GLTP_XENTR
ID GLTP_XENTR Reviewed; 209 AA.
AC B0BLT4;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Glycolipid transfer protein;
DE Short=GLTP;
GN Name=gltp;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GLTP family. {ECO:0000305}.
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DR EMBL; BC158153; AAI58154.1; -; mRNA.
DR AlphaFoldDB; B0BLT4; -.
DR SMR; B0BLT4; -.
DR STRING; 8364.ENSXETP00000040315; -.
DR PaxDb; B0BLT4; -.
DR eggNOG; KOG3221; Eukaryota.
DR InParanoid; B0BLT4; -.
DR Proteomes; UP000008143; Genome assembly.
DR Proteomes; UP000790000; 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:0035627; P:ceramide transport; IBA:GO_Central.
DR GO; GO:0120009; P:intermembrane lipid transfer; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cytoplasm; Lipid transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..209
FT /note="Glycolipid transfer protein"
FT /id="PRO_0000343613"
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"
SQ SEQUENCE 209 AA; 23906 MW; 1BB26DA823C91966 CRC64;
MSVLLQHQFK PLPADKQIDT CCFLDSVSHL PAFFDCFGSA IFSPIKADIT GNISKIRSVY
ESNPSKFKTL QMILEGEKEL HGPQWPKVGA TLALMWLKRG LKFIQVMLQS IADGERDDQN
PNLIKVNITK AYEIALKKYH GWFVQKIFQT ALIAAPYKDD FLKALSKGQT VKEEECIEKI
RQFLVNYTTT IEAIYIMYNK MNAELDYKA