PLTP_MOUSE
ID PLTP_MOUSE Reviewed; 493 AA.
AC P55065; Q99L70;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Phospholipid transfer protein;
DE AltName: Full=Lipid transfer protein II;
DE Flags: Precursor;
GN Name=Pltp;
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], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=7654777; DOI=10.1016/0005-2760(95)00091-p;
RA Albers J.J., Wolfbauer G., Cheung M.C., Day J.R., Ching A.F.T., Lok S.,
RA Tu A.-Y.;
RT "Functional expression of human and mouse plasma phospholipid transfer
RT protein: effect of recombinant and plasma PLTP on HDL subspecies.";
RL Biochim. Biophys. Acta 1258:27-34(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=7615508; DOI=10.1074/jbc.270.29.17133;
RA Jiang X.-C., Bruce C.;
RT "Regulation of murine plasma phospholipid transfer protein activity and
RT mRNA levels by lipopolysaccharide and high cholesterol diet.";
RL J. Biol. Chem. 270:17133-17138(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=10079112; DOI=10.1172/jci5578;
RA Jiang X.C., Bruce C., Mar J., Lin M., Ji Y., Francone O.L., Tall A.R.;
RT "Targeted mutation of plasma phospholipid transfer protein gene markedly
RT reduces high-density lipoprotein levels.";
RL J. Clin. Invest. 103:907-914(1999).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Lung;
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: Mediates the transfer of phospholipids and free cholesterol
CC from triglyceride-rich lipoproteins (low density lipoproteins or LDL
CC and very low density lipoproteins or VLDL) into high-density
CC lipoproteins (HDL) as well as the exchange of phospholipids between
CC triglyceride-rich lipoproteins themselves (PubMed:7654777,
CC PubMed:7615508, PubMed:10079112,). Facilitates the transfer of a
CC spectrum of different lipid molecules, including sphingomyelin,
CC phosphatidylcholine, phosphatidylinositol, phosphatidylglycerol, and
CC phosphatidyl ethanolamine (PubMed:10079112). Plays an important role in
CC HDL remodeling which involves modulating the size and composition of
CC HDL (By similarity). Also plays a key role in the uptake of cholesterol
CC from peripheral cells and tissues that is subsequently transported to
CC the liver for degradation and excretion (By similarity). Two distinct
CC forms of PLTP exist in plasma: an active form that can transfer
CC phosphatidylcholine from phospholipid vesicles to HDL, and an inactive
CC form that lacks this capability (By similarity).
CC {ECO:0000250|UniProtKB:P55058, ECO:0000269|PubMed:10079112,
CC ECO:0000269|PubMed:7615508, ECO:0000269|PubMed:7654777}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-
CC sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571,
CC ChEBI:CHEBI:57643; Evidence={ECO:0000269|PubMed:7615508,
CC ECO:0000269|PubMed:7654777};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38572;
CC Evidence={ECO:0000305|PubMed:7654777};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-
CC diacyl-sn-glycero-3-phosphoethanolamine(out); Xref=Rhea:RHEA:38895,
CC ChEBI:CHEBI:64612; Evidence={ECO:0000250|UniProtKB:P55058};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38896;
CC Evidence={ECO:0000250|UniProtKB:P55058};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol(in) = a 1,2-diacyl-sn-glycerol(out);
CC Xref=Rhea:RHEA:39723, ChEBI:CHEBI:17815;
CC Evidence={ECO:0000250|UniProtKB:P55058};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39724;
CC Evidence={ECO:0000250|UniProtKB:P55058};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate(in) = a 1,2-diacyl-sn-
CC glycero-3-phosphate(out); Xref=Rhea:RHEA:36435, ChEBI:CHEBI:58608;
CC Evidence={ECO:0000250|UniProtKB:P55058};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36436;
CC Evidence={ECO:0000250|UniProtKB:P55058};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sphingomyelin(in) = a sphingomyelin(out);
CC Xref=Rhea:RHEA:39727, ChEBI:CHEBI:17636;
CC Evidence={ECO:0000250|UniProtKB:P55058};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39728;
CC Evidence={ECO:0000250|UniProtKB:P55058};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol)(in) = 1,2-
CC diacyl-sn-glycero-3-phospho-(1'-sn-glycerol)(out);
CC Xref=Rhea:RHEA:39743, ChEBI:CHEBI:64716;
CC Evidence={ECO:0000250|UniProtKB:P55058};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39744;
CC Evidence={ECO:0000250|UniProtKB:P55058};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(in) = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(out);
CC Xref=Rhea:RHEA:38691, ChEBI:CHEBI:57880;
CC Evidence={ECO:0000269|PubMed:10079112};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38692;
CC Evidence={ECO:0000305|PubMed:10079112};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphoethanolamine(in) = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine(out);
CC Xref=Rhea:RHEA:46492, ChEBI:CHEBI:73009;
CC Evidence={ECO:0000269|PubMed:10079112};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46493;
CC Evidence={ECO:0000305|PubMed:10079112};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-(hexadecanoyl)-sphing-4-enine-1-phosphocholine(in) = N-
CC (hexadecanoyl)-sphing-4-enine-1-phosphocholine(out);
CC Xref=Rhea:RHEA:46496, ChEBI:CHEBI:78646;
CC Evidence={ECO:0000269|PubMed:10079112};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46497;
CC Evidence={ECO:0000305|PubMed:10079112};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine(in) = 1,2-
CC dihexadecanoyl-sn-glycero-3-phosphocholine(out);
CC Xref=Rhea:RHEA:46488, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000269|PubMed:10079112};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46489;
CC Evidence={ECO:0000305|PubMed:10079112};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P55058}. Nucleus
CC {ECO:0000250|UniProtKB:P55058}. Note=Nuclear export is XPO1/CRM1-
CC dependent. {ECO:0000250|UniProtKB:P55058}.
CC -!- TISSUE SPECIFICITY: Highest level expression in the lung, brain and
CC heart with relatively low levels in the liver, skeletal muscle and
CC testis and very low levels found in the spleen and kidney.
CC {ECO:0000269|PubMed:10079112, ECO:0000269|PubMed:7615508,
CC ECO:0000269|PubMed:7654777}.
CC -!- PTM: Glycosylation is necessary for secretion and its phospholipid
CC transfer activity. {ECO:0000250|UniProtKB:P55058}.
CC -!- DISRUPTION PHENOTYPE: Mice show a complete loss of phosphatidylcholine,
CC phosphatidylethanolamine, phosphatidylinositol and sphingomyelin
CC transfer activities, and a partial loss of free cholesterol transfer
CC activity (PubMed:10079112). Transfer of VLDL phospholipid into HDL is
CC abolished (PubMed:10079112). A marked reduction in the levels of plasma
CC HDL phospholipid, cholesteryl ester and free cholesterol seen, whereas
CC the levels of non-HDL lipids are not significantly altered
CC (PubMed:10079112). {ECO:0000269|PubMed:10079112}.
CC -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.
CC {ECO:0000305}.
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DR EMBL; U37226; AAA80542.1; -; mRNA.
DR EMBL; U28960; AAA87943.1; -; mRNA.
DR EMBL; BC003782; AAH03782.1; -; mRNA.
DR CCDS; CCDS17063.1; -.
DR PIR; I49370; I49370.
DR RefSeq; NP_035255.1; NM_011125.2.
DR AlphaFoldDB; P55065; -.
DR SMR; P55065; -.
DR BioGRID; 202259; 1.
DR STRING; 10090.ENSMUSP00000061519; -.
DR SwissLipids; SLP:000000471; -.
DR GlyGen; P55065; 7 sites.
DR iPTMnet; P55065; -.
DR PhosphoSitePlus; P55065; -.
DR CPTAC; non-CPTAC-5613; -.
DR CPTAC; non-CPTAC-5614; -.
DR PaxDb; P55065; -.
DR PeptideAtlas; P55065; -.
DR PRIDE; P55065; -.
DR ProteomicsDB; 289696; -.
DR Antibodypedia; 27873; 322 antibodies from 32 providers.
DR DNASU; 18830; -.
DR Ensembl; ENSMUST00000059954; ENSMUSP00000061519; ENSMUSG00000017754.
DR Ensembl; ENSMUST00000109316; ENSMUSP00000104939; ENSMUSG00000017754.
DR GeneID; 18830; -.
DR KEGG; mmu:18830; -.
DR UCSC; uc008nwn.1; mouse.
DR CTD; 5360; -.
DR MGI; MGI:103151; Pltp.
DR VEuPathDB; HostDB:ENSMUSG00000017754; -.
DR eggNOG; KOG4160; Eukaryota.
DR GeneTree; ENSGT01020000230353; -.
DR InParanoid; P55065; -.
DR OMA; MEQQTAN; -.
DR OrthoDB; 463931at2759; -.
DR PhylomeDB; P55065; -.
DR TreeFam; TF315617; -.
DR Reactome; R-MMU-8964058; HDL remodeling.
DR BioGRID-ORCS; 18830; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Pltp; mouse.
DR PRO; PR:P55065; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P55065; protein.
DR Bgee; ENSMUSG00000017754; Expressed in pigmented layer of retina and 257 other tissues.
DR ExpressionAtlas; P55065; baseline and differential.
DR Genevisible; P55065; MM.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0034364; C:high-density lipoprotein particle; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0097001; F:ceramide binding; ISO:MGI.
DR GO; GO:0120017; F:ceramide transfer activity; IBA:GO_Central.
DR GO; GO:0140340; F:cerebroside transfer activity; ISO:MGI.
DR GO; GO:0120020; F:cholesterol transfer activity; IMP:UniProtKB.
DR GO; GO:0140337; F:diacylglyceride transfer activity; ISO:MGI.
DR GO; GO:0019992; F:diacylglycerol binding; ISO:MGI.
DR GO; GO:0008035; F:high-density lipoprotein particle binding; ISS:UniProtKB.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; ISS:UniProtKB.
DR GO; GO:0070300; F:phosphatidic acid binding; ISO:MGI.
DR GO; GO:1990050; F:phosphatidic acid transfer activity; ISO:MGI.
DR GO; GO:0031210; F:phosphatidylcholine binding; ISO:MGI.
DR GO; GO:0120019; F:phosphatidylcholine transfer activity; IMP:UniProtKB.
DR GO; GO:0008525; F:phosphatidylcholine transporter activity; IBA:GO_Central.
DR GO; GO:0008429; F:phosphatidylethanolamine binding; ISO:MGI.
DR GO; GO:1904121; F:phosphatidylethanolamine transfer activity; IMP:UniProtKB.
DR GO; GO:1901611; F:phosphatidylglycerol binding; ISO:MGI.
DR GO; GO:0140339; F:phosphatidylglycerol transfer activity; ISO:MGI.
DR GO; GO:0008526; F:phosphatidylinositol transfer activity; IMP:UniProtKB.
DR GO; GO:0120014; F:phospholipid transfer activity; IDA:UniProtKB.
DR GO; GO:0140338; F:sphingomyelin transfer activity; IMP:UniProtKB.
DR GO; GO:0034189; F:very-low-density lipoprotein particle binding; ISS:UniProtKB.
DR GO; GO:0035627; P:ceramide transport; ISO:MGI.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
DR GO; GO:0046836; P:glycolipid transport; ISO:MGI.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; ISS:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; ISO:MGI.
DR GO; GO:0015914; P:phospholipid transport; ISO:MGI.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; ISO:MGI.
DR GO; GO:0010189; P:vitamin E biosynthetic process; IMP:MGI.
DR InterPro; IPR017943; Bactericidal_perm-incr_a/b_dom.
DR InterPro; IPR030675; BPI/LBP.
DR InterPro; IPR032942; BPI/LBP/Plunc.
DR InterPro; IPR001124; Lipid-bd_serum_glycop_C.
DR InterPro; IPR017954; Lipid-bd_serum_glycop_CS.
DR InterPro; IPR017942; Lipid-bd_serum_glycop_N.
DR InterPro; IPR030179; PLTP.
DR PANTHER; PTHR10504; PTHR10504; 1.
DR PANTHER; PTHR10504:SF16; PTHR10504:SF16; 1.
DR Pfam; PF01273; LBP_BPI_CETP; 1.
DR Pfam; PF02886; LBP_BPI_CETP_C; 1.
DR PIRSF; PIRSF002417; Lipid_binding_protein; 1.
DR SMART; SM00328; BPI1; 1.
DR SMART; SM00329; BPI2; 1.
DR SUPFAM; SSF55394; SSF55394; 2.
DR PROSITE; PS00400; LBP_BPI_CETP; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Lipid transport; Nucleus; Reference proteome;
KW Secreted; Signal; Transport.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..493
FT /note="Phospholipid transfer protein"
FT /id="PRO_0000017163"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 146..185
FT /evidence="ECO:0000250|UniProtKB:P55058"
FT CONFLICT 16..17
FT /note="Missing (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="D -> E (in Ref. 3; AAH03782)"
FT /evidence="ECO:0000305"
FT CONFLICT 53..54
FT /note="DV -> ER (in Ref. 2; AAA87943)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="R -> S (in Ref. 2; AAA87943)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="L -> P (in Ref. 2; AAA87943)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="A -> D (in Ref. 2; AAA87943)"
FT /evidence="ECO:0000305"
FT CONFLICT 242..244
FT /note="KED -> RRN (in Ref. 2; AAA87943)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="K -> M (in Ref. 2; AAA87943)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="F -> L (in Ref. 2; AAA87943)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 54453 MW; E58E2C71142B77B5 CRC64;
MVLLWALFLA LLAGAHAELP GCKIRVTSAA LDLVKQEGLR FLEQELETIT IPDVYGAKGH
FYYNISDVRV TQLHLISSEL HFQPDQDLLL NISNASLGLH FRRQLLYWFL YDGGYINASA
EGVSIRTGLQ LSQDSSGRIK VSNVSCEASV SKMNMAFGGT FRRMYNFFST FITSGMRFLL
NQQICPVLYH AGTVLLNSLL DTVPVRSSVD DLVGIDYSLL KDPVVSNGNL DMEFRGAFFP
LKEDNWSLPN RAVEPQLEDD ERMVYVAFSE FFFDSAMESY FQAGALQLTL VGDKVPSDLD
MLLRATYFGS IVLLSPTVIN SPLKLKLEAT SPPRCTIKPS GTTISITASV TITLAPPMLP
EVELSKMIME GRLSAKLTLR GKALRVKLDL RRFQIYSNQS ALESLALIPL QAPLKTLLQI
GVMPLLNERT WRGVQIPLPE GINFVREVVT NHAGFVTVGA DLHFAKGLRE VIDKNRPADV
AASHVPPPSA AAA
