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P55058 (PLTP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phospholipid transfer protein
Alternative name(s):
Lipid transfer protein II
Gene names
Name:PLTP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Tissue specificity

Wide tissue distribution. Placenta > pancreas > lung > kidney > heart > liver > skeletal muscle > brain.

Sequence similarities

Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P55058-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P55058-2)

The sequence of this isoform differs from the canonical sequence as follows:
     110-162: FYDGGYINASAEGVSIRTGLELSRDPAGRMKVSNVSCQASVSRMHAAFGGTFK → L
Isoform 3 (identifier: P55058-3)

The sequence of this isoform differs from the canonical sequence as follows:
     68-162: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: P55058-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-88: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.1
Chain18 – 493476Phospholipid transfer protein
PRO_0000017162

Amino acid modifications

Glycosylation641N-linked (GlcNAc...) (complex) Ref.9 Ref.11 Ref.12
Glycosylation941N-linked (GlcNAc...) Ref.9
Glycosylation1171N-linked (GlcNAc...) (complex)
Glycosylation1431N-linked (GlcNAc...) Ref.9 Ref.12
Glycosylation2451N-linked (GlcNAc...) (complex) Ref.9 Ref.12
Glycosylation3981N-linked (GlcNAc...) Ref.9
Disulfide bond146 ↔ 185 Ref.8

Natural variations

Alternative sequence1 – 8888Missing in isoform 4.
VSP_054028
Alternative sequence68 – 16295Missing in isoform 3.
VSP_045877
Alternative sequence110 – 16253FYDGG…GGTFK → L in isoform 2.
VSP_003050
Natural variant1241S → Y. Ref.3
Corresponds to variant rs11569636 [ dbSNP | Ensembl ].
VAR_018879
Natural variant2821R → Q. Ref.14
VAR_017020
Natural variant3721R → H. Ref.14
VAR_017021
Natural variant3801R → W. Ref.14
Corresponds to variant rs6065903 [ dbSNP | Ensembl ].
VAR_017022
Natural variant4251M → I. Ref.3
Corresponds to variant rs11569675 [ dbSNP | Ensembl ].
VAR_018880
Natural variant4441F → L.
Corresponds to variant rs1804161 [ dbSNP | Ensembl ].
VAR_012073
Natural variant4871T → K.
Corresponds to variant rs1056929 [ dbSNP | Ensembl ].
VAR_012074

Experimental info

Sequence conflict181E → V in AAH19847. Ref.7
Sequence conflict181E → V in AAH19898. Ref.7
Sequence conflict3311A → V in BAG61226. Ref.4
Sequence conflict3751A → S in BAG56696. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: C6E4852F18E12317

FASTA49354,739
        10         20         30         40         50         60 
MALFGALFLA LLAGAHAEFP GCKIRVTSKA LELVKQEGLR FLEQELETIT IPDLRGKEGH 

        70         80         90        100        110        120 
FYYNISEVKV TELQLTSSEL DFQPQQELML QITNASLGLR FRRQLLYWFF YDGGYINASA 

       130        140        150        160        170        180 
EGVSIRTGLE LSRDPAGRMK VSNVSCQASV SRMHAAFGGT FKKVYDFLST FITSGMRFLL 

       190        200        210        220        230        240 
NQQICPVLYH AGTVLLNSLL DTVPVRSSVD ELVGIDYSLM KDPVASTSNL DMDFRGAFFP 

       250        260        270        280        290        300 
LTERNWSLPN RAVEPQLQEE ERMVYVAFSE FFFDSAMESY FRAGALQLLL VGDKVPHDLD 

       310        320        330        340        350        360 
MLLRATYFGS IVLLSPAVID SPLKLELRVL APPRCTIKPS GTTISVTASV TIALVPPDQP 

       370        380        390        400        410        420 
EVQLSSMTMD ARLSAKMALR GKALRTQLDL RRFRIYSNHS ALESLALIPL QAPLKTMLQI 

       430        440        450        460        470        480 
GVMPMLNERT WRGVQIPLPE GINFVHEVVT NHAGFLTIGA DLHFAKGLRE VIEKNRPADV 

       490 
RASTAPTPST AAV 

« Hide

Isoform 2 [UniParc].

Checksum: 4D7435F89F79ABAA
Show »

FASTA44149,272
Isoform 3 [UniParc].

Checksum: 6D2141C6899E98CB
Show »

FASTA39844,135
Isoform 4 [UniParc].

Checksum: B916DC8F704401C0
Show »

FASTA40544,847

References

« Hide 'large scale' references
[1]"Complete cDNA encoding human phospholipid transfer protein from human endothelial cells."
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.
J. Biol. Chem. 269:9388-9391(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 18-27 AND 163-184.
Tissue: Umbilical vein endothelial cell.
[2]"Molecular cloning and functional characterization of phospholipid transfer protein from human placenta cDNA library."
Kobayashi Y., Ohshiro N., Shibusawa A., Sasaki T., Tokuyama S., Yamamoto T.
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[3]SeattleSNPs variation discovery resource
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM1 1), VARIANTS TYR-124 AND ILE-425.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
Tissue: Adipose tissue.
[5]"The DNA sequence and comparative analysis of human chromosome 20."
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. expand/collapse author list , 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.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain and Placenta.
[8]"Role of cysteine residues in human plasma phospholipid transfer protein."
Qu S.J., Fan H.Z., Kilinc C., Pownall H.J.
J. Protein Chem. 18:193-198(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BOND.
[9]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64; ASN-94; ASN-143; ASN-245 AND ASN-398.
Tissue: Plasma.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64.
Tissue: Liver.
[12]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
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.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-64; ASN-143 AND ASN-245.
[13]"Role of plasma phospholipid transfer protein in lipid and lipoprotein metabolism."
Albers J.J., Vuletic S., Cheung M.C.
Biochim. Biophys. Acta 1821:345-357(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[14]"Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors."
Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S., Alvin G.B., Das K., Gilliam T.C.
Hum. Mol. Genet. 12:2733-2743(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLN-282; HIS-372 AND TRP-380.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L26232 mRNA. Translation: AAA36443.1.
AB076694 mRNA. Translation: BAB79630.1.
AL008726 Genomic DNA. Translation: CAA15499.1.
AK289371 mRNA. Translation: BAF82060.1.
AK293150 mRNA. Translation: BAG56696.1.
AK299181 mRNA. Translation: BAG61226.1.
AL008726 Genomic DNA. Translation: CAC36020.1.
AY509570 Genomic DNA. Translation: AAR87775.1.
CH471077 Genomic DNA. Translation: EAW75782.1.
CH471077 Genomic DNA. Translation: EAW75781.1.
CH471077 Genomic DNA. Translation: EAW75783.1.
CH471077 Genomic DNA. Translation: EAW75785.1.
CH471077 Genomic DNA. Translation: EAW75787.1.
BC005045 mRNA. Translation: AAH05045.1.
BC019847 mRNA. Translation: AAH19847.1.
BC019898 mRNA. Translation: AAH19898.1.
CCDSCCDS13386.1. [P55058-1]
CCDS13387.1. [P55058-2]
CCDS56197.1. [P55058-3]
PIRA53533.
RefSeqNP_001229849.1. NM_001242920.1. [P55058-3]
NP_001229850.1. NM_001242921.1. [P55058-4]
NP_006218.1. NM_006227.3. [P55058-1]
NP_872617.1. NM_182676.2. [P55058-2]
UniGeneHs.439312.

3D structure databases

ProteinModelPortalP55058.
SMRP55058. Positions 20-462.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111374. 3 interactions.
STRING9606.ENSP00000361508.

Chemistry

BindingDBP55058.
ChEMBLCHEMBL5962.

Protein family/group databases

TCDB1.C.40.1.4. the bactericidal permeability increasing protein (bpip) family.

PTM databases

PhosphoSiteP55058.

Polymorphism databases

DMDM1709662.

Proteomic databases

MaxQBP55058.
PaxDbP55058.
PRIDEP55058.

Protocols and materials databases

DNASU5360.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354050; ENSP00000335290; ENSG00000100979. [P55058-2]
ENST00000372431; ENSP00000361508; ENSG00000100979. [P55058-1]
ENST00000420868; ENSP00000411671; ENSG00000100979. [P55058-3]
ENST00000477313; ENSP00000417138; ENSG00000100979. [P55058-1]
GeneID5360.
KEGGhsa:5360.
UCSCuc002xql.2. human. [P55058-1]
uc002xqo.2. human. [P55058-2]

Organism-specific databases

CTD5360.
GeneCardsGC20M044528.
HGNCHGNC:9093. PLTP.
HPACAB032873.
MIM172425. gene.
neXtProtNX_P55058.
PharmGKBPA273.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG290011.
HOGENOMHOG000231006.
HOVERGENHBG103156.
InParanoidP55058.
KOK08761.
OrthoDBEOG76739B.
PhylomeDBP55058.
TreeFamTF315617.

Enzyme and pathway databases

SignaLinkP55058.

Gene expression databases

ArrayExpressP55058.
BgeeP55058.
CleanExHS_PLTP.
GenevestigatorP55058.

Family and domain databases

InterProIPR017943. Bactericidal_perm-incr_a/b_dom.
IPR001124. Lipid-bd_serum_glycop_C.
IPR017954. Lipid-bd_serum_glycop_CS.
IPR017942. Lipid-bd_serum_glycop_N.
[Graphical view]
PfamPF01273. LBP_BPI_CETP. 1 hit.
PF02886. LBP_BPI_CETP_C. 1 hit.
[Graphical view]
SMARTSM00328. BPI1. 1 hit.
SM00329. BPI2. 1 hit.
[Graphical view]
SUPFAMSSF55394. SSF55394. 2 hits.
PROSITEPS00400. LBP_BPI_CETP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPhospholipid_transfer_protein.
GenomeRNAi5360.
NextBio20778.
PMAP-CutDBP55058.
PROP55058.
SOURCESearch...

Entry information

Entry namePLTP_HUMAN
AccessionPrimary (citable) accession number: P55058
Secondary accession number(s): A8K006 expand/collapse secondary AC list , B4DDD5, B4DRB4, E1P5N8, E7EV16, Q8WTT1, Q9BR07, Q9BSH8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM