Q9NZD2 (GLTP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glycolipid transfer protein
Short name=GLTP

Gene names

Name:

GLTP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	209 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Lipid transport Transport
Cellular component	Cytoplasm
Domain	Repeat
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glycolipid transport Inferred from direct assay PubMed 15901739. Source: HGNC
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred by curator PubMed 15901739. Source: HGNC
Molecular_function	glycolipid binding Inferred from direct assay Ref.1PubMed 15901739. Source: HGNC glycolipid transporter activity Inferred from direct assay PubMed 15901739. Source: HGNC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 209

208

Glycolipid transfer protein

PRO_0000148915

Regions

Repeat

45 – 55

11

1

Repeat

56 – 66

11

2

Region

45 – 66

22

2 X 12 AA approximate tandem repeats

Region

48 – 55

8

Glycolipid binding

Sites

Binding site

140

1

Glycolipid

Binding site

207

1

Glycolipid

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Experimental info

Mutagenesis

45

1

I → N: 18% decrease in activity. Ref.9

Mutagenesis

48

1

D → V: Significant inactivation; 15% residual activity. Ref.9

Mutagenesis

52

1

N → I: Significant inactivation; 15% residual activity. Ref.9

Mutagenesis

55

1

K → I: No loss of activity; 90-97% residual activity. Ref.9

Mutagenesis

96

1

W → A: Almost complete inactivation; 1-3% residual activity. Ref.9

Mutagenesis

96

1

W → F: Partial inactivation; 63% residual activity. Ref.9

Mutagenesis

103

1

F → S: About 25% decrease in activity. Ref.9

Mutagenesis

136

1

L → R: Significant inactivation; 5% residual activity. Ref.9

Mutagenesis

140

1

H → L: Almost complete inactivation; 1-3% residual activity. Ref.9

Mutagenesis

148

1

F → S: About 50% decrease in activity. Ref.9

Mutagenesis

165

1

L → R: 46% decrease in activity. Ref.9

Mutagenesis

183

1

F → S: No loss of activity; 90% residual activity. Ref.9

Mutagenesis

207

1

Y → L: No loss of activity; 90-97% residual activity. Ref.9

Secondary structure

1

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209

Helix Strand Turn

Details...

Helix

4 – 6

3

Helix

20 – 27

8

Turn

28 – 30

3

Helix

31 – 36

6

Helix

40 – 42

3

Helix

43 – 62

20

Turn

64 – 67

4

Helix

70 – 81

12

Helix

82 – 84

3

Helix

89 – 112

24

Beta strand

118 – 120

3

Helix

125 – 135

11

Helix

137 – 139

3

Helix

142 – 151

10

Helix

152 – 154

3

Helix

158 – 165

8

Turn

166 – 168

3

Helix

173 – 200

28

Sequences

	Sequence		Length	Mass (Da)
	Q9NZD2 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: F3DD96D702AE22CF	FASTA	209	23,850
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

IPI

IPI00184363.

RefSeq

NP_057517.1. NM_016433.3.

UniGene

Hs.381256.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SWX	X-ray	1.65	A	1-209	[»]
1SX6	X-ray	1.95	A	1-209	[»]
2EUK	X-ray	1.85	A	1-209	[»]
2EUM	X-ray	2.30	A	1-209	[»]
2EVD	X-ray	2.00	A	1-209	[»]
2EVL	X-ray	2.20	A	1-209	[»]
2EVS	X-ray	2.20	A/E	1-209	[»]
2EVT	X-ray	1.99	A	1-209	[»]
3RIC	X-ray	2.10	A	1-209	[»]
3RWV	X-ray	1.50	A/B	1-209	[»]
3RZN	X-ray	1.10	A	1-209	[»]
3S0I	X-ray	1.50	A	1-209	[»]
3S0K	X-ray	1.40	A	1-209	[»]
4GH0	X-ray	1.35	A	1-209	[»]
4GHP	X-ray	1.90	A	1-209	[»]
4GIX	X-ray	1.80	A	1-209	[»]
4GVT	X-ray	2.90	A	1-209	[»]
4GXD	X-ray	2.10	A	1-209	[»]
4GXG	X-ray	2.40	A/B/D/E	1-209	[»]
4H2Z	X-ray	1.45	A	1-209	[»]

ProteinModelPortal

Q9NZD2.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59418N.

IntAct

Q9NZD2. 1 interaction.

STRING

9606.ENSP00000315263.

PTM databases

PhosphoSite

Q9NZD2.

Polymorphism databases

DMDM

20138399.

Proteomic databases

PaxDb

Q9NZD2.

PRIDE

Q9NZD2.

Protocols and materials databases

DNASU

51228.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000318348; ENSP00000315263; ENSG00000139433.

GeneID

51228.

KEGG

hsa:51228.

UCSC

uc001tpm.3. human.

Organism-specific databases

CTD

51228.

GeneCards

GC12M110288.

HGNC

HGNC:24867. GLTP.

MIM

608949. gene.

neXtProt

NX_Q9NZD2.

PharmGKB

PA142671729.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG302244.

HOGENOM

HOG000199421.

HOVERGEN

HBG019001.

InParanoid

Q9NZD2.

OMA

MNADLDY.

OrthoDB

EOG49PB0B.

PhylomeDB

Q9NZD2.

Gene expression databases

ArrayExpress

Q9NZD2.

Bgee

Q9NZD2.

CleanEx

HS_GLTP.

Genevestigator

Q9NZD2.

GermOnline

ENSG00000139433. Homo sapiens.

Family and domain databases

Gene3D

1.10.3520.10. 1 hit.

InterPro

IPR014830. Glycolipid_transfer_prot_dom.
[Graphical view]

Pfam

PF08718. GLTP. 1 hit.
[Graphical view]

SUPFAM

SSF110004. Glycolipid_transfer_prot. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

GLTP. human.

EvolutionaryTrace

Q9NZD2.

GenomeRNAi

51228.

NextBio

54324.

SOURCE

Search...

Entry information

Entry name

GLTP_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 101 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.