GLTP

Protein-coding gene in humans
GLTP
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1SWX, 1SX6, 2EUK, 2EUM, 2EVD, 2EVL, 2EVS, 2EVT, 3RIC, 3RWV, 3RZN, 3S0I, 3S0K, 4GH0, 4GHP, 4GHS, 4GIX, 4GJQ, 4GVT, 4GXD, 4GXG, 4H2Z

Identifiers
AliasesGLTP, glycolipid transfer protein
External IDsOMIM: 608949; MGI: 1929253; HomoloGene: 41133; GeneCards: GLTP; OMA:GLTP - orthologs
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for GLTP
Genomic location for GLTP
Band12q24.11Start109,850,945 bp[1]
End109,880,541 bp[1]
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)[2]
Chromosome 5 (mouse)
Genomic location for GLTP
Genomic location for GLTP
Band5|5 FStart114,807,459 bp[2]
End114,829,045 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • skin of arm

  • gingival epithelium

  • human penis

  • skin of thigh

  • vulva

  • mucosa of pharynx

  • oral cavity

  • skin of hip

  • nasal epithelium

  • mucosa of ileum
Top expressed in
  • skin of external ear

  • superior surface of tongue

  • epidermis

  • lip

  • transitional epithelium of urinary bladder

  • hair follicle

  • skin of back

  • esophagus

  • skin of abdomen

  • condyle
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • protein binding
  • lipid binding
  • glycolipid transfer activity
  • glycolipid binding
  • lipid transfer activity
  • identical protein binding
  • ceramide 1-phosphate binding
  • ceramide 1-phosphate transfer activity
Cellular component
  • cytoplasm
  • cytosol
  • membrane
Biological process
  • lipid transport
  • glycosphingolipid metabolic process
  • glycolipid transport
  • intermembrane lipid transfer
  • ceramide transport
  • ceramide 1-phosphate transport
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

51228

56356

Ensembl

ENSG00000139433

ENSMUSG00000011884

UniProt

Q9NZD2

Q9JL62

RefSeq (mRNA)

NM_016433

NM_019821

RefSeq (protein)

NP_057517

NP_062795

Location (UCSC)Chr 12: 109.85 – 109.88 MbChr 5: 114.81 – 114.83 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Glycolipid transfer protein is a protein that in humans is encoded by the GLTP gene.[5][6][7]

The protein encoded by this gene is similar to bovine and porcine proteins which accelerate transfer of certain glycosphingolipids and glyceroglycolipids between membranes. It is thought to be a cytoplasmic protein.[7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000139433 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000011884 – 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. ^ Li XM, Malakhova ML, Lin X, Pike HM, Chung T, Molotkovsky JG, Brown RE (Aug 2004). "Human glycolipid transfer protein: probing conformation using fluorescence spectroscopy". Biochemistry. 43 (31): 10285–94. doi:10.1021/bi0495432. PMC 2593833. PMID 15287756.
  6. ^ Malakhova ML, Malinina L, Pike HM, Kanack AT, Patel DJ, Brown RE (Jul 2005). "Point mutational analysis of the liganding site in human glycolipid transfer protein. Functionality of the complex". J Biol Chem. 280 (28): 26312–20. doi:10.1074/jbc.M500481200. PMC 1393170. PMID 15901739.
  7. ^ a b "Entrez Gene: GLTP glycolipid transfer protein".

Further reading

  • Brown RE, Mattjus P (2007). "Glycolipid transfer proteins". Biochim. Biophys. Acta. 1771 (6): 746–60. doi:10.1016/j.bbalip.2007.01.011. PMC 1986823. PMID 17320476.
  • Abe A (1990). "Primary structure of glycolipid transfer protein from pig brain". J. Biol. Chem. 265 (17): 9634–7. doi:10.1016/S0021-9258(19)38716-2. PMID 2190982.
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
  • Mattjus P, Pike HM, Molotkovsky JG, Brown RE (2000). "Charged membrane surfaces impede the protein-mediated transfer of glycosphingolipids between phospholipid bilayers". Biochemistry. 39 (5): 1067–75. doi:10.1021/bi991810u. PMC 2637181. PMID 10653652.
  • Lin X, Mattjus P, Pike HM, et al. (2000). "Cloning and expression of glycolipid transfer protein from bovine and porcine brain". J. Biol. Chem. 275 (7): 5104–10. doi:10.1074/jbc.275.7.5104. PMC 2621014. PMID 10671554.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Malinina L, Malakhova ML, Teplov A, et al. (2004). "Structural basis for glycosphingolipid transfer specificity". Nature. 430 (7003): 1048–53. Bibcode:2004Natur.430.1048M. doi:10.1038/nature02856. PMC 2640488. PMID 15329726.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Rao CS, Lin X, Pike HM, et al. (2004). "Glycolipid transfer protein mediated transfer of glycosphingolipids between membranes: a model for action based on kinetic and thermodynamic analyses". Biochemistry. 43 (43): 13805–15. doi:10.1021/bi0492197. PMC 2596630. PMID 15504043.
  • Rao CS, Chung T, Pike HM, Brown RE (2006). "Glycolipid transfer protein interaction with bilayer vesicles: modulation by changing lipid composition". Biophys. J. 89 (6): 4017–28. doi:10.1529/biophysj.105.070631. PMC 1366967. PMID 16169991.
  • Malinina L, Malakhova ML, Kanack AT, et al. (2006). "The liganding of glycolipid transfer protein is controlled by glycolipid acyl structure". PLOS Biol. 4 (11): e362. doi:10.1371/journal.pbio.0040362. PMC 1618416. PMID 17105344.
  • v
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  • e
  • 1swx: Crystal structure of a human glycolipid transfer protein in apo-form
    1swx: Crystal structure of a human glycolipid transfer protein in apo-form
  • 1sx6: Crystal structure of human Glycolipid Transfer protein in lactosylceramide-bound form
    1sx6: Crystal structure of human Glycolipid Transfer protein in lactosylceramide-bound form
  • 1tfj: Crystal structure of Bovine Glycolipid transfer protein in complex with a fatty acid
    1tfj: Crystal structure of Bovine Glycolipid transfer protein in complex with a fatty acid
  • 1wbe: X-RAY STRUCTURE OF BOVINE GLTP
    1wbe: X-RAY STRUCTURE OF BOVINE GLTP
  • 2bv7: CRYSTAL STRUCTURE OF GLTP WITH BOUND GM3
    2bv7: CRYSTAL STRUCTURE OF GLTP WITH BOUND GM3
  • 2euk: Crystal Structure of Human Glycolipid Transfer Protein complexed with 24:1 Galactosylceramide
    2euk: Crystal Structure of Human Glycolipid Transfer Protein complexed with 24:1 Galactosylceramide
  • 2eum: Crystal structure of human Glycolipid Transfer Protein complexed with 8:0 Lactosylceramide
    2eum: Crystal structure of human Glycolipid Transfer Protein complexed with 8:0 Lactosylceramide
  • 2evd: Crystal structure of human Glycolipid Transfer Protein complexed with 12:0 Lactosylceramide
    2evd: Crystal structure of human Glycolipid Transfer Protein complexed with 12:0 Lactosylceramide
  • 2evl: Crystal structure of human Glycolipid Transfer Protein complexed with 18:2 Galactosylceramide
    2evl: Crystal structure of human Glycolipid Transfer Protein complexed with 18:2 Galactosylceramide
  • 2evs: Crystal structure of human Glycolipid Transfer Protein complexed with n-hexyl-beta-D-glucoside
    2evs: Crystal structure of human Glycolipid Transfer Protein complexed with n-hexyl-beta-D-glucoside
  • 2evt: Crystal structure of D48V mutant of human Glycolipid Transfer Protein
    2evt: Crystal structure of D48V mutant of human Glycolipid Transfer Protein


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