Gene_Locus Report

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Gene_locus Report for: human-PNLIP

Homo sapiens (Human) triacylglycerol lipase (pancreatic lipase)

Comment
Ensembl OTTHUMG00000019103 Pancreatic lipase (EC 3.1.1.3), a 56-kD protein, is involved in the hydrolysis of dietary triglycerides to fatty acids in the intestine. This hydrolysis, which is initiated in the stomach by gastric lipase, is essential for the intestinal absorption of long-chain triglyceride fatty acids. Pancreatic colipase (120105) is a 12-kD cofactor that appears to overcome the inhibitory effects of intestinal bile salts on pancreatic lipase.Congenital pancreatic lipase deficiency is a rare, monoenzymatic form of exocrine pancreatic failure. Patients have oily/greasy stools from infancy or early childhood and the absence of discernable pancreatic disease. Failure to thrive has not been observed. Analyses of duodenal contents consistently show a marked decrease of pancreatic lipolytic activity. Fat absorption in patients my may reach 79percent, suggesting that extrapancreatic sources of lipase, such as lingual and gastric lipase, may have an important compensating role in fat digestion. Pancreatic lipase deficiency can be combined with Colipase deficiency


Relationship
Family|Pancreatic_lipase
Block| L
Position in NCBI Life Tree|Homo sapiens
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Eukaryota: N E > Opisthokonta: N E > Metazoa: N E > Eumetazoa: N E > Bilateria: N E > Deuterostomia: N E > Chordata: N E > Craniata: N E > Vertebrata: N E > Gnathostomata: N E > Teleostomi: N E > Euteleostomi: N E > Sarcopterygii: N E > Dipnotetrapodomorpha: N E > Tetrapoda: N E > Amniota: N E > Mammalia: N E > Theria: N E > Eutheria: N E > Boreoeutheria: N E > Euarchontoglires: N E > Primates: N E > Haplorrhini: N E > Simiiformes: N E > Catarrhini: N E > Hominoidea: N E > Hominidae: N E > Homininae: N E > Homo: N E > Homo sapiens: N E


Molecular evidence
Database
8 mutations: Table (e.g. : F300L, F314L, H92N ... more)
4 structures (e.g. : 1GPL, 1LPA, 1LPB... more)
Kinetic: human-PNLIP

Disease: Congenital absence of pancreatic lipase -



5 substrates (e.g. : DEHP, Retinol-palmitate, Tributyrin... more)
5 inhibitors (e.g. : Cetilistat, MUP, Oleanolic-acid... more)
2 Genbank : AL731653, J05125
1 UniProt : P16233
1 Ncbi-nid : 339596
1 Ncbi-pid : 226753
>3 Structure links 1 more: 1LPA, 1LPB, 1GPL
1 UniProt : P16233
1 Interpro : P16233
1 Pfam : P16233
1 PIRSF : P16233
1 SUPERFAM : P16233
1 EntrezGene : 5406
1 SNP : 5406
1 HUGO HGNC : 9155
1 IUPHAR : 2590
2 OMIM : 246600, 614338
1 Ensembl : ENSG00000175535
Sequence
Graphical view for this peptide sequence: human-PNLIP
Colored MSA for Pancreatic_lipase (raw)
MLPLWTLSLLLGAVAGKEVCYERLGCFSDDSPWSGITERPLHILPWSPKD
VNTRFLLYTNENPNNFQEVAADSSSISGSNFKTNRKTRFIIHGFIDKGEE
NWLANVCKNLFKVESVNCICVDWKGGSRTGYTQASQNIRIVGAEVAYFVE
FLQSAFGYSPSNVHVIGHSLGAHAAGEAGRRTNGTIGRITGLDPAEPCFQ
GTPELVRLDPSDAKFVDVIHTDGAPIVPNLGFGMSQVVGHLDFFPNGGVE
MPGCKKNILSQIVDIDGIWEGTRDFAACNHLRSYKYYTDSIVNPDGFAGF
PCASYNVFTANKCFPCPSGGCPQMGHYADRYPGKTNDVGQKFYLDTGDAS
NFARWRYKVSVTLSGKKVTGHILVSLFGNKGNSKQYEIFKGTLKPDSTHS
NEFDSDVDVGDLQMVKFIWYNNVINPTLPRVGASKIIVETNVGKQFNFCS
PETVREEVLLTLTPC
Legend This sequence has been compared to family alignement (MSA)
red => minority aminoacid
blue => majority aminoacid
color intensity => conservation rate
title => sequence position(MSA position)aminoacid rate
Catalytic site
Catalytic site in the MSA

MLPLWTLSLLLGAVAGKEVCYERLGCFSDDSPWSGITERPLHILPWSPKD
VNTRFLLYTNENPNNFQEVAADSSSISGSNFKTNRKTRFIIHGFIDKGEE
NWLANVCKNLFKVESVNCICVDWKGGSRTGYTQASQNIRIVGAEVAYFVE
FLQSAFGYSPSNVHVIGHSLGAHAAGEAGRRTNGTIGRITGLDPAEPCFQ
GTPELVRLDPSDAKFVDVIHTDGAPIVPNLGFGMSQVVGHLDFFPNGGVE
MPGCKKNILSQIVDIDGIWEGTRDFAACNHLRSYKYYTDSIVNPDGFAGF
PCASYNVFTANKCFPCPSGGCPQMGHYADRYPGKTNDVGQKFYLDTGDAS
NFARWRYKVSVTLSGKKVTGHILVSLFGNKGNSKQYEIFKGTLKPDSTHS
NEFDSDVDVGDLQMVKFIWYNNVINPTLPRVGASKIIVETNVGKQFNFCS
PETVREEVLLTLTPC


References
28 more
    Title: (-)-Epigallocatechin-3-gallate inhibits pancreatic lipase and reduces body weight gain in high fat-fed obese mice
    Grove KA, Sae-tan S, Kennett MJ, Lambert JD
    Ref: Obesity (Silver Spring), 20:2311, 2012 : PubMed

            

    Title: Structure of human pancreatic lipase
    Winkler FK, D'Arcy A, Hunziker W
    Ref: Nature, 343:771, 1990 : PubMed

            

    Title: Cloning and characterization of human pancreatic lipase cDNA
    Lowe ME, Rosenblum JL, Strauss AW
    Ref: Journal of Biological Chemistry, 264:20042, 1989 : PubMed

            


Other Papers


Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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