin D metabolic process Inferred from direct assay PubMed 16817851. Source: UniProtKB
Cellular_component	mitochondrial membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay PubMed 16817851. Source: UniProtKB
Molecular_function	cholesterol monooxygenase (side-chain-cleaving) activity Inferred from direct assay PubMed 14657394. Source: UniProtKB 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 – 39

39

Mitochondrion Ref.2 Ref.3

Chain

40 – 520

481

Cholesterol side-chain cleavage enzyme, mitochondrial

PRO_0000003582

Sites

Metal binding

461

1

Iron (heme axial ligand)

Experimental info

Sequence conflict

22

1

T → S in AAA30681. Ref.4

Sequence conflict

57

1

N → D AA sequence Ref.2

Sequence conflict

106

1

D → N AA sequence Ref.2

Sequence conflict

197

1

D → N AA sequence Ref.2

Secondary structure

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520

Helix Strand Turn

Details...

Helix

48 – 50

3

Helix

58 – 68

11

Helix

70 – 72

3

Helix

74 – 85

12

Beta strand

87 – 90

4

Beta strand

99 – 101

3

Helix

104 – 112

9

Helix

124 – 133

10

Turn

139 – 141

3

Helix

145 – 158

14

Turn

161 – 167

7

Helix

168 – 189

22

Beta strand

190 – 192

3

Beta strand

194 – 196

3

Helix

199 – 215

17

Beta strand

223 – 225

3

Helix

229 – 242

14

Helix

243 – 247

5

Helix

252 – 254

3

Helix

255 – 258

4

Helix

260 – 289

30

Helix

300 – 306

7

Helix

312 – 343

32

Helix

345 – 355

11

Turn

356 – 362

7

Helix

366 – 369

4

Helix

374 – 386

13

Beta strand

389 – 391

3

Beta strand

393 – 395

3

Beta strand

401 – 408

8

Beta strand

414 – 416

3

Helix

418 – 423

6

Turn

425 – 427

3

Beta strand

428 – 430

3

Helix

436 – 440

5

Beta strand

446 – 449

4

Helix

457 – 459

3

Helix

464 – 479

16

Beta strand

485 – 488

4

Beta strand

494 – 504

11

Beta strand

508 – 510

3

Sequences

	Sequence		Length	Mass (Da)
	P00189 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 81C84B4AE0E70418	FASTA	520	60,333
	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

References

[1]	"Molecular cloning and nucleotide sequence of cDNA for mRNA of mitochondrial cytochrome P-450(SCC) of bovine adrenal cortex." Morohashi K., Fujii-Kuriyama Y., Okada Y., Sogawa K., Hirose T., Inayama S., Omura T. Proc. Natl. Acad. Sci. U.S.A. 81:4647-4651(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Adrenal cortex.
[2]	"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." Chashchin V.L., Lapko V.N., Adamovich T.B., Lapko A.G., Kuprina N.S., Akhrem A.A. Biochim. Biophys. Acta 871:217-223(1986) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 40-520.
[3]	"Partial amino acid sequences of two mitochondrial and two microsomal cytochrome P-450's from adrenal cortex." Ogishima T., Okada Y., Kominami S., Takemori S., Omura T. J. Biochem. 94:1711-1714(1983) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 40-54.
[4]	"Characterization of the promoter/regulatory region of the bovine CYP11A (P-450scc) gene. Basal and cAMP-dependent expression." Ahlgren R., Simpson E.R., Waterman M.R., Lund J. J. Biol. Chem. 265:3313-3319(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-90.
[5]	"Molecular modeling of the 3-D structure of cytochrome P-450scc." Vijayakumar S., Salerno J.C. Biochim. Biophys. Acta 1160:281-286(1992) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 40-520.
[6]	"Structural basis for three-step sequential catalysis by the cholesterol side chain cleavage enzyme CYP11A1." Mast N., Annalora A.J., Lodowski D.T., Palczewski K., Stout C.D., Pikuleva I.A. J. Biol. Chem. 286:5607-5613(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 41-520 IN COMPLEX WITH HEME AND 22R-HYDROXYCHOLESTEROL, COFACTOR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

K02130 mRNA. Translation: AAA30488.1.
J05245 Genomic DNA. Translation: AAA30681.1.

IPI

IPI00695101.

PIR

O4BOM. A00189.

RefSeq

NP_788817.1. NM_176644.2.

UniGene

Bt.104995.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SCC	model	-	A	40-520	[»]
2ASA	model	-	A	87-516	[»]
3MZS	X-ray	2.50	A/B/C/D	41-520	[»]

ProteinModelPortal

P00189.

ModBase

Search...

Protein-protein interaction databases

STRING

9913.ENSBTAP00000009106.

Proteomic databases

PRIDE

P00189.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

338048.

KEGG

bta:338048.

Organism-specific databases

CTD

1583.

Phylogenomic databases

eggNOG

COG2124.

HOGENOM

HOG000013161.

HOVERGEN

HBG051098.

InParanoid

P00189.

KO

K00498.

OrthoDB

EOG4GXFMF.

Enzyme and pathway databases

SABIO-RK

P00189.

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...

Other

BindingDB

P00189.

ChEMBL

CHEMBL4813.

NextBio

20812499.

Entry information

Entry name

CP11A_BOVIN

Accession

Primary (citable) accession number: P00189
Secondary accession number(s): Q28152

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 1, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program