GLTP_HUMAN
ID GLTP_HUMAN Reviewed; 209 AA.
AC Q9NZD2; Q53Z13; Q96J68;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Glycolipid transfer protein;
DE Short=GLTP;
GN Name=GLTP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skin fibroblast;
RX PubMed=15287756; DOI=10.1021/bi0495432;
RA Li X.-M., Malakhova M.L., Lin X., Pike H.M., Chung T., Molotkovsky J.G.,
RA Brown R.E.;
RT "Human glycolipid transfer protein: probing conformation using fluorescence
RT spectroscopy.";
RL Biochemistry 43:10285-10294(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=18261224; DOI=10.1186/1471-2164-9-72;
RA Zou X., Chung T., Lin X., Malakhova M.L., Pike H.M., Brown R.E.;
RT "Human glycolipid transfer protein (GLTP) genes: organization,
RT transcriptional status and evolution.";
RL BMC Genomics 9:72-72(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Caudate nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION.
RX PubMed=15504043; DOI=10.1021/bi0492197;
RA Rao C.S., Lin X., Pike H.M., Molotkovsky J.G., Brown R.E.;
RT "Glycolipid transfer protein mediated transfer of glycosphingolipids
RT between membranes: a model for action based on kinetic and thermodynamic
RT analyses.";
RL Biochemistry 43:13805-13815(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17980653; DOI=10.1016/j.bbalip.2007.09.001;
RA Tuuf J., Mattjus P.;
RT "Human glycolipid transfer protein -- intracellular localization and
RT effects on the sphingolipid synthesis.";
RL Biochim. Biophys. Acta 1771:1353-1363(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9] {ECO:0007744|PDB:1SWX, ECO:0007744|PDB:1SX6}
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX WITH A
RP LACTOSYLCERAMIDE, FUNCTION, AND MUTAGENESIS OF ILE-45; ASP-48; ASN-52;
RP LYS-55; TRP-96; PHE-103; LEU-136; HIS-140; PHE-148; LEU-165; PHE-183 AND
RP TYR-207.
RX PubMed=15329726; DOI=10.1038/nature02856;
RA Malinina L., Malakhova M.L., Teplov A., Brown R.E., Patel D.J.;
RT "Structural basis for glycosphingolipid transfer specificity.";
RL Nature 430:1048-1053(2004).
RN [10]
RP MUTAGENESIS OF TRP-96.
RX PubMed=29164996; DOI=10.1080/15548627.2017.1393129;
RA Mishra S.K., Gao Y.G., Deng Y., Chalfant C.E., Hinchcliffe E.H.,
RA Brown R.E.;
RT "CPTP: A sphingolipid transfer protein that regulates autophagy and
RT inflammasome activation.";
RL Autophagy 14:862-879(2018).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEXES WITH
RP GLYCOSPHINGOLIPIDS, AND SUBUNIT.
RX PubMed=17105344; DOI=10.1371/journal.pbio.0040362;
RA Malinina L., Malakhova M.L., Kanack A.T., Lu M., Abagyan R., Brown R.E.,
RA Patel D.J.;
RT "The liganding of glycolipid transfer protein is controlled by glycolipid
RT acyl structure.";
RL PLoS Biol. 4:1996-2011(2006).
CC -!- FUNCTION: Accelerates the intermembrane transfer of various
CC glycolipids. Catalyzes the transfer of various glycosphingolipids
CC between membranes but does not catalyze the transfer of phospholipids.
CC May be involved in the intracellular translocation of
CC glucosylceramides. {ECO:0000269|PubMed:15329726,
CC ECO:0000269|PubMed:15504043, ECO:0000269|PubMed:17980653,
CC ECO:0000269|PubMed:18261224}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15329726,
CC ECO:0000269|PubMed:17105344}.
CC -!- INTERACTION:
CC Q9NZD2; Q96DZ9: CMTM5; NbExp=4; IntAct=EBI-2859814, EBI-2548702;
CC Q9NZD2; Q9NZD2: GLTP; NbExp=2; IntAct=EBI-2859814, EBI-2859814;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17980653}.
CC -!- TISSUE SPECIFICITY: Detected in fibroblasts (at protein level).
CC Detected in fibroblasts and in various cancer cell lines.
CC {ECO:0000269|PubMed:17980653, ECO:0000269|PubMed:18261224}.
CC -!- SIMILARITY: Belongs to the GLTP family. {ECO:0000305}.
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DR EMBL; AF209704; AAF33210.1; -; mRNA.
DR EMBL; AY372530; AAR85984.1; -; mRNA.
DR EMBL; AY372531; AAR85985.1; -; mRNA.
DR EMBL; AY372532; AAR87373.1; -; mRNA.
DR EMBL; AK313457; BAG36244.1; -; mRNA.
DR EMBL; CH471054; EAW97880.1; -; Genomic_DNA.
DR EMBL; BC009932; AAH09932.1; -; mRNA.
DR CCDS; CCDS9136.1; -.
DR RefSeq; NP_057517.1; NM_016433.3.
DR PDB; 1SWX; X-ray; 1.65 A; A=1-209.
DR PDB; 1SX6; X-ray; 1.95 A; A=1-209.
DR PDB; 2EUK; X-ray; 1.85 A; A=1-209.
DR PDB; 2EUM; X-ray; 2.30 A; A=1-209.
DR PDB; 2EVD; X-ray; 2.00 A; A=1-209.
DR PDB; 2EVL; X-ray; 2.20 A; A=1-209.
DR PDB; 2EVS; X-ray; 2.20 A; A/E=1-209.
DR PDB; 2EVT; X-ray; 1.99 A; A=1-209.
DR PDB; 3RIC; X-ray; 2.10 A; A=1-209.
DR PDB; 3RWV; X-ray; 1.50 A; A/B=1-209.
DR PDB; 3RZN; X-ray; 1.10 A; A=1-209.
DR PDB; 3S0I; X-ray; 1.50 A; A=1-209.
DR PDB; 3S0K; X-ray; 1.40 A; A=1-209.
DR PDB; 4GH0; X-ray; 1.35 A; A=1-209.
DR PDB; 4GHP; X-ray; 1.90 A; A=1-209.
DR PDB; 4GHS; X-ray; 3.20 A; A/B=1-209.
DR PDB; 4GIX; X-ray; 1.80 A; A=1-209.
DR PDB; 4GJQ; X-ray; 2.00 A; A/B=1-209.
DR PDB; 4GVT; X-ray; 2.90 A; A=1-209.
DR PDB; 4GXD; X-ray; 2.10 A; A=1-209.
DR PDB; 4GXG; X-ray; 2.40 A; A/B/D/E=1-209.
DR PDB; 4H2Z; X-ray; 1.45 A; A=1-209.
DR PDBsum; 1SWX; -.
DR PDBsum; 1SX6; -.
DR PDBsum; 2EUK; -.
DR PDBsum; 2EUM; -.
DR PDBsum; 2EVD; -.
DR PDBsum; 2EVL; -.
DR PDBsum; 2EVS; -.
DR PDBsum; 2EVT; -.
DR PDBsum; 3RIC; -.
DR PDBsum; 3RWV; -.
DR PDBsum; 3RZN; -.
DR PDBsum; 3S0I; -.
DR PDBsum; 3S0K; -.
DR PDBsum; 4GH0; -.
DR PDBsum; 4GHP; -.
DR PDBsum; 4GHS; -.
DR PDBsum; 4GIX; -.
DR PDBsum; 4GJQ; -.
DR PDBsum; 4GVT; -.
DR PDBsum; 4GXD; -.
DR PDBsum; 4GXG; -.
DR PDBsum; 4H2Z; -.
DR AlphaFoldDB; Q9NZD2; -.
DR SMR; Q9NZD2; -.
DR BioGRID; 119392; 21.
DR DIP; DIP-59418N; -.
DR IntAct; Q9NZD2; 6.
DR STRING; 9606.ENSP00000315263; -.
DR DrugBank; DB03600; Capric acid.
DR DrugBank; DB04465; Lactose.
DR DrugBank; DB03017; Lauric acid.
DR DrugBank; DB03203; Sphingosine.
DR iPTMnet; Q9NZD2; -.
DR PhosphoSitePlus; Q9NZD2; -.
DR BioMuta; GLTP; -.
DR DMDM; 20138399; -.
DR EPD; Q9NZD2; -.
DR jPOST; Q9NZD2; -.
DR MassIVE; Q9NZD2; -.
DR MaxQB; Q9NZD2; -.
DR PaxDb; Q9NZD2; -.
DR PeptideAtlas; Q9NZD2; -.
DR PRIDE; Q9NZD2; -.
DR ProteomicsDB; 83375; -.
DR Antibodypedia; 30918; 110 antibodies from 20 providers.
DR DNASU; 51228; -.
DR Ensembl; ENST00000318348.9; ENSP00000315263.3; ENSG00000139433.11.
DR GeneID; 51228; -.
DR KEGG; hsa:51228; -.
DR MANE-Select; ENST00000318348.9; ENSP00000315263.3; NM_016433.4; NP_057517.1.
DR UCSC; uc001tpm.3; human.
DR CTD; 51228; -.
DR DisGeNET; 51228; -.
DR GeneCards; GLTP; -.
DR HGNC; HGNC:24867; GLTP.
DR HPA; ENSG00000139433; Tissue enhanced (esophagus, skin).
DR MIM; 608949; gene.
DR neXtProt; NX_Q9NZD2; -.
DR OpenTargets; ENSG00000139433; -.
DR PharmGKB; PA142671729; -.
DR VEuPathDB; HostDB:ENSG00000139433; -.
DR eggNOG; KOG3221; Eukaryota.
DR GeneTree; ENSGT00940000155182; -.
DR HOGENOM; CLU_079400_2_1_1; -.
DR InParanoid; Q9NZD2; -.
DR OMA; AMSACPY; -.
DR OrthoDB; 1160303at2759; -.
DR PhylomeDB; Q9NZD2; -.
DR TreeFam; TF317467; -.
DR PathwayCommons; Q9NZD2; -.
DR Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
DR SignaLink; Q9NZD2; -.
DR BioGRID-ORCS; 51228; 31 hits in 1087 CRISPR screens.
DR ChiTaRS; GLTP; human.
DR EvolutionaryTrace; Q9NZD2; -.
DR GeneWiki; GLTP; -.
DR GenomeRNAi; 51228; -.
DR Pharos; Q9NZD2; Tbio.
DR PRO; PR:Q9NZD2; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9NZD2; protein.
DR Bgee; ENSG00000139433; Expressed in upper arm skin and 189 other tissues.
DR ExpressionAtlas; Q9NZD2; baseline and differential.
DR Genevisible; Q9NZD2; HS.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:1902387; F:ceramide 1-phosphate binding; IBA:GO_Central.
DR GO; GO:1902388; F:ceramide 1-phosphate transfer activity; IBA:GO_Central.
DR GO; GO:0051861; F:glycolipid binding; IDA:HGNC-UCL.
DR GO; GO:0017089; F:glycolipid transfer activity; TAS:Reactome.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008289; F:lipid binding; IDA:HGNC-UCL.
DR GO; GO:0120013; F:lipid transfer activity; IDA:BHF-UCL.
DR GO; GO:0035627; P:ceramide transport; IBA:GO_Central.
DR GO; GO:0006687; P:glycosphingolipid metabolic process; TAS:Reactome.
DR GO; GO:0120009; P:intermembrane lipid transfer; IDA:BHF-UCL.
DR Gene3D; 1.10.3520.10; -; 1.
DR InterPro; IPR036497; GLTP_sf.
DR InterPro; IPR014830; Glycolipid_transfer_prot_dom.
DR Pfam; PF08718; GLTP; 1.
DR SUPFAM; SSF110004; SSF110004; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Lipid transport; Reference proteome;
KW Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P68266"
FT CHAIN 2..209
FT /note="Glycolipid transfer protein"
FT /id="PRO_0000148915"
FT REPEAT 45..55
FT /note="1"
FT REPEAT 56..66
FT /note="2"
FT REGION 45..66
FT /note="2 X 12 AA approximate tandem repeats"
FT BINDING 48..55
FT /ligand="beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-
FT N-[(9Z)-octadecenoyl]-sphing-4-enine"
FT /ligand_id="ChEBI:CHEBI:131557"
FT /evidence="ECO:0000269|PubMed:15329726,
FT ECO:0007744|PDB:1SX6"
FT BINDING 140
FT /ligand="beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-
FT N-[(9Z)-octadecenoyl]-sphing-4-enine"
FT /ligand_id="ChEBI:CHEBI:131557"
FT /evidence="ECO:0000269|PubMed:15329726,
FT ECO:0007744|PDB:1SX6"
FT BINDING 207
FT /ligand="beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-
FT N-[(9Z)-octadecenoyl]-sphing-4-enine"
FT /ligand_id="ChEBI:CHEBI:131557"
FT /evidence="ECO:0000269|PubMed:15329726,
FT ECO:0007744|PDB:1SX6"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P68266"
FT MUTAGEN 45
FT /note="I->N: 18% decrease in activity."
FT /evidence="ECO:0000269|PubMed:15329726"
FT MUTAGEN 48
FT /note="D->V: Significant inactivation; 15% residual
FT activity."
FT /evidence="ECO:0000269|PubMed:15329726"
FT MUTAGEN 52
FT /note="N->I: Significant inactivation; 15% residual
FT activity."
FT /evidence="ECO:0000269|PubMed:15329726"
FT MUTAGEN 55
FT /note="K->I: No loss of activity; 90-97% residual
FT activity."
FT /evidence="ECO:0000269|PubMed:15329726"
FT MUTAGEN 96
FT /note="W->A: Almost complete inactivation; 1-3% residual
FT activity. No effect on autophagy."
FT /evidence="ECO:0000269|PubMed:15329726,
FT ECO:0000269|PubMed:29164996"
FT MUTAGEN 96
FT /note="W->F: Partial inactivation; 63% residual activity."
FT /evidence="ECO:0000269|PubMed:15329726"
FT MUTAGEN 103
FT /note="F->S: About 25% decrease in activity."
FT /evidence="ECO:0000269|PubMed:15329726"
FT MUTAGEN 136
FT /note="L->R: Significant inactivation; 5% residual acti
FT vity."
FT /evidence="ECO:0000269|PubMed:15329726"
FT MUTAGEN 140
FT /note="H->L: Almost complete inactivation; 1-3% residual
FT activity."
FT /evidence="ECO:0000269|PubMed:15329726"
FT MUTAGEN 148
FT /note="F->S: About 50% decrease in activity."
FT /evidence="ECO:0000269|PubMed:15329726"
FT MUTAGEN 165
FT /note="L->R: 46% decrease in activity."
FT /evidence="ECO:0000269|PubMed:15329726"
FT MUTAGEN 183
FT /note="F->S: No loss of activity; 90% residual activity."
FT /evidence="ECO:0000269|PubMed:15329726"
FT MUTAGEN 207
FT /note="Y->L: No loss of activity; 90-97% residual
FT activity."
FT /evidence="ECO:0000269|PubMed:15329726"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:4GIX"
FT HELIX 20..27
FT /evidence="ECO:0007829|PDB:3RZN"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:3RIC"
FT HELIX 31..36
FT /evidence="ECO:0007829|PDB:3RZN"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:3RZN"
FT HELIX 43..62
FT /evidence="ECO:0007829|PDB:3RZN"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:3RZN"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:3RZN"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:3RZN"
FT HELIX 89..112
FT /evidence="ECO:0007829|PDB:3RZN"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:1SX6"
FT HELIX 125..135
FT /evidence="ECO:0007829|PDB:3RZN"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:3RZN"
FT HELIX 142..151
FT /evidence="ECO:0007829|PDB:3RZN"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:3RZN"
FT HELIX 158..165
FT /evidence="ECO:0007829|PDB:3RZN"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:3RZN"
FT HELIX 173..200
FT /evidence="ECO:0007829|PDB:3RZN"
SQ SEQUENCE 209 AA; 23850 MW; F3DD96D702AE22CF CRC64;
MALLAEHLLK PLPADKQIET GPFLEAVSHL PPFFDCLGSP VFTPIKADIS GNITKIKAVY
DTNPAKFRTL QNILEVEKEM YGAEWPKVGA TLALMWLKRG LRFIQVFLQS ICDGERDENH
PNLIRVNATK AYEMALKKYH GWIVQKIFQA ALYAAPYKSD FLKALSKGQN VTEEECLEKI
RLFLVNYTAT IDVIYEMYTQ MNAELNYKV
