GLTP_BOVIN
ID GLTP_BOVIN Reviewed; 209 AA.
AC P68265; P17403; Q9MYP3;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Glycolipid transfer protein;
DE Short=GLTP;
GN Name=GLTP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10671554; DOI=10.1074/jbc.275.7.5104;
RA Lin X., Mattjus P., Pike H.M., Windebank A.J., Brown R.E.;
RT "Cloning and expression of glycolipid transfer protein from bovine and
RT porcine brain.";
RL J. Biol. Chem. 275:5104-5110(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH
RP GANGLIOSIDE GM3 AND FATTY ACID, FUNCTION, AND SUBUNIT.
RX PubMed=16309699; DOI=10.1016/j.jmb.2005.10.031;
RA Airenne T.T., Kidron H., Nymalm Y., Nylund M., West G., Mattjus P.,
RA Salminen T.A.;
RT "Structural evidence for adaptive ligand binding of glycolipid transfer
RT protein.";
RL J. Mol. Biol. 355:224-236(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:10671554,
CC ECO:0000269|PubMed:16309699}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16309699}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in brain, kidney, spleen, lung,
CC cerebellum, liver and heart. {ECO:0000269|PubMed:10671554}.
CC -!- SIMILARITY: Belongs to the GLTP family. {ECO:0000305}.
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DR EMBL; AF209701; AAF33207.1; -; mRNA.
DR RefSeq; NP_786993.1; NM_175799.3.
DR PDB; 1TFJ; X-ray; 1.61 A; A=2-209.
DR PDB; 1WBE; X-ray; 1.36 A; A=2-209.
DR PDB; 2BV7; X-ray; 1.79 A; A=2-209.
DR PDBsum; 1TFJ; -.
DR PDBsum; 1WBE; -.
DR PDBsum; 2BV7; -.
DR AlphaFoldDB; P68265; -.
DR SMR; P68265; -.
DR STRING; 9913.ENSBTAP00000003355; -.
DR PaxDb; P68265; -.
DR PRIDE; P68265; -.
DR GeneID; 327678; -.
DR KEGG; bta:327678; -.
DR CTD; 51228; -.
DR eggNOG; KOG3221; Eukaryota.
DR InParanoid; P68265; -.
DR OrthoDB; 1160303at2759; -.
DR EvolutionaryTrace; P68265; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0008289; F:lipid binding; ISS:UniProtKB.
DR GO; GO:0120013; F:lipid transfer activity; ISS:UniProtKB.
DR GO; GO:0035627; P:ceramide transport; IBA:GO_Central.
DR GO; GO:0120009; P:intermembrane lipid transfer; ISS:UniProtKB.
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_0000148914"
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:0000250|UniProtKB:Q9NZD2"
FT BINDING 48
FT /ligand="ganglioside GM3 (d18:1(4E))"
FT /ligand_id="ChEBI:CHEBI:60065"
FT /evidence="ECO:0000269|PubMed:16309699,
FT ECO:0007744|PDB:2BV7"
FT BINDING 52
FT /ligand="ganglioside GM3 (d18:1(4E))"
FT /ligand_id="ChEBI:CHEBI:60065"
FT /evidence="ECO:0000269|PubMed:16309699,
FT ECO:0007744|PDB:2BV7"
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:0000250|UniProtKB:Q9NZD2"
FT BINDING 140
FT /ligand="ganglioside GM3 (d18:1(4E))"
FT /ligand_id="ChEBI:CHEBI:60065"
FT /evidence="ECO:0000269|PubMed:16309699,
FT ECO:0007744|PDB:2BV7"
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:0000250|UniProtKB:Q9NZD2"
FT BINDING 207
FT /ligand="ganglioside GM3 (d18:1(4E))"
FT /ligand_id="ChEBI:CHEBI:60065"
FT /evidence="ECO:0000269|PubMed:16309699,
FT ECO:0007744|PDB:2BV7"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P68266"
FT HELIX 20..27
FT /evidence="ECO:0007829|PDB:1WBE"
FT HELIX 31..35
FT /evidence="ECO:0007829|PDB:1WBE"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:1TFJ"
FT HELIX 43..62
FT /evidence="ECO:0007829|PDB:1WBE"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:1WBE"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:1WBE"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:1WBE"
FT HELIX 89..112
FT /evidence="ECO:0007829|PDB:1WBE"
FT HELIX 125..135
FT /evidence="ECO:0007829|PDB:1WBE"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1WBE"
FT HELIX 142..153
FT /evidence="ECO:0007829|PDB:1WBE"
FT HELIX 158..165
FT /evidence="ECO:0007829|PDB:1WBE"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:1WBE"
FT HELIX 173..200
FT /evidence="ECO:0007829|PDB:1WBE"
SQ SEQUENCE 209 AA; 23922 MW; 1C4E2F9CD77DD714 CRC64;
MALLAEHLLR PLPADKQIET GPFLEAVSHL PPFFDCLGSP VFTPIKADIS GNITKIKAVY
DTNPTKFRTL QNILEVEKEM YGAEWPKVGA TLALMWLKRG LRFIQVFLQS ICDGERDENH
PNLIRVNATK AYEMALKKYH GWIVQKIFQA ALYAAPYKSD FLKALSKGQN VTEEECLEKV
RLFLVNYTAT IDVIYEMYTR MNAELNYKV
