Lap3 leucine aminopeptidase 3 [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Lap3provided by RGD
Official Full Name: leucine aminopeptidase 3provided by RGD
Primary source: RGD:1307985
See related: EnsemblRapid:ENSRNOG00000003289 AllianceGenome:RGD:1307985
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
Also known as: LAP-3
Summary: Predicted to enable peptidase activity. Predicted to be involved in proteolysis. Located in trans-Golgi network. Orthologous to human LAP3 (leucine aminopeptidase 3). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Biased expression in Liver (RPKM 979.7), Kidney (RPKM 458.6) and 9 other tissues See more
Orthologs: human mouse all
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Genomic context

Location:: 14q11

Exon count:: 13

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	14	NC_086032.1 (69820907..69839891, complement)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	14	NC_051349.1 (65608375..65627359, complement)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	14	NC_005113.4 (70102813..70121797, complement)

Chromosome 14 - NC_086032.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Cholesterol-induced leucine aminopeptidase 3 (LAP3) upregulation inhibits cell autophagy in pathogenesis of NAFLD.
Title: Cholesterol-induced leucine aminopeptidase 3 (LAP3) upregulation inhibits cell autophagy in pathogenesis of NAFLD.

Submit: New GeneRIF Correction

General gene information

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Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables carboxypeptidase activity	IEA Inferred from Electronic Annotation more info
enables manganese ion binding	IEA Inferred from Electronic Annotation more info
enables metalloaminopeptidase activity	IEA Inferred from Electronic Annotation more info
enables peptidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables peptidase 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 proteolysis	IBA Inferred from Biological aspect of Ancestor more info
involved_in proteolysis	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in mitochondrion	ISO Inferred from Sequence Orthology more info	PubMed
located_in trans-Golgi network	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: cytosol aminopeptidase

Names: LAP; cysteinylglycine-S-conjugate dipeptidase; leucyl aminopeptidase; peptidase S; proline aminopeptidase; prolyl aminopeptidase

NP_001011910.1

EC 3.4.11.1

EC 3.4.11.5

EC 3.4.13.23

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_001011910.1 → NP_001011910.1 cytosol aminopeptidase

See identical proteins and their annotated locations for NP_001011910.1

Status: PROVISIONAL

Source sequence(s)

BC079381

UniProtKB/Swiss-Prot

Q68FS4

UniProtKB/TrEMBL

A0A8I6AG50, A6IJL5

Related

ENSRNOP00000004770.3, ENSRNOT00000004770.7

Conserved Domains (1) summary

cd00433
Location:33 → 511

Peptidase_M17; Cytosol aminopeptidase family, N-terminal and catalytic domains. Family M17 contains zinc- and manganese-dependent exopeptidases ( EC 3.4.11.1), including leucine aminopeptidase. They catalyze removal of amino acids from the N-terminus of a protein and ...