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19  structures 261  species 1  interaction 702  sequences 10  architectures

Family: GLTP (PF08718)

Summary: Glycolipid transfer protein (GLTP)

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This is the Wikipedia entry entitled "Glycolipid transfer protein". More...

Glycolipid transfer protein Edit Wikipedia article

Glycolipid transfer protein (GLTP)
PDB 1swx EBI.jpg
Symbol GLTP
Pfam PF08718
InterPro IPR014830
OPM superfamily 92
OPM protein 1swx

Glycolipid transfer protein is a cytosolic protein that catalyses the transfer of glycolipids between different intracellular membranes. [1][2]

It was discovered by Metz and Radin in 1980 and partially purified and characterized in 1982. [3][4]

Recent reviews on structure and possible function are available. [5][6]

This protein transport primarily different glycosphingolipids and glyceroglycolipids between intracellular membranes, but not phospholipids. It might be also involved in translocation of glucosylceramides. It was found in brain, kidney, spleen, lung, cerebellum, liver and heart.

Human proteins containing this domain[edit]



  1. ^ Brown RE, Lin X, Rao CS, Pike HM, Molotkovsky JG (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. 
  2. ^ Nymalm Y, Airenne TT, Kidron H, Salminen TA, Nylund M, West G, Mattjus P (2006). "Structural evidence for adaptive ligand binding of glycolipid transfer protein". J. Mol. Biol. 355 (2): 224–36. doi:10.1016/j.jmb.2005.10.031. PMID 16309699. 
  3. ^ Metz, RJ, and Radin, NS. Glucosylceramide Uptake Protein from Spleen Cytosol. Journal of Biological Chemistry. 1980;255(10):4463–67. PMID 7372587.
  4. ^ Metz, RJ, and Radin NS. Purification and Properties of a Cerebroside Transfer Protein. Journal of Biological Chemistry. 1982;257(21):12901–07. PMID 7130186.
  5. ^ Mattjus P. Glycolipid transfer proteins and membrane interaction. Biochimica et Biophysica Acta. 2009;1788:267–72. PMID 19007748.
  6. ^ Brown RE, and Mattjus P. Glycolipid transfer proteins. Biochimica et Biophysica Acta. 2007;1771:746-60. doi:10.1016/j.bbalip.2007.01.011. PMID 17320476. PMC 1986823.

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Glycolipid transfer protein (GLTP) Provide feedback

GLTP is a cytosolic protein that catalyses the intermembrane transfer of glycolipids [1].

Literature references

  1. Rao CS, Lin X, Pike HM, Molotkovsky JG, Brown RE; , Biochemistry. 2004;43:13805-13815.: Glycolipid transfer protein mediated transfer of glycosphingolipids between membranes: a model for action based on kinetic and thermodynamic analyses. PUBMED:15504043 EPMC:15504043

  2. Airenne TT, Kidron H, Nymalm Y, Nylund M, West G, Mattjus P, Salminen TA; , J Mol Biol. 2006;355:224-236.: Structural evidence for adaptive ligand binding of glycolipid transfer protein. PUBMED:16309699 EPMC:16309699

  3. Malinina L, Malakhova ML, Kanack AT, Lu M, Abagyan R, Brown RE, Patel DJ; , PLoS Biol. 2006;4:e362.: The liganding of glycolipid transfer protein is controlled by glycolipid acyl structure. PUBMED:17105344 EPMC:17105344

  4. Malinina L, Malakhova ML, Teplov A, Brown RE, Patel DJ; , Nature. 2004;430:1048-1053.: Structural basis for glycosphingolipid transfer specificity. PUBMED:15329726 EPMC:15329726

  5. Rao CS, Chung T, Pike HM, Brown RE; , Biophys J. 2005;89:4017-4028.: Glycolipid transfer protein interaction with bilayer vesicles: modulation by changing lipid composition. PUBMED:16169991 EPMC:16169991

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR014830

Glycolipid transfer protein (GLTP) is a cytosolic protein that catalyses the intermembrane transfer of glycolipids such as glycosphingolipids, glyceroglycolipids, and possibly glucosylceramides, but not of phospholipids. The GLTP protein consists of a single domain with a multi-helical structure consisting of two layers of orthogonally packed helices [PUBMED:15504043, PUBMED:16309699].

The GLTP domain is also found in trans-Golgi network proteins involved in Golgi-to-cell-surface membrane traffic [PUBMED:15107860].

Gene Ontology

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Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...

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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

Pfam alignments:

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

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Seed source: pdb_1wbe
Previous IDs: none
Type: Domain
Author: Mistry J
Number in seed: 68
Number in full: 702
Average length of the domain: 140.30 aa
Average identity of full alignment: 27 %
Average coverage of the sequence by the domain: 56.28 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.6 25.6
Trusted cut-off 26.0 25.6
Noise cut-off 24.9 25.5
Model length: 149
Family (HMM) version: 6
Download: download the raw HMM for this family

Species distribution

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There is 1 interaction for this family. More...



For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the GLTP domain has been found. There are 19 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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