ID   GLTP1_ARATH             Reviewed;         202 AA.
AC   O22797;
DT   01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Glycolipid transfer protein 1 {ECO:0000303|PubMed:16309699};
GN   Name=GLTP1 {ECO:0000303|PubMed:16309699};
GN   OrderedLocusNames=At2g33470 {ECO:0000312|Araport:AT2G33470};
GN   ORFNames=F4P9.24 {ECO:0000312|EMBL:AAB80664.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION.
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: May be involved in glycolipids transfer.
CC       {ECO:0000305|PubMed:16309699}.
CC   -!- SIMILARITY: Belongs to the GLTP family. {ECO:0000305}.
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DR   EMBL; AC002332; AAB80664.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08838.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08839.1; -; Genomic_DNA.
DR   EMBL; BT004207; AAO42225.1; -; mRNA.
DR   EMBL; BT005674; AAO64094.1; -; mRNA.
DR   EMBL; AK317264; BAH19942.1; -; mRNA.
DR   EMBL; AY085884; AAM63096.1; -; mRNA.
DR   PIR; H84745; H84745.
DR   RefSeq; NP_565766.1; NM_128907.5.
DR   RefSeq; NP_973588.1; NM_201859.4.
DR   AlphaFoldDB; O22797; -.
DR   SMR; O22797; -.
DR   STRING; 3702.AT2G33470.1; -.
DR   PaxDb; O22797; -.
DR   PRIDE; O22797; -.
DR   ProteomicsDB; 248524; -.
DR   DNASU; 817912; -.
DR   EnsemblPlants; AT2G33470.1; AT2G33470.1; AT2G33470.
DR   EnsemblPlants; AT2G33470.2; AT2G33470.2; AT2G33470.
DR   GeneID; 817912; -.
DR   Gramene; AT2G33470.1; AT2G33470.1; AT2G33470.
DR   Gramene; AT2G33470.2; AT2G33470.2; AT2G33470.
DR   KEGG; ath:AT2G33470; -.
DR   Araport; AT2G33470; -.
DR   TAIR; locus:2051043; AT2G33470.
DR   eggNOG; KOG3221; Eukaryota.
DR   HOGENOM; CLU_079400_3_0_1; -.
DR   InParanoid; O22797; -.
DR   OMA; AMSACPY; -.
DR   OrthoDB; 1160303at2759; -.
DR   PhylomeDB; O22797; -.
DR   PRO; PR:O22797; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O22797; baseline and differential.
DR   Genevisible; O22797; AT.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
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   Lipid transport; Reference proteome; Transport.
FT   CHAIN           1..202
FT                   /note="Glycolipid transfer protein 1"
FT                   /id="PRO_0000432644"
FT   BINDING         52
FT                   /ligand="ganglioside GM3 (d18:1(4E))"
FT                   /ligand_id="ChEBI:CHEBI:60065"
FT                   /evidence="ECO:0000305|PubMed:16309699"
FT   BINDING         56
FT                   /ligand="ganglioside GM3 (d18:1(4E))"
FT                   /ligand_id="ChEBI:CHEBI:60065"
FT                   /evidence="ECO:0000305|PubMed:16309699"
FT   BINDING         99
FT                   /ligand="ganglioside GM3 (d18:1(4E))"
FT                   /ligand_id="ChEBI:CHEBI:60065"
FT                   /evidence="ECO:0000305|PubMed:16309699"
FT   BINDING         138
FT                   /ligand="ganglioside GM3 (d18:1(4E))"
FT                   /ligand_id="ChEBI:CHEBI:60065"
FT                   /evidence="ECO:0000305|PubMed:16309699"
SQ   SEQUENCE   202 AA;  22740 MW;  221833E4BF92FD35 CRC64;
     MEGTVFTPCL EGMKHVKSDQ GEMLTKPFLE LCKTILPVID KFGAAMTLVK SDIGGNITRL
     EKNYLSDPDK FKYLYTFVQV EIESKIAKGS SSCTNGLLWL TRAMDFLVEL FRNLVAHQDW
     SMPQACADSY QKTLKKWHGW LASSTFSMAL KLAPDRKKFM DVISGSGNIQ ADMERFCAEF
     GPFLHDNHKF LASVGMDDMK AS