PLTP_HUMAN
ID PLTP_HUMAN Reviewed; 493 AA.
AC P55058; A8K006; B4DDD5; B4DRB4; E1P5N8; E7EV16; Q8WTT1; Q9BR07; Q9BSH8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Phospholipid transfer protein;
DE AltName: Full=Lipid transfer protein II;
DE Flags: Precursor;
GN Name=PLTP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 18-27 AND
RP 163-184.
RC TISSUE=Umbilical vein endothelial cell;
RX PubMed=8132678; DOI=10.1016/s0021-9258(17)37120-x;
RA Day J.R., Albers J.J., Lofton-Day C.E., Gilbert T.L., Ching A.F.T.,
RA Grant F.J., O'Hara P.J., Marcovina S.M., Adolphson J.L.;
RT "Complete cDNA encoding human phospholipid transfer protein from human
RT endothelial cells.";
RL J. Biol. Chem. 269:9388-9391(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RA Kobayashi Y., Ohshiro N., Shibusawa A., Sasaki T., Tokuyama S.,
RA Yamamoto T.;
RT "Molecular cloning and functional characterization of phospholipid transfer
RT protein from human placenta cDNA library.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1), AND
RP VARIANTS TYR-124 AND ILE-425.
RG SeattleSNPs variation discovery resource;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC TISSUE=Adipose tissue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Placenta;
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE 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 [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9132017; DOI=10.1021/bi962776b;
RA Rao R., Albers J.J., Wolfbauer G., Pownall H.J.;
RT "Molecular and macromolecular specificity of human plasma phospholipid
RT transfer protein.";
RL Biochemistry 36:3645-3653(1997).
RN [10]
RP DISULFIDE BOND.
RX PubMed=10333293; DOI=10.1023/a:1020628006453;
RA Qu S.J., Fan H.Z., Kilinc C., Pownall H.J.;
RT "Role of cysteine residues in human plasma phospholipid transfer protein.";
RL J. Protein Chem. 18:193-198(1999).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11013307;
RA Oka T., Kujiraoka T., Ito M., Egashira T., Takahashi S., Nanjee M.N.,
RA Miller N.E., Metso J., Olkkonen V.M., Ehnholm C., Jauhiainen M.,
RA Hattori H.;
RT "Distribution of phospholipid transfer protein in human plasma: presence of
RT two forms of phospholipid transfer protein, one catalytically active and
RT the other inactive.";
RL J. Lipid Res. 41:1651-1657(2000).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64; ASN-94; ASN-143; ASN-245
RP AND ASN-398.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF ASN-64; ASN-94; ASN-117 AND ASN-143.
RX PubMed=19321130; DOI=10.1016/j.bbamcr.2009.01.010;
RA Vuletic S., Dong W., Wolfbauer G., Day J.R., Albers J.J.;
RT "PLTP is present in the nucleus, and its nuclear export is CRM1-
RT dependent.";
RL Biochim. Biophys. Acta 1793:584-591(2009).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [16]
RP GLYCOSYLATION AT ASN-64; ASN-143 AND ASN-245.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [17]
RP FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT ASN-64; ASN-94; ASN-117;
RP ASN-143; ASN-245 AND ASN-398, AND MUTAGENESIS OF SER-66; SER-96; SER-119;
RP SER-145; SER-247 AND SER-400.
RX PubMed=21515415; DOI=10.1016/j.bbapap.2011.04.004;
RA Albers J.J., Day J.R., Wolfbauer G., Kennedy H., Vuletic S., Cheung M.C.;
RT "Impact of site-specific N-glycosylation on cellular secretion, activity
RT and specific activity of the plasma phospholipid transfer protein.";
RL Biochim. Biophys. Acta 1814:908-911(2011).
RN [18]
RP REVIEW ON FUNCTION.
RX PubMed=21736953; DOI=10.1016/j.bbalip.2011.06.013;
RA Albers J.J., Vuletic S., Cheung M.C.;
RT "Role of plasma phospholipid transfer protein in lipid and lipoprotein
RT metabolism.";
RL Biochim. Biophys. Acta 1821:345-357(2012).
RN [19]
RP VARIANTS GLN-282; HIS-372 AND TRP-380.
RX PubMed=12966036; DOI=10.1093/hmg/ddg314;
RA Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S.,
RA Alvin G.B., Das K., Gilliam T.C.;
RT "Association of extreme blood lipid profile phenotypic variation with 11
RT reverse cholesterol transport genes and 10 non-genetic cardiovascular
RT disease risk factors.";
RL Hum. Mol. Genet. 12:2733-2743(2003).
RN [20]
RP 3D-STRUCTURE MODELING, STRUCTURE BY ELECTRON CRYOMICROSCOPY, FUNCTION,
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF MET-176.
RX PubMed=29883800; DOI=10.1016/j.bbalip.2018.06.001;
RA Zhang M., Zhai X., Li J., Albers J.J., Vuletic S., Ren G.;
RT "Structural basis of the lipid transfer mechanism of phospholipid transfer
RT protein (PLTP).";
RL Biochim. Biophys. Acta 1863:1082-1094(2018).
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:9132017, PubMed:11013307, PubMed:19321130, PubMed:21515415,
CC PubMed:29883800). Facilitates the transfer of a spectrum of different
CC lipid molecules, including diacylglycerol, phosphatidic acid,
CC sphingomyelin, phosphatidylcholine, phosphatidylinositol,
CC phosphatidylglycerol, cerebroside and phosphatidyl ethanolamine
CC (PubMed:9132017). Plays an important role in HDL remodeling which
CC involves modulating the size and composition of HDL (PubMed:29883800).
CC Also plays a key role in the uptake of cholesterol from peripheral
CC cells and tissues that is subsequently transported to the liver for
CC degradation and excretion (PubMed:21736953). Two distinct forms of PLTP
CC exist in plasma: an active form that can transfer phosphatidylcholine
CC from phospholipid vesicles to HDL, and an inactive form that lacks this
CC capability (PubMed:11013307). {ECO:0000269|PubMed:11013307,
CC ECO:0000269|PubMed:19321130, ECO:0000269|PubMed:21515415,
CC ECO:0000269|PubMed:29883800, ECO:0000269|PubMed:7654777,
CC ECO:0000269|PubMed:9132017, ECO:0000303|PubMed:21736953}.
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:11013307,
CC ECO:0000269|PubMed:19321130, ECO:0000269|PubMed:21515415,
CC ECO:0000269|PubMed:29883800, ECO:0000269|PubMed:7654777,
CC ECO:0000269|PubMed:9132017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38572;
CC Evidence={ECO:0000305|PubMed:9132017};
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:0000269|PubMed:9132017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38896;
CC Evidence={ECO:0000305|PubMed:9132017};
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:0000269|PubMed:9132017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39724;
CC Evidence={ECO:0000305|PubMed:9132017};
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:0000269|PubMed:9132017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36436;
CC Evidence={ECO:0000305|PubMed:9132017};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sphingomyelin(in) = a sphingomyelin(out);
CC Xref=Rhea:RHEA:39727, ChEBI:CHEBI:17636;
CC Evidence={ECO:0000269|PubMed:9132017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39728;
CC Evidence={ECO:0000305|PubMed:9132017};
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:0000269|PubMed:9132017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39744;
CC Evidence={ECO:0000305|PubMed:9132017};
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:0000250|UniProtKB:P55065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38692;
CC Evidence={ECO:0000250|UniProtKB:P55065};
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:0000250|UniProtKB:P55065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46493;
CC Evidence={ECO:0000250|UniProtKB:P55065};
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:0000250|UniProtKB:P55065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46497;
CC Evidence={ECO:0000250|UniProtKB:P55065};
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:0000250|UniProtKB:P55065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46489;
CC Evidence={ECO:0000250|UniProtKB:P55065};
CC -!- INTERACTION:
CC P55058-2; Q96CV9: OPTN; NbExp=3; IntAct=EBI-12701312, EBI-748974;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19321130}. Nucleus
CC {ECO:0000269|PubMed:19321130}. Note=Nuclear export is XPO1/CRM1-
CC dependent. {ECO:0000269|PubMed:19321130}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P55058-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P55058-2; Sequence=VSP_003050;
CC Name=3;
CC IsoId=P55058-3; Sequence=VSP_045877;
CC Name=4;
CC IsoId=P55058-4; Sequence=VSP_054028;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest level of expression in
CC the ovary, thymus and placenta, with moderate levels found in the
CC pancreas, small intestine, testis, lung and prostrate. Low level
CC expression in the kidney, liver and spleen, with very low levels found
CC in the heart, colon, skeletal muscle, leukocytes and brain. Expressed
CC in the cortical neurons. {ECO:0000269|PubMed:19321130,
CC ECO:0000269|PubMed:7654777}.
CC -!- PTM: Glycosylation is necessary for secretion and its phospholipid
CC transfer activity. {ECO:0000269|PubMed:21515415}.
CC -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/pltp/";
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DR EMBL; L26232; AAA36443.1; -; mRNA.
DR EMBL; AB076694; BAB79630.1; -; mRNA.
DR EMBL; AL008726; CAA15499.1; -; Genomic_DNA.
DR EMBL; AK289371; BAF82060.1; -; mRNA.
DR EMBL; AK293150; BAG56696.1; -; mRNA.
DR EMBL; AK299181; BAG61226.1; -; mRNA.
DR EMBL; AL008726; CAC36020.1; -; Genomic_DNA.
DR EMBL; AY509570; AAR87775.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75782.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75781.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75783.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75785.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75787.1; -; Genomic_DNA.
DR EMBL; BC005045; AAH05045.1; -; mRNA.
DR EMBL; BC019847; AAH19847.1; -; mRNA.
DR EMBL; BC019898; AAH19898.1; -; mRNA.
DR CCDS; CCDS13386.1; -. [P55058-1]
DR CCDS; CCDS13387.1; -. [P55058-2]
DR CCDS; CCDS56196.1; -. [P55058-4]
DR CCDS; CCDS56197.1; -. [P55058-3]
DR PIR; A53533; A53533.
DR RefSeq; NP_001229849.1; NM_001242920.1. [P55058-3]
DR RefSeq; NP_001229850.1; NM_001242921.1. [P55058-4]
DR RefSeq; NP_006218.1; NM_006227.3. [P55058-1]
DR RefSeq; NP_872617.1; NM_182676.2. [P55058-2]
DR AlphaFoldDB; P55058; -.
DR SMR; P55058; -.
DR BioGRID; 111374; 54.
DR IntAct; P55058; 23.
DR STRING; 9606.ENSP00000417138; -.
DR BindingDB; P55058; -.
DR ChEMBL; CHEMBL5962; -.
DR DrugBank; DB00163; Vitamin E.
DR SwissLipids; SLP:000000469; -.
DR TCDB; 1.C.40.1.4; the bactericidal permeability increasing protein (bpip) family.
DR GlyConnect; 683; 16 N-Linked glycans (5 sites).
DR GlyGen; P55058; 7 sites, 20 N-linked glycans (5 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P55058; -.
DR PhosphoSitePlus; P55058; -.
DR BioMuta; PLTP; -.
DR DMDM; 1709662; -.
DR CPTAC; CPTAC-1321; -.
DR CPTAC; non-CPTAC-1145; -.
DR EPD; P55058; -.
DR jPOST; P55058; -.
DR MassIVE; P55058; -.
DR MaxQB; P55058; -.
DR PaxDb; P55058; -.
DR PeptideAtlas; P55058; -.
DR PRIDE; P55058; -.
DR ProteomicsDB; 18550; -.
DR ProteomicsDB; 56769; -. [P55058-1]
DR ProteomicsDB; 56770; -. [P55058-2]
DR TopDownProteomics; P55058-1; -. [P55058-1]
DR Antibodypedia; 27873; 322 antibodies from 32 providers.
DR DNASU; 5360; -.
DR Ensembl; ENST00000354050.8; ENSP00000335290.4; ENSG00000100979.15. [P55058-2]
DR Ensembl; ENST00000372420.5; ENSP00000361497.1; ENSG00000100979.15. [P55058-4]
DR Ensembl; ENST00000372431.8; ENSP00000361508.3; ENSG00000100979.15. [P55058-1]
DR Ensembl; ENST00000420868.2; ENSP00000411671.2; ENSG00000100979.15. [P55058-3]
DR Ensembl; ENST00000477313.5; ENSP00000417138.1; ENSG00000100979.15. [P55058-1]
DR GeneID; 5360; -.
DR KEGG; hsa:5360; -.
DR MANE-Select; ENST00000372431.8; ENSP00000361508.3; NM_006227.4; NP_006218.1.
DR UCSC; uc002xql.3; human. [P55058-1]
DR CTD; 5360; -.
DR DisGeNET; 5360; -.
DR GeneCards; PLTP; -.
DR HGNC; HGNC:9093; PLTP.
DR HPA; ENSG00000100979; Low tissue specificity.
DR MIM; 172425; gene.
DR neXtProt; NX_P55058; -.
DR OpenTargets; ENSG00000100979; -.
DR PharmGKB; PA273; -.
DR VEuPathDB; HostDB:ENSG00000100979; -.
DR eggNOG; KOG4160; Eukaryota.
DR GeneTree; ENSGT01020000230353; -.
DR HOGENOM; CLU_028970_2_0_1; -.
DR InParanoid; P55058; -.
DR OMA; MEQQTAN; -.
DR OrthoDB; 463931at2759; -.
DR PhylomeDB; P55058; -.
DR TreeFam; TF315617; -.
DR PathwayCommons; P55058; -.
DR Reactome; R-HSA-8964058; HDL remodeling.
DR Reactome; R-HSA-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR SignaLink; P55058; -.
DR BioGRID-ORCS; 5360; 5 hits in 1073 CRISPR screens.
DR ChiTaRS; PLTP; human.
DR GeneWiki; Phospholipid_transfer_protein; -.
DR GenomeRNAi; 5360; -.
DR Pharos; P55058; Tbio.
DR PRO; PR:P55058; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; P55058; protein.
DR Bgee; ENSG00000100979; Expressed in right coronary artery and 194 other tissues.
DR Genevisible; P55058; HS.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0034364; C:high-density lipoprotein particle; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0097001; F:ceramide binding; IDA:BHF-UCL.
DR GO; GO:0120017; F:ceramide transfer activity; IBA:GO_Central.
DR GO; GO:0140340; F:cerebroside transfer activity; IDA:BHF-UCL.
DR GO; GO:0120020; F:cholesterol transfer activity; ISS:UniProtKB.
DR GO; GO:0140337; F:diacylglyceride transfer activity; IDA:BHF-UCL.
DR GO; GO:0019992; F:diacylglycerol binding; IDA:BHF-UCL.
DR GO; GO:0008035; F:high-density lipoprotein particle binding; IDA:UniProtKB.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; IDA:UniProtKB.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:BHF-UCL.
DR GO; GO:1990050; F:phosphatidic acid transfer activity; IDA:BHF-UCL.
DR GO; GO:0031210; F:phosphatidylcholine binding; IDA:BHF-UCL.
DR GO; GO:0120019; F:phosphatidylcholine transfer activity; IDA:BHF-UCL.
DR GO; GO:0008525; F:phosphatidylcholine transporter activity; IBA:GO_Central.
DR GO; GO:0008429; F:phosphatidylethanolamine binding; IDA:BHF-UCL.
DR GO; GO:1904121; F:phosphatidylethanolamine transfer activity; IDA:BHF-UCL.
DR GO; GO:1901611; F:phosphatidylglycerol binding; IDA:BHF-UCL.
DR GO; GO:0140339; F:phosphatidylglycerol transfer activity; IDA:BHF-UCL.
DR GO; GO:0008526; F:phosphatidylinositol transfer activity; ISS:UniProtKB.
DR GO; GO:0120014; F:phospholipid transfer activity; IDA:UniProtKB.
DR GO; GO:0140338; F:sphingomyelin transfer activity; IDA:BHF-UCL.
DR GO; GO:0034189; F:very-low-density lipoprotein particle binding; IDA:UniProtKB.
DR GO; GO:0035627; P:ceramide transport; IDA:BHF-UCL.
DR GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
DR GO; GO:0046836; P:glycolipid transport; IDA:ARUK-UCL.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IDA:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR GO; GO:0006869; P:lipid transport; IDA:BHF-UCL.
DR GO; GO:0015914; P:phospholipid transport; IDA:BHF-UCL.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; IDA:AgBase.
DR GO; GO:0010189; P:vitamin E biosynthetic process; IEA:Ensembl.
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 Alternative splicing; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Lipid transport; Nucleus; Reference proteome; Secreted;
KW Signal; Transport.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:8132678"
FT CHAIN 18..493
FT /note="Phospholipid transfer protein"
FT /id="PRO_0000017162"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:21515415"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:21515415"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:21515415"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:21515415"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:21515415"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT DISULFID 146..185
FT /evidence="ECO:0000269|PubMed:10333293,
FT ECO:0000269|PubMed:21515415"
FT VAR_SEQ 1..88
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054028"
FT VAR_SEQ 68..162
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045877"
FT VAR_SEQ 110..162
FT /note="FYDGGYINASAEGVSIRTGLELSRDPAGRMKVSNVSCQASVSRMHAAFGGTF
FT K -> L (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_003050"
FT VARIANT 124
FT /note="S -> Y (in dbSNP:rs11569636)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_018879"
FT VARIANT 282
FT /note="R -> Q (in dbSNP:rs56126980)"
FT /evidence="ECO:0000269|PubMed:12966036"
FT /id="VAR_017020"
FT VARIANT 372
FT /note="R -> H (in dbSNP:rs144710772)"
FT /evidence="ECO:0000269|PubMed:12966036"
FT /id="VAR_017021"
FT VARIANT 380
FT /note="R -> W (in dbSNP:rs6065903)"
FT /evidence="ECO:0000269|PubMed:12966036"
FT /id="VAR_017022"
FT VARIANT 425
FT /note="M -> I (in dbSNP:rs11569675)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_018880"
FT VARIANT 444
FT /note="F -> L (in dbSNP:rs1804161)"
FT /id="VAR_012073"
FT VARIANT 487
FT /note="T -> K (in dbSNP:rs1056929)"
FT /id="VAR_012074"
FT MUTAGEN 64
FT /note="N->A: Increased nuclear localization; when
FT associated with A-94; A-117 and A-143."
FT /evidence="ECO:0000269|PubMed:19321130"
FT MUTAGEN 66
FT /note="S->A: Significant reduction in phospholipid transfer
FT activity. No effect on secretion."
FT /evidence="ECO:0000269|PubMed:21515415"
FT MUTAGEN 94
FT /note="N->A: Increased nuclear localization; when
FT associated with A-64; A-117 and A-143."
FT /evidence="ECO:0000269|PubMed:19321130"
FT MUTAGEN 96
FT /note="S->A: Significant reduction in phospholipid transfer
FT activity. Increased secretion."
FT /evidence="ECO:0000269|PubMed:21515415"
FT MUTAGEN 117
FT /note="N->A: Increased nuclear localization; when
FT associated with A-64; A-94 and A-143."
FT /evidence="ECO:0000269|PubMed:19321130"
FT MUTAGEN 119
FT /note="S->A: Significant reduction in phospholipid transfer
FT activity. Increased secretion."
FT /evidence="ECO:0000269|PubMed:21515415"
FT MUTAGEN 143
FT /note="N->A: Increased nuclear localization; when
FT associated with A-64; A-94 and A-117."
FT /evidence="ECO:0000269|PubMed:19321130"
FT MUTAGEN 145
FT /note="S->A: Significant reduction in phospholipid transfer
FT activity. Reduced secretion."
FT /evidence="ECO:0000269|PubMed:21515415"
FT MUTAGEN 176
FT /note="M->E: Significant reduction in HDL-binding and
FT absence of lipid transfer activity."
FT /evidence="ECO:0000269|PubMed:29883800"
FT MUTAGEN 247
FT /note="S->A: Significant reduction in phospholipid transfer
FT activity. Reduced secretion."
FT /evidence="ECO:0000269|PubMed:21515415"
FT MUTAGEN 400
FT /note="S->A: Significant reduction in phospholipid transfer
FT activity. Reduced secretion."
FT /evidence="ECO:0000269|PubMed:21515415"
FT CONFLICT 18
FT /note="E -> V (in Ref. 7; AAH19847/AAH19898)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="A -> V (in Ref. 4; BAG61226)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="A -> S (in Ref. 4; BAG56696)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 54739 MW; C6E4852F18E12317 CRC64;
MALFGALFLA LLAGAHAEFP GCKIRVTSKA LELVKQEGLR FLEQELETIT IPDLRGKEGH
FYYNISEVKV TELQLTSSEL DFQPQQELML QITNASLGLR FRRQLLYWFF YDGGYINASA
EGVSIRTGLE LSRDPAGRMK VSNVSCQASV SRMHAAFGGT FKKVYDFLST FITSGMRFLL
NQQICPVLYH AGTVLLNSLL DTVPVRSSVD ELVGIDYSLM KDPVASTSNL DMDFRGAFFP
LTERNWSLPN RAVEPQLQEE ERMVYVAFSE FFFDSAMESY FRAGALQLLL VGDKVPHDLD
MLLRATYFGS IVLLSPAVID SPLKLELRVL APPRCTIKPS GTTISVTASV TIALVPPDQP
EVQLSSMTMD ARLSAKMALR GKALRTQLDL RRFRIYSNHS ALESLALIPL QAPLKTMLQI
GVMPMLNERT WRGVQIPLPE GINFVHEVVT NHAGFLTIGA DLHFAKGLRE VIEKNRPADV
RASTAPTPST AAV
