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Protein

Cholesterol side-chain cleavage enzyme, mitochondrial

Gene

CYP11A1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the side-chain cleavage reaction of cholesterol to pregnenolone.By similarity

Catalytic activityi

Cholesterol + 6 reduced adrenodoxin + 3 O2 + 6 H+ = pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin + 4 H2O.By similarity

Cofactori

heme1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi461 – 4611Iron (heme axial ligand)

GO - Molecular functioni

  1. cholesterol monooxygenase (side-chain-cleaving) activity Source: UniProtKB
  2. heme binding Source: UniProtKB
  3. iron ion binding Source: InterPro

GO - Biological processi

  1. C21-steroid hormone biosynthetic process Source: UniProtKB
  2. cholesterol metabolic process Source: UniProtKB
  3. vitamin D metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Steroidogenesis, Sterol metabolism

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.14.15.6. 908.
SABIO-RKP00189.
UniPathwayiUPA00229.

Names & Taxonomyi

Protein namesi
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 namesi
Name:CYP11A1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial membrane Source: UniProtKB-SubCell
  2. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3939Mitochondrion2 PublicationsAdd
BLAST
Chaini40 – 520481Cholesterol side-chain cleavage enzyme, mitochondrialPRO_0000003582Add
BLAST

Proteomic databases

PRIDEiP00189.

Interactioni

Subunit structurei

Interacts with FDX1/adrenodoxin.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000009106.

Structurei

Secondary structure

1
520
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi48 – 503Combined sources
Helixi58 – 6811Combined sources
Helixi70 – 723Combined sources
Helixi74 – 8512Combined sources
Beta strandi87 – 904Combined sources
Beta strandi99 – 1013Combined sources
Helixi104 – 1129Combined sources
Helixi124 – 13310Combined sources
Turni139 – 1413Combined sources
Helixi145 – 15814Combined sources
Turni161 – 1677Combined sources
Helixi168 – 18922Combined sources
Beta strandi190 – 1923Combined sources
Beta strandi194 – 1963Combined sources
Helixi199 – 21517Combined sources
Beta strandi223 – 2253Combined sources
Helixi229 – 24214Combined sources
Helixi243 – 2475Combined sources
Helixi252 – 2543Combined sources
Helixi255 – 2584Combined sources
Helixi260 – 28930Combined sources
Helixi300 – 3067Combined sources
Helixi312 – 34332Combined sources
Helixi345 – 35511Combined sources
Turni356 – 3627Combined sources
Helixi366 – 3694Combined sources
Helixi374 – 38613Combined sources
Beta strandi389 – 3913Combined sources
Beta strandi393 – 3953Combined sources
Beta strandi401 – 4088Combined sources
Beta strandi414 – 4163Combined sources
Helixi418 – 4236Combined sources
Turni425 – 4273Combined sources
Beta strandi428 – 4303Combined sources
Helixi436 – 4405Combined sources
Beta strandi446 – 4494Combined sources
Helixi457 – 4593Combined sources
Helixi464 – 47916Combined sources
Beta strandi485 – 4884Combined sources
Beta strandi494 – 50411Combined sources
Beta strandi508 – 5103Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SCCmodel-A40-520[»]
2ASAmodel-A87-516[»]
3MZSX-ray2.50A/B/C/D41-520[»]
ProteinModelPortaliP00189.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG2124.
HOGENOMiHOG000013161.
HOVERGENiHBG051098.
InParanoidiP00189.
KOiK00498.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00189-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLARGLPLRS ALVKACPPIL STVGEGWGHH RVGTGEGAGI STKTPRPYSE
60 70 80 90 100
IPSPGDNGWL NLYHFWREKG SQRIHFRHIE NFQKYGPIYR EKLGNLESVY
110 120 130 140 150
IIHPEDVAHL FKFEGSYPER YDIPPWLAYH RYYQKPIGVL FKKSGTWKKD
160 170 180 190 200
RVVLNTEVMA PEAIKNFIPL LNPVSQDFVS LLHKRIKQQG SGKFVGDIKE
210 220 230 240 250
DLFHFAFESI TNVMFGERLG MLEETVNPEA QKFIDAVYKM FHTSVPLLNV
260 270 280 290 300
PPELYRLFRT KTWRDHVAAW DTIFNKAEKY TEIFYQDLRR KTEFRNYPGI
310 320 330 340 350
LYCLLKSEKM LLEDVKANIT EMLAGGVNTT SMTLQWHLYE MARSLNVQEM
360 370 380 390 400
LREEVLNARR QAEGDISKML QMVPLLKASI KETLRLHPIS VTLQRYPESD
410 420 430 440 450
LVLQDYLIPA KTLVQVAIYA MGRDPAFFSS PDKFDPTRWL SKDKDLIHFR
460 470 480 490 500
NLGFGWGVRQ CVGRRIAELE MTLFLIHILE NFKVEMQHIG DVDTIFNLIL
510 520
TPDKPIFLVF RPFNQDPPQA
Length:520
Mass (Da):60,333
Last modified:July 20, 1986 - v1
Checksum:i81C84B4AE0E70418
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221T → S in AAA30681 (PubMed:2154474).Curated
Sequence conflicti57 – 571N → D AA sequence (PubMed:3518802).Curated
Sequence conflicti106 – 1061D → N AA sequence (PubMed:3518802).Curated
Sequence conflicti197 – 1971D → N AA sequence (PubMed:3518802).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02130 mRNA. Translation: AAA30488.1.
J05245 Genomic DNA. Translation: AAA30681.1.
PIRiA00189. O4BOM.
RefSeqiNP_788817.1. NM_176644.2.
UniGeneiBt.104995.

Genome annotation databases

GeneIDi338048.
KEGGibta:338048.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02130 mRNA. Translation: AAA30488.1.
J05245 Genomic DNA. Translation: AAA30681.1.
PIRiA00189. O4BOM.
RefSeqiNP_788817.1. NM_176644.2.
UniGeneiBt.104995.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SCCmodel-A40-520[»]
2ASAmodel-A87-516[»]
3MZSX-ray2.50A/B/C/D41-520[»]
ProteinModelPortaliP00189.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000009106.

Chemistry

BindingDBiP00189.
ChEMBLiCHEMBL4813.

Proteomic databases

PRIDEiP00189.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi338048.
KEGGibta:338048.

Organism-specific databases

CTDi1583.

Phylogenomic databases

eggNOGiCOG2124.
HOGENOMiHOG000013161.
HOVERGENiHBG051098.
InParanoidiP00189.
KOiK00498.

Enzyme and pathway databases

UniPathwayiUPA00229.
BRENDAi1.14.15.6. 908.
SABIO-RKP00189.

Miscellaneous databases

NextBioi20812499.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1983) [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(1985) [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(1982) [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(1989) [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(1991) [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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 41-520 IN COMPLEX WITH HEME AND 22R-HYDROXYCHOLESTEROL, COFACTOR.

Entry informationi

Entry nameiCP11A_BOVIN
AccessioniPrimary (citable) accession number: P00189
Secondary accession number(s): Q28152
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 20, 1986
Last sequence update: July 20, 1986
Last modified: March 31, 2015
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.