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   24-JAN-2024, entry version 166.
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.ENSMUSP00000104939; -.
DR   SwissLipids; SLP:000000471; -.
DR   GlyCosmos; P55065; 7 sites, No reported glycans.
DR   GlyGen; P55065; 7 sites.
DR   iPTMnet; P55065; -.
DR   PhosphoSitePlus; P55065; -.
DR   CPTAC; non-CPTAC-5613; -.
DR   CPTAC; non-CPTAC-5614; -.
DR   PaxDb; 10090-ENSMUSP00000061519; -.
DR   PeptideAtlas; P55065; -.
DR   ProteomicsDB; 289696; -.
DR   Antibodypedia; 27873; 353 antibodies from 32 providers.
DR   DNASU; 18830; -.
DR   Ensembl; ENSMUST00000059954.14; ENSMUSP00000061519.8; ENSMUSG00000017754.14.
DR   Ensembl; ENSMUST00000109316.8; ENSMUSP00000104939.2; ENSMUSG00000017754.14.
DR   GeneID; 18830; -.
DR   KEGG; mmu:18830; -.
DR   UCSC; uc008nwn.1; mouse.
DR   AGR; MGI:103151; -.
DR   CTD; 5360; -.
DR   MGI; MGI:103151; Pltp.
DR   VEuPathDB; HostDB:ENSMUSG00000017754; -.
DR   eggNOG; KOG4160; Eukaryota.
DR   GeneTree; ENSGT01100000263545; -.
DR   InParanoid; P55065; -.
DR   OMA; GMFAYYS; -.
DR   OrthoDB; 5307035at2759; -.
DR   PhylomeDB; P55065; -.
DR   TreeFam; TF315617; -.
DR   Reactome; R-MMU-8964058; HDL remodeling.
DR   BioGRID-ORCS; 18830; 1 hit in 78 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 261 other cell types or tissues.
DR   ExpressionAtlas; P55065; baseline and differential.
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: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   CDD; cd00025; BPI1; 1.
DR   CDD; cd00026; BPI2; 1.
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   PANTHER; PTHR10504; BACTERICIDAL PERMEABILITY-INCREASING BPI PROTEIN-RELATED; 1.
DR   PANTHER; PTHR10504:SF16; PHOSPHOLIPID TRANSFER PROTEIN; 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; Bactericidal permeability-increasing protein, BPI; 2.
DR   PROSITE; PS00400; LBP_BPI_CETP; 1.
DR   Genevisible; P55065; MM.
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
//