PNLIPRP2
entrez
5408
canonical
uniprot
P54317
canonical
ensembl
ENSG00000266200
resolver
ensembl
ENSG00000291895
resolver
ensp
ENSP00000517529
resolver
enst
ENST00000709157
resolver
genesymbol
PNLIPRP2
resolver
genesymbol_syn
PLRP2
resolver
hgnc
HGNC:9157
resolver
uniprot
A0A075B781
resolver
uniprot
A0AAG2UV77
resolver
uniprot
A8K627
resolver
uniprot
Q6IB55
resolver
uniprot_entry
A0AAG2UV77_HUMAN
resolver
uniprot_entry
LIPR2_HUMAN
resolver
uniprot_sec
A0A075B781
resolver
uniprot_sec
A8K627
resolver
uniprot_sec
Q6IB55
resolver
activity_regulation
ACTIVITY REGULATION: Regulated by CLPS and bile salts levels ranging 1-5 mM in neonates and 2-30 mM in healthy adults. CLPS stimulates milk fat digestion in the presence of 4 mM bile salts (PubMed:23732775). Triacylglycerol lipase activity toward short- and medium-chain triglycerides is inhibited by increasing concentrations of bile salts and weakly reactivated by CLPS (PubMed:15287741, PubMed:17401110, PubMed:21652702, PubMed:26494624). Optimal triacylglycerol lipase activity is reached at bile salts concentrations ranging from 0.1 to 0.5 mM and then decreases at concentrations higher than 1 mM (PubMed:15287741, PubMed:17401110, PubMed:21652702). Lipase activity toward long-chain glycerolipids is stimulated by CLPS in the presence of 4 mM bile salts (PubMed:21652702). Galactolipase activity is inhibited at high concentrations of bile salts (PubMed:20083229). Triacylglycerol lipase activity is inhibited by anti-obesity drug tetrahydrolipstatin (PubMed:17401110). {ECO:0000269|PubMed:15287741, ECO:0000269|PubMed:17401110, ECO:0000269|PubMed:20083229, ECO:0000269|PubMed:21652702, ECO:0000269|PubMed:23732775, ECO:0000269|PubMed:26494624}.
uniprot
proteins
amino_acid_sequence
MLPPWTLGLLLLATVRGKEVCYGQLGCFSDEKPWAGTLQRPVKLLPWSPEDIDTRFLLYTNENPNNFQLITGTEPDTIEASNFQLDRKTRFIIHGFLDKAEDSWPSDMCKKMFEVEKVNCICVDWRHGSRAMYTQAVQNIRVVGAETAFLIQALSTQLGYSLEDVHVIGHSLGAHTAAEAGRRLGGRVGRITGLDPAGPCFQDEPEEVRLDPSDAVFVDVIHTDSSPIVPSLGFGMSQKVGHLDFFPNGGKEMPGCKKNVLSTITDIDGIWEGIGGFVSCNHLRSFEYYSSSVLNPDGFLGYPCASYDEFQESKCFPCPAEGCPKMGHYADQFKGKTSAVEQTFFLNTGESGNFTSWRYKISVTLSGKEKVNGYIRIALYGSNENSKQYEIFKGSLKPDASHTCAIDVDFNVGKIQKVKFLWNKRGINLSEPKLGASQITVQSGEDGTEYNFCSSDTVEENVLQSLYPC
uniprot
proteins
ec_number
3.1.1.26
uniprot
proteins
ec_number
3.1.1.3
uniprot
proteins
function
FUNCTION: Lipase that primarily hydrolyzes triglycerides and galactosylglycerides (PubMed:15287741, PubMed:17401110, PubMed:18702514, PubMed:19451396, PubMed:20083229, PubMed:21865348, PubMed:26494624). In neonates, may play a major role in pancreatic digestion of dietary fats such as milk fat globules enriched in long-chain triglycerides (PubMed:19824014, PubMed:21652702, PubMed:23732775). Hydrolyzes short-, medium- and long-chain fatty acyls in triglycerides without apparent positional specificity (PubMed:15287741, PubMed:17401110, PubMed:18702514, PubMed:21652702, PubMed:21865348). Can completely deacylate triacylglycerols (PubMed:21865348). When the liver matures and bile salt synthesis increases, likely functions mainly as a galactolipase and monoacylglycerol lipase. Hydrolyzes monogalactosyldiglycerols (MGDG) and digalactosyldiacylglycerols (DGDG) present in a plant-based diet, releasing long-chain polyunsaturated fatty acids (PubMed:15287741, PubMed:17401110, PubMed:18702514, PubMed:20083229, PubMed:26494624). Hydrolyzes medium- and long-chain fatty acyls in galactolipids (PubMed:18702514, PubMed:20083229). May act together with LIPF to hydrolyze partially digested triglycerides (PubMed:23732775). Hydrolyzes long-chain monoglycerides with high efficiency (PubMed:17401110, PubMed:21652702, PubMed:23732775). In cytotoxic T cells, contributes to perforin-dependent cell lysis, but is unlikely to mediate direct cytotoxicity (By similarity). Also has low phospholipase activity (PubMed:17401110, PubMed:18702514). In neurons, required for the localization of the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) to neurite tips through acyl chain remodeling of membrane phospholipids (By similarity). The resulting OPPC-rich lipid membrane domain recruits the t-SNARE protein STX4 by selectively interacting with the STX4 transmembrane domain and this promotes surface expression of the dopamine transporter SLC6A3/DAT at neurite tips by facilitating fusion of SLC6A3-containing transport vesicles with the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P17892, ECO:0000250|UniProtKB:P54318, ECO:0000269|PubMed:15287741, ECO:0000269|PubMed:17401110, ECO:0000269|PubMed:18702514, ECO:0000269|PubMed:19451396, ECO:0000269|PubMed:19824014, ECO:0000269|PubMed:20083229, ECO:0000269|PubMed:21652702, ECO:0000269|PubMed:21865348, ECO:0000269|PubMed:23732775, ECO:0000269|PubMed:26494624}.
uniprot
proteins
mass_dalton
51961
uniprot
proteins
mutagenesis
MUTAGEN 353; /note="N->Q: Loss of N-glycosylation."; /evidence="ECO:0000269|PubMed:18702514
uniprot
proteins
pathway_participation
PATHWAY: Glycerolipid metabolism; triacylglycerol degradation. {ECO:0000269|PubMed:21865348}.; PATHWAY: Glycolipid metabolism. {ECO:0000269|PubMed:20083229}.
uniprot
proteins
protein_family
AB hydrolase superfamily
uniprot
proteins
protein_family
Lipase family
uniprot
proteins
pubmed
10674344
uniprot
proteins
pubmed
1379598
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15287741
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17401110
uniprot
proteins
pubmed
18702514
uniprot
proteins
pubmed
19451396
uniprot
proteins
pubmed
19824014
uniprot
proteins
pubmed
20083229
uniprot
proteins
pubmed
20445095
uniprot
proteins
pubmed
21652702
uniprot
proteins
pubmed
21865348
uniprot
proteins
pubmed
23732775
uniprot
proteins
pubmed
26494624
uniprot
proteins
pubmed
30408063
uniprot
proteins
sequence_length
469
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18702514, ECO:0000269|PubMed:19824014}. Zymogen granule membrane {ECO:0000250|UniProtKB:P54318}; Peripheral membrane protein {ECO:0000250|UniProtKB:P54318}. Cell projection, neuron projection {ECO:0000250|UniProtKB:P54318}. Note=Localizes to neurite tips in neuronal cells. {ECO:0000250|UniProtKB:P54318}.
uniprot
proteins