PNLIP pancreatic lipase [Sus scrofa (pig)] - Gene

Summary

Official Symbol: PNLIPprovided by VGNC
Official Full Name: pancreatic lipaseprovided by VGNC
Primary source: VGNC:VGNC:91597
See related: Ensembl:ENSSSCG00000010658
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Sus scrofa
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus
Also known as: PL; PTL
Annotation information: Annotation category: partial on reference assembly
Expression: Low expression observed in reference dataset See more
Orthologs: human mouse all
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Genomic context

Location:: chromosome: 14

Exon count:: 12

Annotation release	Status	Assembly	Chr	Location
106	current	Sscrofa11.1 (GCF_000003025.6)	14	NC_010456.5 (126771920..126789097)
105	previous assembly	Sscrofa10.2 (GCF_000003025.5)	14	NC_010456.4 (138017775..138032310)

Chromosome 14 - NC_010456.5 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Transcriptome data used for gene annotation Transcriptome data used for gene annotation
Description: Nine kinds of tissues and a mixture of multiple tissues were sequenced for genome annotation
BioProject: PRJNA311523
Publication: PMID 27646534
Analysis date: Thu Dec 14 17:10:49 2017

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

PPL in closed conformation is stable in water and the open conformation is driven towards closed state. The lid follows a swirling trajectory during the closure. Conformational state of the lid regulates the activity and substrate specificity of PPL. Hence, it is essential to understand the lid dynamics and the role of specific amino acid residues involved.
Title: Lid closure dynamics of porcine pancreatic lipase in aqueous solution.
Only the double mutant at higher temperature showed lid opening movement suggesting the essential role of the three residues in holding the lid in closed conformation. The lid opening dynamics was faster in octanol than water suggesting that non-polar solvents favor open conformation of the lid.
Title: Lid dynamics of porcine pancreatic lipase in non-aqueous solvents.

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General gene information

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Markers

SW761 (e-PCR), detects polymorphism
- UniSTS:252049

Gene Ontology Provided by RefSeq

Function	Evidence Code	Pubs
enables protein binding	IEA Inferred from Electronic Annotation more info	PubMed
enables triacylglycerol lipase activity	IEA Inferred from Electronic Annotation more info	PubMed

Process	Evidence Code	Pubs
involved_in lipid metabolic process	IEA Inferred from Electronic Annotation more info	PubMed

General protein information

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Preferred Names: pancreatic triacylglycerol lipase

NP_001171383.1

EC 3.1.1.3

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001177912.2 → NP_001171383.1 pancreatic triacylglycerol lipase precursor

See identical proteins and their annotated locations for NP_001171383.1

Status: PROVISIONAL

Source sequence(s)

GU576971

UniProtKB/TrEMBL

A0A4X1T0H9, D4P6H2

Related

ENSSSCP00000072179.1, ENSSSCT00000081695.2

Conserved Domains (3) summary

cd00707
Location:51 → 348

Pancreat_lipase_like; Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the ...

cd01759
Location:355 → 465

PLAT_PL; PLAT/LH2 domain of pancreatic triglyceride lipase. Lipases hydrolyze phospholipids and triglycerides to generate fatty acids for energy production or for storage and to release inositol phosphates that act as second messengers. The central role of ...

pfam00151
Location:17 → 352

Lipase; Lipase