GLTP_MOUSE
ID GLTP_MOUSE Reviewed; 209 AA.
AC Q9JL62; Q91YJ7; Q9CTK9;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Glycolipid transfer protein;
DE Short=GLTP;
GN Name=Gltp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Epidermis;
RA Lin X., Mattjus P., Pike H.M., Windebank A.J., Brown R.E.;
RT "Cloning of mouse glycolipid transfer protein cDNA.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 154-209.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; AF209703; AAF33209.1; -; mRNA.
DR EMBL; BC016584; AAH16584.1; -; mRNA.
DR EMBL; AK003218; BAB22649.1; -; mRNA.
DR CCDS; CCDS19569.1; -.
DR RefSeq; NP_062795.2; NM_019821.2.
DR AlphaFoldDB; Q9JL62; -.
DR SMR; Q9JL62; -.
DR BioGRID; 207920; 1.
DR IntAct; Q9JL62; 2.
DR MINT; Q9JL62; -.
DR STRING; 10090.ENSMUSP00000012028; -.
DR iPTMnet; Q9JL62; -.
DR PhosphoSitePlus; Q9JL62; -.
DR EPD; Q9JL62; -.
DR jPOST; Q9JL62; -.
DR MaxQB; Q9JL62; -.
DR PaxDb; Q9JL62; -.
DR PRIDE; Q9JL62; -.
DR ProteomicsDB; 271000; -.
DR Antibodypedia; 30918; 110 antibodies from 20 providers.
DR DNASU; 56356; -.
DR Ensembl; ENSMUST00000012028; ENSMUSP00000012028; ENSMUSG00000011884.
DR GeneID; 56356; -.
DR KEGG; mmu:56356; -.
DR UCSC; uc008yzw.2; mouse.
DR CTD; 51228; -.
DR MGI; MGI:1929253; Gltp.
DR VEuPathDB; HostDB:ENSMUSG00000011884; -.
DR eggNOG; KOG3221; Eukaryota.
DR GeneTree; ENSGT00940000155182; -.
DR HOGENOM; CLU_079400_2_1_1; -.
DR InParanoid; Q9JL62; -.
DR OMA; AMSACPY; -.
DR OrthoDB; 1160303at2759; -.
DR PhylomeDB; Q9JL62; -.
DR TreeFam; TF317467; -.
DR Reactome; R-MMU-1660662; Glycosphingolipid metabolism.
DR BioGRID-ORCS; 56356; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Gltp; mouse.
DR PRO; PR:Q9JL62; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9JL62; protein.
DR Bgee; ENSMUSG00000011884; Expressed in tail skin and 267 other tissues.
DR ExpressionAtlas; Q9JL62; baseline and differential.
DR Genevisible; Q9JL62; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
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:HGNC-UCL.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
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; 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_0000148916"
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"
FT CONFLICT 205..208
FT /note="LDYT -> INYK (in Ref. 1; AAF33209)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 209 AA; 23690 MW; A7CBDD142C76BB1A CRC64;
MALLAEHLLK PLPADRQIET GPFLEAVAHL PPFFDCLGSP VFTPIKADIS GNITKIKAVY
DTDPAKFKTL QNILEVEKGM YGAEWPKVGA TLALLWLKRG LRFIQVFLQS ICDGERDENH
PNLIRVNANK AYEMALKKYH GWLVQKIFKA ALYAAPYKSD FLKALSKGQN VTEEECLEKI
RLFLVNYTAT IDAIYDMYTK MNAELDYTV
