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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: C21-steroid hormone metabolism

This protein is involved in the pathway C21-steroid hormone metabolism, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway C21-steroid hormone metabolism and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi461Iron (heme axial ligand)1

GO - Molecular functioni

GO - Biological processi

  • C21-steroid hormone biosynthetic process Source: UniProtKB
  • cholesterol metabolic process Source: UniProtKB
  • vitamin D metabolic process Source: UniProtKB

Keywordsi

Molecular functionMonooxygenase, Oxidoreductase
Biological processCholesterol metabolism, Lipid metabolism, Steroid metabolism, Steroidogenesis, Sterol metabolism
LigandHeme, Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.14.15.6. 908.
SABIO-RKiP00189.
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
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane, Mitochondrion

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4813.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 39Mitochondrion2 PublicationsAdd BLAST39
ChainiPRO_000000358240 – 520Cholesterol side-chain cleavage enzyme, mitochondrialAdd BLAST481

Proteomic databases

PaxDbiP00189.
PRIDEiP00189.

Interactioni

Subunit structurei

Interacts with FDX1/adrenodoxin.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000009106.

Chemistry databases

BindingDBiP00189.

Structurei

Secondary structure

1520
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi48 – 50Combined sources3
Helixi58 – 68Combined sources11
Helixi70 – 72Combined sources3
Helixi74 – 85Combined sources12
Beta strandi87 – 90Combined sources4
Beta strandi99 – 101Combined sources3
Helixi104 – 112Combined sources9
Helixi124 – 133Combined sources10
Turni139 – 141Combined sources3
Helixi145 – 158Combined sources14
Turni161 – 167Combined sources7
Helixi168 – 189Combined sources22
Beta strandi190 – 192Combined sources3
Beta strandi194 – 196Combined sources3
Helixi199 – 215Combined sources17
Beta strandi223 – 225Combined sources3
Helixi229 – 242Combined sources14
Helixi243 – 247Combined sources5
Helixi252 – 254Combined sources3
Helixi255 – 258Combined sources4
Helixi260 – 289Combined sources30
Helixi300 – 306Combined sources7
Helixi312 – 343Combined sources32
Helixi345 – 355Combined sources11
Turni356 – 362Combined sources7
Helixi366 – 369Combined sources4
Helixi374 – 386Combined sources13
Beta strandi389 – 391Combined sources3
Beta strandi393 – 395Combined sources3
Beta strandi401 – 408Combined sources8
Beta strandi414 – 416Combined sources3
Helixi418 – 423Combined sources6
Turni425 – 427Combined sources3
Beta strandi428 – 430Combined sources3
Helixi436 – 440Combined sources5
Beta strandi446 – 449Combined sources4
Helixi457 – 459Combined sources3
Helixi464 – 479Combined sources16
Beta strandi485 – 488Combined sources4
Beta strandi494 – 504Combined sources11
Beta strandi508 – 510Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SCCmodel-A40-520[»]
2ASAmodel-A87-516[»]
3MZSX-ray2.50A/B/C/D41-520[»]
ProteinModelPortaliP00189.
SMRiP00189.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0159. Eukaryota.
COG2124. LUCA.
HOGENOMiHOG000013161.
HOVERGENiHBG051098.
InParanoidiP00189.
KOiK00498.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiView protein in InterPro
IPR033283. CYP11A1.
IPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
IPR036396. Cyt_P450_sf.
PANTHERiPTHR24279:SF3. PTHR24279:SF3. 1 hit.
PfamiView protein in Pfam
PF00067. p450. 1 hit.
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiView protein in PROSITE
PS00086. CYTOCHROME_P450. 1 hit.

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 21, 1986 - v1
Checksum:i81C84B4AE0E70418
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti22T → S in AAA30681 (PubMed:2154474).Curated1
Sequence conflicti57N → D AA sequence (PubMed:3518802).Curated1
Sequence conflicti106D → N AA sequence (PubMed:3518802).Curated1
Sequence conflicti197D → N AA sequence (PubMed:3518802).Curated1

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.

Similar proteinsi

Entry informationi

Entry nameiCP11A_BOVIN
AccessioniPrimary (citable) accession number: P00189
Secondary accession number(s): Q28152
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 25, 2017
This is version 132 of the entry and version 1 of the sequence. See 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