EBP
Identifiers
AliasesEBP, CDPX2, CHO2, CPX, CPXD, MEND, emopamil binding protein (sterol isomerase), cholestenol delta-isomerase, EBP cholestenol delta-isomerase
External IDsOMIM: 300205 MGI: 107822 HomoloGene: 4798 GeneCards: EBP
EC number5.3.3.5
Orthologs
SpeciesHumanMouse
Entrez

10682

13595

Ensembl

ENSG00000147155

ENSMUSG00000031168

UniProt

Q15125

P70245

RefSeq (mRNA)

NM_006579

NM_007898

RefSeq (protein)

NP_006570

NP_031924

Location (UCSC)Chr X: 48.52 – 48.53 MbChr X: 8.05 – 8.06 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse
The homodimer structure of Emopamil binding protein is shown.

Emopamil binding protein is a protein that in humans is encoded by the EBP gene, located on the X chromosome.[5] The protein is shown to have a high-affinity reception for anti-ischemic drugs, such as Emopamil, resulting in its discovery and given name. EBP has a mass of 27.3 kDa and resembles a σ-receptor that resides in the endoplasmic reticulum of various tissues as an integral membrane protein.[6]

Clinical significance

Mutations in EBP cause Conradi–Hünermann syndrome and impairs cholesterol biosynthesis.[7] Unborn males affected with EBP mutations are not expected to be liveborn, (with up to only 5% male births). Individuals, mostly female, that are liveborn with EBP mutations experience stunted growth, limb reduction and back problems. Later in life, the individual may develop cataracts along with coarse hair and hair loss.[8]

Cloning

Isolation, replication and characterization of the EBP and EBP-like protein have been performed in yeast/E. Coli strains (which lack the EBP protein in nature) to study the high-affinity drug binding effects.[6]

See also

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000147155 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000031168 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Guggenberger C, Ilgen D, Adamski J (May 2007). "Functional analysis of cholesterol biosynthesis by RNA interference". The Journal of Steroid Biochemistry and Molecular Biology. 104 (3–5): 105–109. doi:10.1016/j.jsbmb.2007.03.001. PMID 17498944. S2CID 20838858.
  6. 1 2 Hanner M, Moebius FF, Weber F, Grabner M, Striessnig J, Glossmann H (March 1995). "Phenylalkylamine Ca2+ antagonist binding protein. Molecular cloning, tissue distribution, and heterologous expression". The Journal of Biological Chemistry. 270 (13): 7551–7557. doi:10.1074/jbc.270.13.7551. PMID 7706302.
  7. Barboza-Cerda MC, Wong LJ, Martínez-de-Villarreal LE, Zhang VW, Déctor MA (July 2014). "A novel EBP c.224T>A mutation supports the existence of a male-specific disorder independent of CDPX2". American Journal of Medical Genetics. Part A. 164A (7): 1642–1647. doi:10.1002/ajmg.a.36508. PMID 24700572. S2CID 6501291.
  8. Krakow D (2018). "Chondrodysplasia Punctata". In Copel JA, D'Alton ME, Reapply WC, Feltovich H, Gratacós E, Krakow D, Odibo AO, Platt LD, Tutschek B (eds.). Obstetric Imaging: Fetal Diagnosis and Care (2nd ed.). Elsevier. pp. 259–261. doi:10.1016/b978-0-323-44548-1.00048-6. ISBN 978-0-323-44548-1.
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