GLTP

GLTP
Available structures PDB Ortholog 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
Aliases	GLTP , glycolipid transfer protein
External IDs	OMIM: 608949; MGI: 1929253; HomoloGene: 41133; GeneCards: GLTP; OMA:GLTP - orthologs
Gene location (Human) Chr. Chromosome 12 (human) [1] Band 12q24.11 Start 109,850,945 bp [1] End 109,880,541 bp [1]
Gene location (Mouse) Chr. Chromosome 5 (mouse) [2] Band 5|5 F Start 114,807,459 bp [2] End 114,829,045 bp [2]
RNA expression pattern Bgee Human Mouse (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 Species Human Mouse 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 Mb Chr 5: 114.81 – 114.83 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/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. GRCh38: Ensembl release 89: ENSG00000139433 – Ensembl, May 2017
2. 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. "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.