ID   GLTP_RAT                Reviewed;         209 AA.
AC   B0BNM9;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Glycolipid transfer protein;
DE            Short=GLTP;
GN   Name=GLTP;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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).
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; CH473973; EDM13930.1; -; Genomic_DNA.
DR   EMBL; BC158884; AAI58885.1; -; mRNA.
DR   RefSeq; NP_001127885.1; NM_001134413.1.
DR   AlphaFoldDB; B0BNM9; -.
DR   SMR; B0BNM9; -.
DR   BioGRID; 252660; 1.
DR   STRING; 10116.ENSRNOP00000001581; -.
DR   iPTMnet; B0BNM9; -.
DR   PhosphoSitePlus; B0BNM9; -.
DR   SwissPalm; B0BNM9; -.
DR   jPOST; B0BNM9; -.
DR   PaxDb; B0BNM9; -.
DR   PeptideAtlas; B0BNM9; -.
DR   PRIDE; B0BNM9; -.
DR   Ensembl; ENSRNOT00000001581; ENSRNOP00000001581; ENSRNOG00000001192.
DR   GeneID; 288707; -.
DR   KEGG; rno:288707; -.
DR   UCSC; RGD:1564442; rat.
DR   CTD; 51228; -.
DR   RGD; 1564442; Gltp.
DR   eggNOG; KOG3221; Eukaryota.
DR   GeneTree; ENSGT00940000155182; -.
DR   HOGENOM; CLU_079400_2_1_1; -.
DR   InParanoid; B0BNM9; -.
DR   OMA; AMSACPY; -.
DR   OrthoDB; 1160303at2759; -.
DR   PhylomeDB; B0BNM9; -.
DR   TreeFam; TF317467; -.
DR   Reactome; R-RNO-1660662; Glycosphingolipid metabolism.
DR   PRO; PR:B0BNM9; -.
DR   Proteomes; UP000002494; Chromosome 12.
DR   Proteomes; UP000234681; Chromosome 12.
DR   Bgee; ENSRNOG00000001192; Expressed in esophagus and 20 other tissues.
DR   Genevisible; B0BNM9; RN.
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; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0008289; F:lipid binding; ISO:RGD.
DR   GO; GO:0120013; F:lipid transfer activity; ISO:RGD.
DR   GO; GO:0035627; P:ceramide transport; IBA:GO_Central.
DR   GO; GO:0120009; P:intermembrane lipid transfer; ISO:RGD.
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   Acetylation; Cytoplasm; Lipid transport; Reference proteome; Repeat;
KW   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_0000343609"
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:0000250|UniProtKB:P68266"
SQ   SEQUENCE   209 AA;  23704 MW;  A7CBDD142C77FE1A CRC64;
     MALLAEHLLK PLPADRQIET GPFLEAVAHL PPFFDCLGSP VFTPIKADIS GNITKIKAVY
     DTDPAKFKTL QNILEVEKGM YGAEWPKVGA TLALLWLKRG LRFIQVFLQS ICDGERDENH
     PNLIRVNANK AYEMALKKYH GWLVQKIFKA ALYAAPYKSD FLKALSKGQN VTEEECLEKI
     RLFLVNYTAT IDAIYEMYTK MNAELDYTV