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Phospholipid transfer protein (Lipid transfer protein II)

 PLTP_HUMAN              Reviewed;         493 AA.
P55058; A8K006; B4DDD5; B4DRB4; E1P5N8; E7EV16; Q8WTT1; Q9BR07;
Q9BSH8;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-APR-2018, entry version 171.
RecName: Full=Phospholipid transfer protein;
AltName: Full=Lipid transfer protein II;
Flags: Precursor;
Name=PLTP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 18-27
AND 163-184.
TISSUE=Umbilical vein endothelial cell;
PubMed=8132678;
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]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
Kobayashi Y., Ohshiro N., Shibusawa A., Sasaki T., Tokuyama S.,
Yamamoto T.;
"Molecular cloning and functional characterization of phospholipid
transfer protein from human placenta cDNA library.";
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1),
AND VARIANTS TYR-124 AND ILE-425.
SeattleSNPs variation discovery resource;
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
TISSUE=Adipose tissue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
DISULFIDE BOND.
PubMed=10333293; DOI=10.1023/A:1020628006453;
Qu S.J., Fan H.Z., Kilinc C., Pownall H.J.;
"Role of cysteine residues in human plasma phospholipid transfer
protein.";
J. Protein Chem. 18:193-198(1999).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64; ASN-94; ASN-143;
ASN-245 AND ASN-398.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[12]
GLYCOSYLATION AT ASN-64; ASN-143 AND ASN-245.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[13]
REVIEW ON FUNCTION.
PubMed=21736953; DOI=10.1016/j.bbalip.2011.06.013;
Albers J.J., Vuletic S., Cheung M.C.;
"Role of plasma phospholipid transfer protein in lipid and lipoprotein
metabolism.";
Biochim. Biophys. Acta 1821:345-357(2012).
[14]
VARIANTS GLN-282; HIS-372 AND TRP-380.
PubMed=12966036; DOI=10.1093/hmg/ddg314;
Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S.,
Alvin G.B., Das K., Gilliam T.C.;
"Association of extreme blood lipid profile phenotypic variation with
11 reverse cholesterol transport genes and 10 non-genetic
cardiovascular disease risk factors.";
Hum. Mol. Genet. 12:2733-2743(2003).
-!- FUNCTION: Facilitates the transfer of a spectrum of different
lipid molecules, including diacylglycerol, phosphatidic acid,
sphingomyelin, phosphatidylcholine, phosphatidylglycerol,
cerebroside and phosphatidyl ethanolamine. Essential for the
transfer of excess surface lipids from triglyceride-rich
lipoproteins to HDL, thereby facilitating the formation of smaller
lipoprotein remnants, contributing to the formation of LDL, and
assisting in the maturation of HDL particles. PLTP also plays a
key role in the uptake of cholesterol from peripheral cells and
tissues that is subsequently transported to the liver for
degradation and excretion. Two distinct forms of PLTP exist in
plasma: an active form that can transfer PC from phospholipid
vesicles to high-density lipoproteins (HDL), and an inactive form
that lacks this capability.
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P55058-1; Sequence=Displayed;
Name=2;
IsoId=P55058-2; Sequence=VSP_003050;
Name=3;
IsoId=P55058-3; Sequence=VSP_045877;
Note=No experimental confirmation available.;
Name=4;
IsoId=P55058-4; Sequence=VSP_054028;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Wide tissue distribution. Placenta > pancreas
> lung > kidney > heart > liver > skeletal muscle > brain.
-!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/pltp/";
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EMBL; L26232; AAA36443.1; -; mRNA.
EMBL; AB076694; BAB79630.1; -; mRNA.
EMBL; AL008726; CAA15499.1; -; Genomic_DNA.
EMBL; AK289371; BAF82060.1; -; mRNA.
EMBL; AK293150; BAG56696.1; -; mRNA.
EMBL; AK299181; BAG61226.1; -; mRNA.
EMBL; AL008726; CAC36020.1; -; Genomic_DNA.
EMBL; AY509570; AAR87775.1; -; Genomic_DNA.
EMBL; CH471077; EAW75782.1; -; Genomic_DNA.
EMBL; CH471077; EAW75781.1; -; Genomic_DNA.
EMBL; CH471077; EAW75783.1; -; Genomic_DNA.
EMBL; CH471077; EAW75785.1; -; Genomic_DNA.
EMBL; CH471077; EAW75787.1; -; Genomic_DNA.
EMBL; BC005045; AAH05045.1; -; mRNA.
EMBL; BC019847; AAH19847.1; -; mRNA.
EMBL; BC019898; AAH19898.1; -; mRNA.
CCDS; CCDS13386.1; -. [P55058-1]
CCDS; CCDS13387.1; -. [P55058-2]
CCDS; CCDS56196.1; -. [P55058-4]
CCDS; CCDS56197.1; -. [P55058-3]
PIR; A53533; A53533.
RefSeq; NP_001229849.1; NM_001242920.1. [P55058-3]
RefSeq; NP_001229850.1; NM_001242921.1. [P55058-4]
RefSeq; NP_006218.1; NM_006227.3. [P55058-1]
RefSeq; NP_872617.1; NM_182676.2. [P55058-2]
UniGene; Hs.439312; -.
ProteinModelPortal; P55058; -.
BioGrid; 111374; 36.
IntAct; P55058; 1.
STRING; 9606.ENSP00000361508; -.
BindingDB; P55058; -.
ChEMBL; CHEMBL5962; -.
SwissLipids; SLP:000000469; -.
TCDB; 1.C.40.1.4; the bactericidal permeability increasing protein (bpip) family.
GlyConnect; 683; -.
iPTMnet; P55058; -.
PhosphoSitePlus; P55058; -.
UniCarbKB; P55058; -.
BioMuta; PLTP; -.
DMDM; 1709662; -.
EPD; P55058; -.
MaxQB; P55058; -.
PaxDb; P55058; -.
PeptideAtlas; P55058; -.
PRIDE; P55058; -.
TopDownProteomics; P55058-1; -. [P55058-1]
DNASU; 5360; -.
Ensembl; ENST00000354050; ENSP00000335290; ENSG00000100979. [P55058-2]
Ensembl; ENST00000372420; ENSP00000361497; ENSG00000100979. [P55058-4]
Ensembl; ENST00000372431; ENSP00000361508; ENSG00000100979. [P55058-1]
Ensembl; ENST00000420868; ENSP00000411671; ENSG00000100979. [P55058-3]
Ensembl; ENST00000477313; ENSP00000417138; ENSG00000100979. [P55058-1]
GeneID; 5360; -.
KEGG; hsa:5360; -.
UCSC; uc002xql.3; human. [P55058-1]
CTD; 5360; -.
DisGeNET; 5360; -.
EuPathDB; HostDB:ENSG00000100979.14; -.
GeneCards; PLTP; -.
HGNC; HGNC:9093; PLTP.
HPA; CAB032873; -.
MIM; 172425; gene.
neXtProt; NX_P55058; -.
OpenTargets; ENSG00000100979; -.
PharmGKB; PA273; -.
eggNOG; KOG4160; Eukaryota.
eggNOG; ENOG410Z88E; LUCA.
GeneTree; ENSGT00730000110583; -.
HOGENOM; HOG000231006; -.
HOVERGEN; HBG103156; -.
InParanoid; P55058; -.
KO; K08761; -.
OMA; RGVQIPL; -.
OrthoDB; EOG091G058L; -.
PhylomeDB; P55058; -.
TreeFam; TF315617; -.
Reactome; R-HSA-8964058; HDL remodeling.
SignaLink; P55058; -.
GeneWiki; Phospholipid_transfer_protein; -.
GenomeRNAi; 5360; -.
PMAP-CutDB; P55058; -.
PRO; PR:P55058; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000100979; -.
CleanEx; HS_PLTP; -.
Genevisible; P55058; HS.
GO; GO:0005576; C:extracellular region; TAS:ProtInc.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:0034364; C:high-density lipoprotein particle; IDA:BHF-UCL.
GO; GO:0097001; F:ceramide binding; IDA:BHF-UCL.
GO; GO:0035620; F:ceramide transporter activity; IDA:BHF-UCL.
GO; GO:0019992; F:diacylglycerol binding; IDA:BHF-UCL.
GO; GO:0005319; F:lipid transporter activity; IDA:BHF-UCL.
GO; GO:0070300; F:phosphatidic acid binding; IDA:BHF-UCL.
GO; GO:1990050; F:phosphatidic acid transporter activity; IDA:BHF-UCL.
GO; GO:0031210; F:phosphatidylcholine binding; IDA:BHF-UCL.
GO; GO:0008525; F:phosphatidylcholine transporter activity; IDA:BHF-UCL.
GO; GO:0008429; F:phosphatidylethanolamine binding; IDA:BHF-UCL.
GO; GO:1904121; F:phosphatidylethanolamine transporter activity; IDA:BHF-UCL.
GO; GO:1901611; F:phosphatidylglycerol binding; IDA:BHF-UCL.
GO; GO:0005548; F:phospholipid transporter activity; IDA:BHF-UCL.
GO; GO:0035627; P:ceramide transport; IDA:BHF-UCL.
GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
GO; GO:0034375; P:high-density lipoprotein particle remodeling; IDA:AgBase.
GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
GO; GO:0006869; P:lipid transport; IDA:BHF-UCL.
GO; GO:0015914; P:phospholipid transport; IDA:BHF-UCL.
GO; GO:0010875; P:positive regulation of cholesterol efflux; IDA:AgBase.
GO; GO:0010189; P:vitamin E biosynthetic process; IEA:Ensembl.
InterPro; IPR017943; Bactericidal_perm-incr_a/b_dom.
InterPro; IPR030675; BPI/LBP.
InterPro; IPR032942; BPI/LBP/Plunc.
InterPro; IPR001124; Lipid-bd_serum_glycop_C.
InterPro; IPR017954; Lipid-bd_serum_glycop_CS.
InterPro; IPR017942; Lipid-bd_serum_glycop_N.
InterPro; IPR030179; PLTP.
PANTHER; PTHR10504; PTHR10504; 1.
PANTHER; PTHR10504:SF16; PTHR10504:SF16; 1.
Pfam; PF01273; LBP_BPI_CETP; 1.
Pfam; PF02886; LBP_BPI_CETP_C; 1.
PIRSF; PIRSF002417; Lipid_binding_protein; 1.
SMART; SM00328; BPI1; 1.
SMART; SM00329; BPI2; 1.
SUPFAM; SSF55394; SSF55394; 2.
PROSITE; PS00400; LBP_BPI_CETP; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Lipid transport; Polymorphism;
Reference proteome; Secreted; Signal; Transport.
SIGNAL 1 17 {ECO:0000269|PubMed:8132678}.
CHAIN 18 493 Phospholipid transfer protein.
/FTId=PRO_0000017162.
CARBOHYD 64 64 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218}.
CARBOHYD 94 94 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 117 117 N-linked (GlcNAc...) (complex)
asparagine.
CARBOHYD 143 143 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490}.
CARBOHYD 245 245 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490}.
CARBOHYD 398 398 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
DISULFID 146 185 {ECO:0000269|PubMed:10333293}.
VAR_SEQ 1 88 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054028.
VAR_SEQ 68 162 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045877.
VAR_SEQ 110 162 FYDGGYINASAEGVSIRTGLELSRDPAGRMKVSNVSCQASV
SRMHAAFGGTFK -> L (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_003050.
VARIANT 124 124 S -> Y (in dbSNP:rs11569636).
{ECO:0000269|Ref.3}.
/FTId=VAR_018879.
VARIANT 282 282 R -> Q (in dbSNP:rs56126980).
{ECO:0000269|PubMed:12966036}.
/FTId=VAR_017020.
VARIANT 372 372 R -> H (in dbSNP:rs144710772).
{ECO:0000269|PubMed:12966036}.
/FTId=VAR_017021.
VARIANT 380 380 R -> W (in dbSNP:rs6065903).
{ECO:0000269|PubMed:12966036}.
/FTId=VAR_017022.
VARIANT 425 425 M -> I (in dbSNP:rs11569675).
{ECO:0000269|Ref.3}.
/FTId=VAR_018880.
VARIANT 444 444 F -> L (in dbSNP:rs1804161).
/FTId=VAR_012073.
VARIANT 487 487 T -> K (in dbSNP:rs1056929).
/FTId=VAR_012074.
CONFLICT 18 18 E -> V (in Ref. 7; AAH19847/AAH19898).
{ECO:0000305}.
CONFLICT 331 331 A -> V (in Ref. 4; BAG61226).
{ECO:0000305}.
CONFLICT 375 375 A -> S (in Ref. 4; BAG56696).
{ECO:0000305}.
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


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U0814h CLIA CETP,Cholesteryl ester transfer protein,Homo sapiens,Human,Lipid transfer protein I 96T
E0814Rb ELISA CETP,Cholesteryl ester transfer protein,Lipid transfer protein I,Oryctolagus cuniculus,Rabbit 96T
U0814Rb CLIA CETP,Cholesteryl ester transfer protein,Lipid transfer protein I,Oryctolagus cuniculus,Rabbit 96T
E1515Hu Human cholest erolester transfer protein per lipid transfer protein,CETP per LTP ELISA Kit 48T
E1515Hu Human cholest erolester transfer protein-lipid transfer protein,CETP-LTP ELISA Kit 48T
YHB0694Hu Human cholest erolester transfer protein-lipid transfer protein,CETP-LTP ELISA Kit 48T
SL0449Hu Human cholest erolester transfer protein lipid transfer protein,CETP LTP ELISA Kit 96T
E1515Hu Human cholest erolester transfer protein per lipid transfer protein,CETP per LTP ELISA Kit 96T
E1515Hu Human cholest erolester transfer protein-lipid transfer protein,CETP-LTP ELISA Kit 96T
YHB0694Hu Human cholest erolester transfer protein-lipid transfer protein,CETP-LTP ELISA Kit 96T
UB-E03917 Human cholest erolester transfer protein per lipid transfer protein(CETP per LTP)ELISA Kit 96T
EIAAB31992 Homo sapiens,Human,PCTP,PC-TP,Phosphatidylcholine transfer protein,StARD2,STARD2,StAR-related lipid transfer protein 2,START domain-containing protein 2
EIAAB31993 Pctp,PC-TP,Phosphatidylcholine transfer protein,Rat,Rattus norvegicus,StARD2,Stard2,StAR-related lipid transfer protein 2,START domain-containing protein 2
EIAAB31990 Mouse,Mus musculus,Pctp,PC-TP,Phosphatidylcholine transfer protein,StARD2,Stard2,StAR-related lipid transfer protein 2,START domain-containing protein 2
EIAAB31991 Bos taurus,Bovine,PCTP,PC-TP,Phosphatidylcholine transfer protein,StARD2,STARD2,StAR-related lipid transfer protein 2,START domain-containing protein 2
EIAAB04828 Ceramide transfer protein,Col4a3bp,Collagen type IV alpha-3-binding protein,Goodpasture antigen-binding protein,GPBP,Mouse,Mus musculus,StARD11,Stard11,StAR-related lipid transfer protein 11,START dom
EIAAB04829 Bos taurus,Bovine,Ceramide transfer protein,COL4A3BP,Collagen type IV alpha-3-binding protein,Goodpasture antigen-binding protein,GPBP,StARD11,STARD11,StAR-related lipid transfer protein 11,START doma
EIAAB04830 Ceramide transfer protein,CERT,COL4A3BP,Collagen type IV alpha-3-binding protein,Goodpasture antigen-binding protein,GPBP,hCERT,Homo sapiens,Human,StARD11,STARD11,StAR-related lipid transfer protein 1
290-65401 Human CETP ELISA Kit Wako Cholesteryl ester transfer protein (CETP), also called plasma lipid transfer protein, is a plasma protein that facilitates the transport of cholesteryl esters and triglyceri 72 tests
27-090 SCP2 protein is thought to be an intracellular lipid transfer protein. SCP2 is highly expressed in organs involved in lipid metabolism, and may play a role in Zellweger syndrome, in which cells are de 0.05 mg


 

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