Full text data of PLTP
PLTP
[Confidence: low (only semi-automatic identification from reviews)]
Phospholipid transfer protein (Lipid transfer protein II; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Phospholipid transfer protein (Lipid transfer protein II; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P55058
ID PLTP_HUMAN Reviewed; 493 AA.
AC P55058; A8K006; B4DRB4; E1P5N8; E7EV16; Q8WTT1; Q9BR07; Q9BSH8;
read moreDT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 133.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 18-27 AND 163-184.
RC TISSUE=Umbilical vein endothelial cell;
RX PubMed=8132678;
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].
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
RT transfer protein from human placenta cDNA library.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND 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 AND 3).
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA 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.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
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
RT protein.";
RL J. Protein Chem. 18:193-198(1999).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64; ASN-94; ASN-143;
RP ASN-245 AND ASN-398, AND MASS SPECTROMETRY.
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.,
RA Moore R.J., 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 [10]
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 [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64, AND MASS SPECTROMETRY.
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
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [12]
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.,
RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core
RT fucosylated glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [13]
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 [14]
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
RT 11 reverse cholesterol transport genes and 10 non-genetic
RT cardiovascular disease risk factors.";
RL Hum. Mol. Genet. 12:2733-2743(2003).
CC -!- FUNCTION: Facilitates the transfer of a spectrum of different
CC lipid molecules, including diacylglycerol, phosphatidic acid,
CC sphingomyelin, phosphatidylcholine, phosphatidylglycerol,
CC cerebroside and phosphatidyl ethanolamine. Essential for the
CC transfer of excess surface lipids from triglyceride-rich
CC lipoproteins to HDL, thereby facilitating the formation of smaller
CC lipoprotein remnants, contributing to the formation of LDL, and
CC assisting in the maturation of HDL particles. PLTP also plays a
CC key role in the uptake of cholesterol from peripheral cells and
CC tissues that is subsequently transported to the liver for
CC degradation and excretion. Two distinct forms of PLTP exist in
CC plasma: an active form that can transfer PC from phospholipid
CC vesicles to high-density lipoproteins (HDL), and an inactive form
CC that lacks this capability.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Wide tissue distribution. Placenta > pancreas
CC > lung > kidney > heart > liver > skeletal muscle > brain.
CC -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP
CC family.
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; 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 PIR; A53533; A53533.
DR RefSeq; NP_001229849.1; NM_001242920.1.
DR RefSeq; NP_006218.1; NM_006227.3.
DR RefSeq; NP_872617.1; NM_182676.2.
DR UniGene; Hs.439312; -.
DR ProteinModelPortal; P55058; -.
DR SMR; P55058; 20-462.
DR STRING; 9606.ENSP00000361508; -.
DR BindingDB; P55058; -.
DR ChEMBL; CHEMBL5962; -.
DR TCDB; 1.C.40.1.4; the bactericidal permeability increasing protein (bpip) family.
DR PhosphoSite; P55058; -.
DR DMDM; 1709662; -.
DR PaxDb; P55058; -.
DR PRIDE; P55058; -.
DR DNASU; 5360; -.
DR Ensembl; ENST00000354050; ENSP00000335290; ENSG00000100979.
DR Ensembl; ENST00000372431; ENSP00000361508; ENSG00000100979.
DR Ensembl; ENST00000420868; ENSP00000411671; ENSG00000100979.
DR Ensembl; ENST00000477313; ENSP00000417138; ENSG00000100979.
DR GeneID; 5360; -.
DR KEGG; hsa:5360; -.
DR UCSC; uc010zxj.2; human.
DR CTD; 5360; -.
DR GeneCards; GC20M044528; -.
DR HGNC; HGNC:9093; PLTP.
DR HPA; CAB032873; -.
DR MIM; 172425; gene.
DR neXtProt; NX_P55058; -.
DR PharmGKB; PA273; -.
DR eggNOG; NOG290011; -.
DR HOVERGEN; HBG103156; -.
DR InParanoid; P55058; -.
DR KO; K08761; -.
DR OrthoDB; EOG76739B; -.
DR PhylomeDB; P55058; -.
DR SignaLink; P55058; -.
DR GeneWiki; Phospholipid_transfer_protein; -.
DR GenomeRNAi; 5360; -.
DR NextBio; 20778; -.
DR PMAP-CutDB; P55058; -.
DR PRO; PR:P55058; -.
DR ArrayExpress; P55058; -.
DR Bgee; P55058; -.
DR CleanEx; HS_PLTP; -.
DR Genevestigator; P55058; -.
DR GO; GO:0005576; C:extracellular region; TAS:ProtInc.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0030317; P:sperm motility; IEA:Ensembl.
DR GO; GO:0010189; P:vitamin E biosynthetic process; IEA:Ensembl.
DR InterPro; IPR017943; Bactericidal_perm-incr_a/b_dom.
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 Pfam; PF01273; LBP_BPI_CETP; 1.
DR Pfam; PF02886; LBP_BPI_CETP_C; 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; Complete proteome; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Lipid transport; Polymorphism;
KW Reference proteome; Secreted; Signal; Transport.
FT SIGNAL 1 17
FT CHAIN 18 493 Phospholipid transfer protein.
FT /FTId=PRO_0000017162.
FT CARBOHYD 64 64 N-linked (GlcNAc...) (complex).
FT CARBOHYD 94 94 N-linked (GlcNAc...).
FT CARBOHYD 117 117 N-linked (GlcNAc...) (complex).
FT CARBOHYD 143 143 N-linked (GlcNAc...).
FT CARBOHYD 245 245 N-linked (GlcNAc...) (complex).
FT CARBOHYD 398 398 N-linked (GlcNAc...).
FT DISULFID 146 185
FT VAR_SEQ 68 162 Missing (in isoform 3).
FT /FTId=VSP_045877.
FT VAR_SEQ 110 162 FYDGGYINASAEGVSIRTGLELSRDPAGRMKVSNVSCQASV
FT SRMHAAFGGTFK -> L (in isoform 2).
FT /FTId=VSP_003050.
FT VARIANT 124 124 S -> Y (in dbSNP:rs11569636).
FT /FTId=VAR_018879.
FT VARIANT 282 282 R -> Q.
FT /FTId=VAR_017020.
FT VARIANT 372 372 R -> H.
FT /FTId=VAR_017021.
FT VARIANT 380 380 R -> W (in dbSNP:rs6065903).
FT /FTId=VAR_017022.
FT VARIANT 425 425 M -> I (in dbSNP:rs11569675).
FT /FTId=VAR_018880.
FT VARIANT 444 444 F -> L (in dbSNP:rs1804161).
FT /FTId=VAR_012073.
FT VARIANT 487 487 T -> K (in dbSNP:rs1056929).
FT /FTId=VAR_012074.
FT CONFLICT 18 18 E -> V (in Ref. 7; AAH19847/AAH19898).
FT CONFLICT 331 331 A -> V (in Ref. 4; BAG61226).
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
//
ID PLTP_HUMAN Reviewed; 493 AA.
AC P55058; A8K006; B4DRB4; E1P5N8; E7EV16; Q8WTT1; Q9BR07; Q9BSH8;
read moreDT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 133.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 18-27 AND 163-184.
RC TISSUE=Umbilical vein endothelial cell;
RX PubMed=8132678;
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].
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
RT transfer protein from human placenta cDNA library.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND 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 AND 3).
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA 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.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
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
RT protein.";
RL J. Protein Chem. 18:193-198(1999).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64; ASN-94; ASN-143;
RP ASN-245 AND ASN-398, AND MASS SPECTROMETRY.
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.,
RA Moore R.J., 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 [10]
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 [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64, AND MASS SPECTROMETRY.
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
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [12]
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.,
RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core
RT fucosylated glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [13]
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 [14]
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
RT 11 reverse cholesterol transport genes and 10 non-genetic
RT cardiovascular disease risk factors.";
RL Hum. Mol. Genet. 12:2733-2743(2003).
CC -!- FUNCTION: Facilitates the transfer of a spectrum of different
CC lipid molecules, including diacylglycerol, phosphatidic acid,
CC sphingomyelin, phosphatidylcholine, phosphatidylglycerol,
CC cerebroside and phosphatidyl ethanolamine. Essential for the
CC transfer of excess surface lipids from triglyceride-rich
CC lipoproteins to HDL, thereby facilitating the formation of smaller
CC lipoprotein remnants, contributing to the formation of LDL, and
CC assisting in the maturation of HDL particles. PLTP also plays a
CC key role in the uptake of cholesterol from peripheral cells and
CC tissues that is subsequently transported to the liver for
CC degradation and excretion. Two distinct forms of PLTP exist in
CC plasma: an active form that can transfer PC from phospholipid
CC vesicles to high-density lipoproteins (HDL), and an inactive form
CC that lacks this capability.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Wide tissue distribution. Placenta > pancreas
CC > lung > kidney > heart > liver > skeletal muscle > brain.
CC -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP
CC family.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/pltp/";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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; 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 PIR; A53533; A53533.
DR RefSeq; NP_001229849.1; NM_001242920.1.
DR RefSeq; NP_006218.1; NM_006227.3.
DR RefSeq; NP_872617.1; NM_182676.2.
DR UniGene; Hs.439312; -.
DR ProteinModelPortal; P55058; -.
DR SMR; P55058; 20-462.
DR STRING; 9606.ENSP00000361508; -.
DR BindingDB; P55058; -.
DR ChEMBL; CHEMBL5962; -.
DR TCDB; 1.C.40.1.4; the bactericidal permeability increasing protein (bpip) family.
DR PhosphoSite; P55058; -.
DR DMDM; 1709662; -.
DR PaxDb; P55058; -.
DR PRIDE; P55058; -.
DR DNASU; 5360; -.
DR Ensembl; ENST00000354050; ENSP00000335290; ENSG00000100979.
DR Ensembl; ENST00000372431; ENSP00000361508; ENSG00000100979.
DR Ensembl; ENST00000420868; ENSP00000411671; ENSG00000100979.
DR Ensembl; ENST00000477313; ENSP00000417138; ENSG00000100979.
DR GeneID; 5360; -.
DR KEGG; hsa:5360; -.
DR UCSC; uc010zxj.2; human.
DR CTD; 5360; -.
DR GeneCards; GC20M044528; -.
DR HGNC; HGNC:9093; PLTP.
DR HPA; CAB032873; -.
DR MIM; 172425; gene.
DR neXtProt; NX_P55058; -.
DR PharmGKB; PA273; -.
DR eggNOG; NOG290011; -.
DR HOVERGEN; HBG103156; -.
DR InParanoid; P55058; -.
DR KO; K08761; -.
DR OrthoDB; EOG76739B; -.
DR PhylomeDB; P55058; -.
DR SignaLink; P55058; -.
DR GeneWiki; Phospholipid_transfer_protein; -.
DR GenomeRNAi; 5360; -.
DR NextBio; 20778; -.
DR PMAP-CutDB; P55058; -.
DR PRO; PR:P55058; -.
DR ArrayExpress; P55058; -.
DR Bgee; P55058; -.
DR CleanEx; HS_PLTP; -.
DR Genevestigator; P55058; -.
DR GO; GO:0005576; C:extracellular region; TAS:ProtInc.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0030317; P:sperm motility; IEA:Ensembl.
DR GO; GO:0010189; P:vitamin E biosynthetic process; IEA:Ensembl.
DR InterPro; IPR017943; Bactericidal_perm-incr_a/b_dom.
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 Pfam; PF01273; LBP_BPI_CETP; 1.
DR Pfam; PF02886; LBP_BPI_CETP_C; 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; Complete proteome; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Lipid transport; Polymorphism;
KW Reference proteome; Secreted; Signal; Transport.
FT SIGNAL 1 17
FT CHAIN 18 493 Phospholipid transfer protein.
FT /FTId=PRO_0000017162.
FT CARBOHYD 64 64 N-linked (GlcNAc...) (complex).
FT CARBOHYD 94 94 N-linked (GlcNAc...).
FT CARBOHYD 117 117 N-linked (GlcNAc...) (complex).
FT CARBOHYD 143 143 N-linked (GlcNAc...).
FT CARBOHYD 245 245 N-linked (GlcNAc...) (complex).
FT CARBOHYD 398 398 N-linked (GlcNAc...).
FT DISULFID 146 185
FT VAR_SEQ 68 162 Missing (in isoform 3).
FT /FTId=VSP_045877.
FT VAR_SEQ 110 162 FYDGGYINASAEGVSIRTGLELSRDPAGRMKVSNVSCQASV
FT SRMHAAFGGTFK -> L (in isoform 2).
FT /FTId=VSP_003050.
FT VARIANT 124 124 S -> Y (in dbSNP:rs11569636).
FT /FTId=VAR_018879.
FT VARIANT 282 282 R -> Q.
FT /FTId=VAR_017020.
FT VARIANT 372 372 R -> H.
FT /FTId=VAR_017021.
FT VARIANT 380 380 R -> W (in dbSNP:rs6065903).
FT /FTId=VAR_017022.
FT VARIANT 425 425 M -> I (in dbSNP:rs11569675).
FT /FTId=VAR_018880.
FT VARIANT 444 444 F -> L (in dbSNP:rs1804161).
FT /FTId=VAR_012073.
FT VARIANT 487 487 T -> K (in dbSNP:rs1056929).
FT /FTId=VAR_012074.
FT CONFLICT 18 18 E -> V (in Ref. 7; AAH19847/AAH19898).
FT CONFLICT 331 331 A -> V (in Ref. 4; BAG61226).
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
//
MIM
172425
*RECORD*
*FIELD* NO
172425
*FIELD* TI
+172425 PHOSPHOLIPID TRANSFER PROTEIN; PLTP
;;LIPID TRANSFER PROTEIN II
HIGH DENSITY LIPOPROTEIN CHOLESTEROL LEVEL QUANTITATIVE TRAIT LOCUS
read more9, INCLUDED; HDLCQ9, INCLUDED
*FIELD* TX
CLONING
Human plasma contains at least 2 different lipid transfer proteins:
cholesteryl ester transfer protein (118470), also referred to as lipid
transfer protein I, and phospholipid transfer protein (PLTP), also
referred to as lipid transfer protein II. Day et al. (1994) purified
phospholipid transfer protein with an apparent molecular mass of 81 kD
from human plasma. From the NH2-terminal amino acid sequence, they
designed primers for polymerase chain reaction and isolated a
full-length cDNA from a human endothelial cDNA library. The cDNA was
1,750 bp long and contained an open reading frame of 1,518 nucleotides
encoding a leader of 17 amino acids and a mature protein of 476
residues.
GENE FUNCTION
Tu et al. (1995) identified the functional promoter of the PLTP gene.
The promoter consists of a TATA box, a high-GC content region, and
several consensus sequences for the potential binding of transcription
factors. A minimal promoter of 159 bp between -230 and -72 relative to
the first transcriptional initiation site was responsible for the full
activity. Two transcription factor-binding motifs, SP1 and AP-2, are
located within this area. It appeared that the PLTP promoter activity
relies primarily on the putative cis-elements in the functional region.
MAPPING
Using a human/rodent somatic cell hybrid mapping panel, Day et al.
(1994) mapped the PLTP gene to chromosome 20. Whitmore et al. (1995)
narrowed the assignment to 20q12-q13.1 by fluorescence in situ
hybridization. LeBoeuf et al. (1996) demonstrated that the Pltp gene
maps to the distal portion of mouse chromosome 2.
MOLECULAR GENETICS
In an evaluation of the hypothesis that multiple high density
lipoprotein cholesterol (HDL-C) levels reflect the cumulative
contributions of multiple common DNA sequence variants, each of which
has a small effect, Spirin et al. (2007) identified a single-nucleotide
polymorphism (SNP) of the PLTP gene (172425.0001) that acts in concert
with other SNPs in the CETP (118470.0005) and LPL (118470.0042) genes to
affect plasma levels of high density lipoprotein cholesterol.
In a metaanalysis of plasma lipid concentrations in greater than 100,000
individuals of European descent, Teslovich et al. (2010) identified
dbSNP rs6065906 near the PLTP gene as having an effect on HDL
cholesterol concentrations as well as triglyceride with an effect size
of -0.93 mg per deciliter and a P value of 2 x 10(-22).
ANIMAL MODEL
Using homologous recombination in embryonic stem cells, Jiang et al.
(1999) produced mice with no PLTP gene expression. Reduced plasma PLTP
activity caused markedly decreased high density lipoprotein (HDL) lipid
and apoprotein, demonstrating the importance of transfer surface
components of triglyceride-rich lipoproteins in the maintenance of HDL
levels. Vesicular lipoproteins accumulating in PLTP -/- mice on a
high-fat diet could influence the development of atherosclerosis.
*FIELD* AV
.0001
HIGH DENSITY LIPOPROTEIN CHOLESTEROL LEVEL QUANTITATIVE TRAIT LOCUS
9
PLTP, C-T
In an association study of 7 HDL metabolism genes in participants in the
Dallas Heart Study and in 849 African American men and women from
Maywood, IL, Spirin et al. (2007) identified a SNP of the PLTP gene,
dbSNP rs3843763, that was associated with incremental changes in HDL
cholesterol levels in 3 independent samples. This SNP achieved a P value
of 1.19 x 10(-4) in analysis of covariance in the entire sample in a
model that included race, sex, age, and body mass index (BMI). The minor
allele, T, was associated with lowering of HDL cholesterol.
*FIELD* RF
1. Day, J. R.; Albers, J. J.; Lofton-Day, C. E.; Gilbert, T. L.; Ching,
A. F. T.; Grant, F. J.; O'Hara, P. J.; Marcovina, S. M.; Adolphson,
J. L.: Complete cDNA encoding human phospholipid transfer protein
from human endothelial cells. J. Biol. Chem. 269: 9388-9391, 1994.
2. Jiang, X.; Bruce, C.; Mar, J.; Lin, M.; Ji, Y.; Francone, O. L.;
Tall, A. R.: Targeted mutation of plasma phospholipid transfer protein
gene markedly reduces high-density lipoprotein levels. J. Clin. Invest. 103:
907-914, 1999.
3. LeBoeuf, R. C.; Caldwell, M.; Tu, A.-Y.; Albers, J. J.: Phospholipid
transfer protein maps to distal mouse chromosome 2. Genomics 34:
259-260, 1996.
4. Spirin, V.; Schmidt, S.; Pertsemlidis, A.; Cooper, R. S.; Cohen,
J. C.; Sunyaev, S. R.: Common single-nucleotide polymorphisms act
in concert to affect plasma levels of high-density lipoprotein cholesterol. Am.
J. Hum. Genet. 81: 1298-1303, 2007.
5. Teslovich, T. M.; Musunuru, K.; Smith, A. V.; Edmondson, A. C.;
Stylianou, I. M.; Koseki, M.; Pirruccello, J. P.; Ripatti, S.; Chasman,
D. I.; Willer, C. J.; Johansen, C. T.; Fouchier, S. W.; and 197 others
: Biological, clinical and population relevance of 95 loci for blood
lipids. Nature 466: 707-713, 2010.
6. Tu, A.-Y.; Wolfbauer, G.; Albers, J. J.: Functional characterization
of the promoter region of the human phospholipid transfer protein
gene. Biochem. Biophys. Res. Commun. 217: 705-711, 1995.
7. Whitmore, T. E.; Day, J. R.; Albers, J. J.: Localization of the
human phospholipid transfer protein gene to chromosome 20q12-q13.1. Genomics 28:
599-600, 1995.
*FIELD* CN
Ada Hamosh - updated: 10/12/2010
Victor A. McKusick - updated: 11/28/2007
Victor A. McKusick - updated: 4/16/1999
Alan F. Scott - updated: 9/27/1995
*FIELD* CD
Victor A. McKusick: 5/20/1994
*FIELD* ED
alopez: 10/12/2010
carol: 3/25/2009
alopez: 12/13/2007
terry: 11/28/2007
carol: 4/19/1999
terry: 4/16/1999
terry: 6/26/1996
terry: 6/21/1996
terry: 4/17/1996
mark: 3/4/1996
terry: 2/23/1996
carol: 5/20/1994
*RECORD*
*FIELD* NO
172425
*FIELD* TI
+172425 PHOSPHOLIPID TRANSFER PROTEIN; PLTP
;;LIPID TRANSFER PROTEIN II
HIGH DENSITY LIPOPROTEIN CHOLESTEROL LEVEL QUANTITATIVE TRAIT LOCUS
read more9, INCLUDED; HDLCQ9, INCLUDED
*FIELD* TX
CLONING
Human plasma contains at least 2 different lipid transfer proteins:
cholesteryl ester transfer protein (118470), also referred to as lipid
transfer protein I, and phospholipid transfer protein (PLTP), also
referred to as lipid transfer protein II. Day et al. (1994) purified
phospholipid transfer protein with an apparent molecular mass of 81 kD
from human plasma. From the NH2-terminal amino acid sequence, they
designed primers for polymerase chain reaction and isolated a
full-length cDNA from a human endothelial cDNA library. The cDNA was
1,750 bp long and contained an open reading frame of 1,518 nucleotides
encoding a leader of 17 amino acids and a mature protein of 476
residues.
GENE FUNCTION
Tu et al. (1995) identified the functional promoter of the PLTP gene.
The promoter consists of a TATA box, a high-GC content region, and
several consensus sequences for the potential binding of transcription
factors. A minimal promoter of 159 bp between -230 and -72 relative to
the first transcriptional initiation site was responsible for the full
activity. Two transcription factor-binding motifs, SP1 and AP-2, are
located within this area. It appeared that the PLTP promoter activity
relies primarily on the putative cis-elements in the functional region.
MAPPING
Using a human/rodent somatic cell hybrid mapping panel, Day et al.
(1994) mapped the PLTP gene to chromosome 20. Whitmore et al. (1995)
narrowed the assignment to 20q12-q13.1 by fluorescence in situ
hybridization. LeBoeuf et al. (1996) demonstrated that the Pltp gene
maps to the distal portion of mouse chromosome 2.
MOLECULAR GENETICS
In an evaluation of the hypothesis that multiple high density
lipoprotein cholesterol (HDL-C) levels reflect the cumulative
contributions of multiple common DNA sequence variants, each of which
has a small effect, Spirin et al. (2007) identified a single-nucleotide
polymorphism (SNP) of the PLTP gene (172425.0001) that acts in concert
with other SNPs in the CETP (118470.0005) and LPL (118470.0042) genes to
affect plasma levels of high density lipoprotein cholesterol.
In a metaanalysis of plasma lipid concentrations in greater than 100,000
individuals of European descent, Teslovich et al. (2010) identified
dbSNP rs6065906 near the PLTP gene as having an effect on HDL
cholesterol concentrations as well as triglyceride with an effect size
of -0.93 mg per deciliter and a P value of 2 x 10(-22).
ANIMAL MODEL
Using homologous recombination in embryonic stem cells, Jiang et al.
(1999) produced mice with no PLTP gene expression. Reduced plasma PLTP
activity caused markedly decreased high density lipoprotein (HDL) lipid
and apoprotein, demonstrating the importance of transfer surface
components of triglyceride-rich lipoproteins in the maintenance of HDL
levels. Vesicular lipoproteins accumulating in PLTP -/- mice on a
high-fat diet could influence the development of atherosclerosis.
*FIELD* AV
.0001
HIGH DENSITY LIPOPROTEIN CHOLESTEROL LEVEL QUANTITATIVE TRAIT LOCUS
9
PLTP, C-T
In an association study of 7 HDL metabolism genes in participants in the
Dallas Heart Study and in 849 African American men and women from
Maywood, IL, Spirin et al. (2007) identified a SNP of the PLTP gene,
dbSNP rs3843763, that was associated with incremental changes in HDL
cholesterol levels in 3 independent samples. This SNP achieved a P value
of 1.19 x 10(-4) in analysis of covariance in the entire sample in a
model that included race, sex, age, and body mass index (BMI). The minor
allele, T, was associated with lowering of HDL cholesterol.
*FIELD* RF
1. Day, J. R.; Albers, J. J.; Lofton-Day, C. E.; Gilbert, T. L.; Ching,
A. F. T.; Grant, F. J.; O'Hara, P. J.; Marcovina, S. M.; Adolphson,
J. L.: Complete cDNA encoding human phospholipid transfer protein
from human endothelial cells. J. Biol. Chem. 269: 9388-9391, 1994.
2. Jiang, X.; Bruce, C.; Mar, J.; Lin, M.; Ji, Y.; Francone, O. L.;
Tall, A. R.: Targeted mutation of plasma phospholipid transfer protein
gene markedly reduces high-density lipoprotein levels. J. Clin. Invest. 103:
907-914, 1999.
3. LeBoeuf, R. C.; Caldwell, M.; Tu, A.-Y.; Albers, J. J.: Phospholipid
transfer protein maps to distal mouse chromosome 2. Genomics 34:
259-260, 1996.
4. Spirin, V.; Schmidt, S.; Pertsemlidis, A.; Cooper, R. S.; Cohen,
J. C.; Sunyaev, S. R.: Common single-nucleotide polymorphisms act
in concert to affect plasma levels of high-density lipoprotein cholesterol. Am.
J. Hum. Genet. 81: 1298-1303, 2007.
5. Teslovich, T. M.; Musunuru, K.; Smith, A. V.; Edmondson, A. C.;
Stylianou, I. M.; Koseki, M.; Pirruccello, J. P.; Ripatti, S.; Chasman,
D. I.; Willer, C. J.; Johansen, C. T.; Fouchier, S. W.; and 197 others
: Biological, clinical and population relevance of 95 loci for blood
lipids. Nature 466: 707-713, 2010.
6. Tu, A.-Y.; Wolfbauer, G.; Albers, J. J.: Functional characterization
of the promoter region of the human phospholipid transfer protein
gene. Biochem. Biophys. Res. Commun. 217: 705-711, 1995.
7. Whitmore, T. E.; Day, J. R.; Albers, J. J.: Localization of the
human phospholipid transfer protein gene to chromosome 20q12-q13.1. Genomics 28:
599-600, 1995.
*FIELD* CN
Ada Hamosh - updated: 10/12/2010
Victor A. McKusick - updated: 11/28/2007
Victor A. McKusick - updated: 4/16/1999
Alan F. Scott - updated: 9/27/1995
*FIELD* CD
Victor A. McKusick: 5/20/1994
*FIELD* ED
alopez: 10/12/2010
carol: 3/25/2009
alopez: 12/13/2007
terry: 11/28/2007
carol: 4/19/1999
terry: 4/16/1999
terry: 6/26/1996
terry: 6/21/1996
terry: 4/17/1996
mark: 3/4/1996
terry: 2/23/1996
carol: 5/20/1994