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Q9NZD2 (GLTP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycolipid transfer protein

Short name=GLTP
Gene names
Name:GLTP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length209 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Accelerates the intermembrane transfer of various glycolipids. Catalyzes the transfer of various glycosphingolipids between membranes but does not catalyze the transfer of phospholipids. May be involved in the intracellular translocation of glucosylceramides. Ref.2 Ref.6 Ref.7 Ref.9

Subunit structure

Monomer. Ref.10

Subcellular location

Cytoplasm Ref.7.

Tissue specificity

Detected in fibroblasts (at protein level). Detected in fibroblasts and in various cancer cell lines. Ref.2 Ref.7

Sequence similarities

Belongs to the GLTP family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 209208Glycolipid transfer protein
PRO_0000148915

Regions

Repeat45 – 55111
Repeat56 – 66112
Region45 – 66222 X 12 AA approximate tandem repeats
Region48 – 558Glycolipid binding

Sites

Binding site1401Glycolipid
Binding site2071Glycolipid

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Experimental info

Mutagenesis451I → N: 18% decrease in activity. Ref.9
Mutagenesis481D → V: Significant inactivation; 15% residual activity. Ref.9
Mutagenesis521N → I: Significant inactivation; 15% residual activity. Ref.9
Mutagenesis551K → I: No loss of activity; 90-97% residual activity. Ref.9
Mutagenesis961W → A: Almost complete inactivation; 1-3% residual activity. Ref.9
Mutagenesis961W → F: Partial inactivation; 63% residual activity. Ref.9
Mutagenesis1031F → S: About 25% decrease in activity. Ref.9
Mutagenesis1361L → R: Significant inactivation; 5% residual activity. Ref.9
Mutagenesis1401H → L: Almost complete inactivation; 1-3% residual activity. Ref.9
Mutagenesis1481F → S: About 50% decrease in activity. Ref.9
Mutagenesis1651L → R: 46% decrease in activity. Ref.9
Mutagenesis1831F → S: No loss of activity; 90% residual activity. Ref.9
Mutagenesis2071Y → L: No loss of activity; 90-97% residual activity. Ref.9

Secondary structure

............................... 209
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9NZD2 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: F3DD96D702AE22CF

FASTA20923,850
        10         20         30         40         50         60 
MALLAEHLLK PLPADKQIET GPFLEAVSHL PPFFDCLGSP VFTPIKADIS GNITKIKAVY 

        70         80         90        100        110        120 
DTNPAKFRTL QNILEVEKEM YGAEWPKVGA TLALMWLKRG LRFIQVFLQS ICDGERDENH 

       130        140        150        160        170        180 
PNLIRVNATK AYEMALKKYH GWIVQKIFQA ALYAAPYKSD FLKALSKGQN VTEEECLEKI 

       190        200 
RLFLVNYTAT IDVIYEMYTQ MNAELNYKV 

« Hide

References

« Hide 'large scale' references
[1]"Human glycolipid transfer protein: probing conformation using fluorescence spectroscopy."
Li X.-M., Malakhova M.L., Lin X., Pike H.M., Chung T., Molotkovsky J.G., Brown R.E.
Biochemistry 43:10285-10294(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Skin fibroblast.
[2]"Human glycolipid transfer protein (GLTP) genes: organization, transcriptional status and evolution."
Zou X., Chung T., Lin X., Malakhova M.L., Pike H.M., Brown R.E.
BMC Genomics 9:72-72(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Tissue: Brain.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Caudate nucleus.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[6]"Glycolipid transfer protein mediated transfer of glycosphingolipids between membranes: a model for action based on kinetic and thermodynamic analyses."
Rao C.S., Lin X., Pike H.M., Molotkovsky J.G., Brown R.E.
Biochemistry 43:13805-13815(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Human glycolipid transfer protein -- intracellular localization and effects on the sphingolipid synthesis."
Tuuf J., Mattjus P.
Biochim. Biophys. Acta 1771:1353-1363(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Structural basis for glycosphingolipid transfer specificity."
Malinina L., Malakhova M.L., Teplov A., Brown R.E., Patel D.J.
Nature 430:1048-1053(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX WITH GLYCOLIPID, FUNCTION, MUTAGENESIS OF ILE-45; ASP-48; ASN-52; LYS-55; TRP-96; PHE-103; LEU-136; HIS-140; PHE-148; LEU-165; PHE-183 AND TYR-207.
[10]"The liganding of glycolipid transfer protein is controlled by glycolipid acyl structure."
Malinina L., Malakhova M.L., Kanack A.T., Lu M., Abagyan R., Brown R.E., Patel D.J.
PLoS Biol. 4:1996-2011(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEXES WITH GLYCOSPHINGOLIPIDS, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF209704 mRNA. Translation: AAF33210.1.
AY372530 mRNA. Translation: AAR85984.1.
AY372531 mRNA. Translation: AAR85985.1.
AY372532 mRNA. Translation: AAR87373.1.
AK313457 mRNA. Translation: BAG36244.1.
CH471054 Genomic DNA. Translation: EAW97880.1.
BC009932 mRNA. Translation: AAH09932.1.
CCDSCCDS9136.1.
RefSeqNP_057517.1. NM_016433.3.
UniGeneHs.381256.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SWXX-ray1.65A1-209[»]
1SX6X-ray1.95A1-209[»]
2EUKX-ray1.85A1-209[»]
2EUMX-ray2.30A1-209[»]
2EVDX-ray2.00A1-209[»]
2EVLX-ray2.20A1-209[»]
2EVSX-ray2.20A/E1-209[»]
2EVTX-ray1.99A1-209[»]
3RICX-ray2.10A1-209[»]
3RWVX-ray1.50A/B1-209[»]
3RZNX-ray1.10A1-209[»]
3S0IX-ray1.50A1-209[»]
3S0KX-ray1.40A1-209[»]
4GH0X-ray1.35A1-209[»]
4GHPX-ray1.90A1-209[»]
4GHSX-ray3.20A/B1-209[»]
4GIXX-ray1.80A1-209[»]
4GJQX-ray2.00A/B1-209[»]
4GVTX-ray2.90A1-209[»]
4GXDX-ray2.10A1-209[»]
4GXGX-ray2.40A/B/D/E1-209[»]
4H2ZX-ray1.45A1-209[»]
ProteinModelPortalQ9NZD2.
SMRQ9NZD2. Positions 4-209.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119392. 2 interactions.
DIPDIP-59418N.
IntActQ9NZD2. 1 interaction.
STRING9606.ENSP00000315263.

PTM databases

PhosphoSiteQ9NZD2.

Polymorphism databases

DMDM20138399.

Proteomic databases

MaxQBQ9NZD2.
PaxDbQ9NZD2.
PRIDEQ9NZD2.

Protocols and materials databases

DNASU51228.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000318348; ENSP00000315263; ENSG00000139433.
GeneID51228.
KEGGhsa:51228.
UCSCuc001tpm.3. human.

Organism-specific databases

CTD51228.
GeneCardsGC12M110288.
HGNCHGNC:24867. GLTP.
HPAHPA056461.
MIM608949. gene.
neXtProtNX_Q9NZD2.
PharmGKBPA142671729.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG302244.
HOGENOMHOG000199421.
HOVERGENHBG019001.
InParanoidQ9NZD2.
OMAKFHNFVV.
OrthoDBEOG7FJH25.
PhylomeDBQ9NZD2.
TreeFamTF317467.

Gene expression databases

ArrayExpressQ9NZD2.
BgeeQ9NZD2.
CleanExHS_GLTP.
GenevestigatorQ9NZD2.

Family and domain databases

Gene3D1.10.3520.10. 1 hit.
InterProIPR014830. Glycolipid_transfer_prot_dom.
[Graphical view]
PfamPF08718. GLTP. 1 hit.
[Graphical view]
SUPFAMSSF110004. SSF110004. 1 hit.
ProtoNetSearch...

Other

ChiTaRSGLTP. human.
EvolutionaryTraceQ9NZD2.
GeneWikiGLTP.
GenomeRNAi51228.
NextBio54324.
PROQ9NZD2.
SOURCESearch...

Entry information

Entry nameGLTP_HUMAN
AccessionPrimary (citable) accession number: Q9NZD2
Secondary accession number(s): Q53Z13, Q96J68
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM