GLTP_PIG
ID GLTP_PIG Reviewed; 209 AA.
AC P68266; P17403; Q9MYP3;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Glycolipid transfer protein;
DE Short=GLTP;
GN Name=GLTP;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 PROTEIN SEQUENCE OF 2-209, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain;
RX PubMed=2190982; DOI=10.1016/s0021-9258(19)38716-2;
RA Abe A.;
RT "Primary structure of glycolipid transfer protein from pig brain.";
RL J. Biol. Chem. 265:9634-9637(1990).
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 glucosylceramides
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GLTP family. {ECO:0000305}.
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DR EMBL; AF209702; AAF33208.1; -; mRNA.
DR PIR; A36432; A36432.
DR RefSeq; NP_998987.1; NM_213822.1.
DR RefSeq; XP_013842375.1; XM_013986921.1.
DR AlphaFoldDB; P68266; -.
DR SMR; P68266; -.
DR STRING; 9823.ENSSSCP00000010597; -.
DR iPTMnet; P68266; -.
DR PaxDb; P68266; -.
DR PeptideAtlas; P68266; -.
DR PRIDE; P68266; -.
DR GeneID; 396765; -.
DR CTD; 51228; -.
DR eggNOG; KOG3221; Eukaryota.
DR InParanoid; P68266; -.
DR OrthoDB; 1160303at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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:HGNC-UCL.
DR GO; GO:0120013; F:lipid transfer activity; ISS:HGNC.
DR GO; GO:0035627; P:ceramide transport; IBA:GO_Central.
DR GO; GO:0120009; P:intermembrane lipid transfer; ISS:HGNC.
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 Acetylation; Cytoplasm; Direct protein sequencing; Lipid transport;
KW Reference proteome; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2190982"
FT CHAIN 2..209
FT /note="Glycolipid transfer protein"
FT /id="PRO_0000148917"
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 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 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 MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:2190982"
FT CONFLICT 10
FT /note="R -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="T -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="R -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
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