PLTP
entrez
5360
canonical
uniprot
P55058
canonical
ensembl
ENSG00000100979
resolver
ensp
ENSP00000335290
resolver
ensp
ENSP00000361497
resolver
ensp
ENSP00000361508
resolver
ensp
ENSP00000411671
resolver
genesymbol
PLTP
resolver
hgnc
HGNC:9093
resolver
uniprot
A8K006
resolver
uniprot
B4DDD5
resolver
uniprot
B4DRB4
resolver
uniprot
E1P5N8
resolver
uniprot
E7EV16
resolver
uniprot
Q8WTT1
resolver
uniprot
Q9BR07
resolver
uniprot
Q9BSH8
resolver
uniprot_entry
PLTP_HUMAN
resolver
uniprot_sec
A8K006
resolver
uniprot_sec
B4DDD5
resolver
uniprot_sec
B4DRB4
resolver
uniprot_sec
E1P5N8
resolver
uniprot_sec
E7EV16
resolver
uniprot_sec
Q8WTT1
resolver
uniprot_sec
Q9BR07
resolver
uniprot_sec
Q9BSH8
resolver
amino_acid_sequence
MALFGALFLALLAGAHAEFPGCKIRVTSKALELVKQEGLRFLEQELETITIPDLRGKEGHFYYNISEVKVTELQLTSSELDFQPQQELMLQITNASLGLRFRRQLLYWFFYDGGYINASAEGVSIRTGLELSRDPAGRMKVSNVSCQASVSRMHAAFGGTFKKVYDFLSTFITSGMRFLLNQQICPVLYHAGTVLLNSLLDTVPVRSSVDELVGIDYSLMKDPVASTSNLDMDFRGAFFPLTERNWSLPNRAVEPQLQEEERMVYVAFSEFFFDSAMESYFRAGALQLLLVGDKVPHDLDMLLRATYFGSIVLLSPAVIDSPLKLELRVLAPPRCTIKPSGTTISVTASVTIALVPPDQPEVQLSSMTMDARLSAKMALRGKALRTQLDLRRFRIYSNHSALESLALIPLQAPLKTMLQIGVMPMLNERTWRGVQIPLPEGINFVHEVVTNHAGFLTIGADLHFAKGLREVIEKNRPADVRASTAPTPSTAAV
uniprot
proteins
function
FUNCTION: Mediates the transfer of phospholipids and free cholesterol from triglyceride-rich lipoproteins (low density lipoproteins or LDL and very low density lipoproteins or VLDL) into high-density lipoproteins (HDL) as well as the exchange of phospholipids between triglyceride-rich lipoproteins themselves (PubMed:11013307, PubMed:19321130, PubMed:21515415, PubMed:29883800, PubMed:7654777, PubMed:9132017). Facilitates the transfer of a spectrum of different lipid molecules, including diacylglycerol, phosphatidic acid, sphingomyelin, phosphatidylcholine, phosphatidylinositol, phosphatidylglycerol, cerebroside and phosphatidyl ethanolamine (PubMed:9132017). Plays an important role in HDL remodeling which involves modulating the size and composition of HDL (PubMed:29883800). 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 (PubMed:21736953). Two distinct forms of PLTP exist in plasma: an active form that can transfer phosphatidylcholine from phospholipid vesicles to HDL, and an inactive form that lacks this capability (PubMed:11013307). {ECO:0000269|PubMed:11013307, ECO:0000269|PubMed:19321130, ECO:0000269|PubMed:21515415, ECO:0000269|PubMed:29883800, ECO:0000269|PubMed:7654777, ECO:0000269|PubMed:9132017, ECO:0000303|PubMed:21736953}.
uniprot
proteins
mass_dalton
54739
uniprot
proteins
mutagenesis
MUTAGEN 64; /note="N->A: Increased nuclear localization; when associated with A-94; A-117 and A-143."; /evidence="ECO:0000269|PubMed:19321130"; MUTAGEN 66; /note="S->A: Significant reduction in phospholipid transfer activity. No effect on secretion."; /evidence="ECO:0000269|PubMed:21515415"; MUTAGEN 94; /note="N->A: Increased nuclear localization; when associated with A-64; A-117 and A-143."; /evidence="ECO:0000269|PubMed:19321130"; MUTAGEN 96; /note="S->A: Significant reduction in phospholipid transfer activity. Increased secretion."; /evidence="ECO:0000269|PubMed:21515415"; MUTAGEN 117; /note="N->A: Increased nuclear localization; when associated with A-64; A-94 and A-143."; /evidence="ECO:0000269|PubMed:19321130"; MUTAGEN 119; /note="S->A: Significant reduction in phospholipid transfer activity. Increased secretion."; /evidence="ECO:0000269|PubMed:21515415"; MUTAGEN 143; /note="N->A: Increased nuclear localization; when associated with A-64; A-94 and A-117."; /evidence="ECO:0000269|PubMed:19321130"; MUTAGEN 145; /note="S->A: Significant reduction in phospholipid transfer activity. Reduced secretion."; /evidence="ECO:0000269|PubMed:21515415"; MUTAGEN 176; /note="M->E: Significant reduction in HDL-binding and absence of lipid transfer activity."; /evidence="ECO:0000269|PubMed:29883800"; MUTAGEN 247; /note="S->A: Significant reduction in phospholipid transfer activity. Reduced secretion."; /evidence="ECO:0000269|PubMed:21515415"; MUTAGEN 400; /note="S->A: Significant reduction in phospholipid transfer activity. Reduced secretion."; /evidence="ECO:0000269|PubMed:21515415
uniprot
proteins
post_translational_modification
PTM: Glycosylation is necessary for secretion and its phospholipid transfer activity. {ECO:0000269|PubMed:21515415}.
uniprot
proteins
protein_family
BPI/LBP family
uniprot
proteins
protein_family
BPI/LBP/Plunc superfamily
uniprot
proteins
pubmed
10333293
uniprot
proteins
pubmed
11013307
uniprot
proteins
pubmed
11780052
uniprot
proteins
pubmed
12966036
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19139490
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19321130
uniprot
proteins
pubmed
21515415
uniprot
proteins
pubmed
21736953
uniprot
proteins
pubmed
29883800
uniprot
proteins
pubmed
7654777
uniprot
proteins
pubmed
8132678
uniprot
proteins
pubmed
9132017
uniprot
proteins
sequence_length
493
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19321130}. Nucleus {ECO:0000269|PubMed:19321130}. Note=Nuclear export is XPO1/CRM1-dependent. {ECO:0000269|PubMed:19321130}.
uniprot
proteins