Lipi lipase I [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Lipiprovided by RGD
Official Full Name: lipase Iprovided by RGD
Primary source: RGD:1310162
See related: EnsemblRapid:ENSRNOG00000033441 AllianceGenome:RGD:1310162
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Summary: Predicted to enable heparin binding activity and phospholipase activity. Predicted to be involved in lipid catabolic process. Predicted to be located in plasma membrane. Predicted to be active in extracellular space. Orthologous to human LIPI (lipase I). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Low expression observed in reference dataset See more
Orthologs: human mouse all
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Genomic context

Location:: 11p11

Exon count:: 11

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	11	NC_086029.1 (27676354..27716025, complement)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	11	NC_051346.1 (14189323..14228992, complement)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	11	NC_005110.4 (13960246..13999869, complement)

Chromosome 11 - NC_086029.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages
Description: 320 RNA samples isolated from 11 organs (adrenal gland, brain, heart, kidney, liver, lung, muscle, spleen, thymus, and testes or uterus) from both sexes of Fischer 344 rats across four developmental stages (2-, 6-, 21-, and 104-weeks-old)
BioProject: PRJNA238328
Publication: PMID 24510058
Analysis date: Mon Jun 6 17:44:12 2016

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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General gene information

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Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables heparin binding	ISO Inferred from Sequence Orthology more info
enables phospholipase activity	IBA Inferred from Biological aspect of Ancestor more info
enables phospholipase activity	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in biological_process	ND No biological Data available more info
involved_in lipid catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in lipid catabolic process	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
is_active_in extracellular space	IBA Inferred from Biological aspect of Ancestor more info
located_in extracellular space	ISO Inferred from Sequence Orthology more info
located_in plasma membrane	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: lipase member I

Names: lipase, member H; lipase, member I

NP_001099369.1

EC 2.7.11.30

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_001105899.1 → NP_001099369.1 lipase member I precursor

See identical proteins and their annotated locations for NP_001099369.1

Status: PROVISIONAL

Source sequence(s)

CH473989

UniProtKB/TrEMBL

A6JL12, D3ZMG4

Related

ENSRNOP00000041652.3, ENSRNOT00000045835.7

Conserved Domains (1) summary

cd00707
Location:57 → 346

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 ...