Enpep glutamyl aminopeptidase [Rattus norvegicus (Norway rat)] - Gene

Summary

Symbol: Enpepprovided by RGD
Full Name: glutamyl aminopeptidaseprovided by RGD
Primary source: RGD:621228
See related: EnsemblRapid:ENSRNOG00000051854 AllianceGenome:RGD:621228
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Summary: Enables aminopeptidase activity and peptide binding activity. Involved in peptide catabolic process and protein processing. Located in brush border membrane. Orthologous to human ENPEP (glutamyl aminopeptidase). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Biased expression in Kidney (RPKM 612.5), Lung (RPKM 262.1) and 6 other tissues See more
Orthologs: human mouse all
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Genomic context

Location:: 2q42

Exon count:: 20

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	2	NC_086020.1 (220456258..220526218, complement)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	2	NC_051337.1 (217781985..217851947, complement)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	2	NC_005101.4 (233667253..233743866, complement)

Chromosome 2 - NC_086020.1 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: 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?

Chromosome 2 Fragment Substitutions in Dahl Salt-Sensitive Rats and RNA Sequencing Identified Enpep and Hs2st1 as Vascular Inflammatory Modulators.
Title: Chromosome 2 Fragment Substitutions in Dahl Salt-Sensitive Rats and RNA Sequencing Identified Enpep and Hs2st1 as Vascular Inflammatory Modulators.
A discrepancy between the high expression of AP-A in kidney of hyperthyroid rats and the low activity of AP-A measured in plasma and kidney of hyperthyroid animals was found.
Title: Influence of thyroid disorders on the kidney expression and plasma activity of aminopeptidase A.
Hypertension caused by chronic ethanol treatment as well as L-NAME administration could be associated with the reduction of aminopeptidase N and aminopeptidase A activity.
Title: Ethanol inhibitory effect on rat kidney brush border aminopeptidases.

Submit: New GeneRIF Correction

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

RH133895 (e-PCR)
- UniSTS:217178

BE111146 (e-PCR)
- UniSTS:245620

D2Wox67 (e-PCR)
- UniSTS:518272

Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables aminopeptidase activity	IDA Inferred from Direct Assay more info	PubMed
enables aminopeptidase activity	IEA Inferred from Electronic Annotation more info
enables aminopeptidase activity	ISO Inferred from Sequence Orthology more info
enables metalloaminopeptidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables metalloaminopeptidase activity	IEA Inferred from Electronic Annotation more info
enables metalloaminopeptidase activity	ISO Inferred from Sequence Orthology more info
enables metalloaminopeptidase activity	ISS Inferred from Sequence or Structural Similarity more info
enables metallopeptidase activity	IEA Inferred from Electronic Annotation more info
enables peptidase activity	ISO Inferred from Sequence Orthology more info
enables peptide binding	IBA Inferred from Biological aspect of Ancestor more info
enables peptide binding	IDA Inferred from Direct Assay more info	PubMed
enables zinc ion binding	IBA Inferred from Biological aspect of Ancestor more info
enables zinc ion binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in angiogenesis	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within angiogenesis	ISO Inferred from Sequence Orthology more info
involved_in cell migration	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within cell migration	ISO Inferred from Sequence Orthology more info
involved_in cell migration	ISS Inferred from Sequence or Structural Similarity more info
involved_in cell population proliferation	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within cell population proliferation	ISO Inferred from Sequence Orthology more info
involved_in cell population proliferation	ISS Inferred from Sequence or Structural Similarity more info
involved_in glomerulus development	IEA Inferred from Electronic Annotation more info
involved_in glomerulus development	ISO Inferred from Sequence Orthology more info
involved_in peptide catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in peptide catabolic process	IDA Inferred from Direct Assay more info	PubMed
involved_in protein processing	IDA Inferred from Direct Assay more info	PubMed
involved_in proteolysis	IBA Inferred from Biological aspect of Ancestor more info
involved_in proteolysis	IEA Inferred from Electronic Annotation more info
involved_in regulation of blood pressure	IBA Inferred from Biological aspect of Ancestor more info
involved_in regulation of systemic arterial blood pressure by renin-angiotensin	IEA Inferred from Electronic Annotation more info
involved_in regulation of systemic arterial blood pressure by renin-angiotensin	ISO Inferred from Sequence Orthology more info
involved_in regulation of systemic arterial blood pressure by renin-angiotensin	ISS Inferred from Sequence or Structural Similarity more info

Component	Evidence Code	Pubs
located_in apical part of cell	ISO Inferred from Sequence Orthology more info
located_in apical plasma membrane	IEA Inferred from Electronic Annotation more info
located_in apical plasma membrane	ISO Inferred from Sequence Orthology more info
located_in brush border	IEA Inferred from Electronic Annotation more info
located_in brush border	ISO Inferred from Sequence Orthology more info
located_in brush border membrane	IDA Inferred from Direct Assay more info	PubMed
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasmic vesicle	IEA Inferred from Electronic Annotation more info
located_in cytoplasmic vesicle	ISO Inferred from Sequence Orthology more info
located_in external side of plasma membrane	IEA Inferred from Electronic Annotation more info
located_in external side of plasma membrane	ISO Inferred from Sequence Orthology more info
is_active_in extracellular space	IBA Inferred from Biological aspect of Ancestor more info
is_active_in plasma membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in plasma membrane	IEA Inferred from Electronic Annotation more info
located_in plasma membrane	ISO Inferred from Sequence Orthology more info
located_in plasma membrane	ISS Inferred from Sequence or Structural Similarity more info

General protein information

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Preferred Names: glutamyl aminopeptidase

Names: AP-A; EAP; aminopeptidase A

NP_071587.2

EC 3.4.11.7

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_022251.2 → NP_071587.2 glutamyl aminopeptidase

Status: VALIDATED

Source sequence(s)

AF146044, AF214568, BC066663, CB747518, CK481363

UniProtKB/Swiss-Prot

P50123, Q64200, Q9JLQ7, Q9JLQ9, Q9QV24

UniProtKB/TrEMBL

A0A0G2JTI8, A6HVN5

Related

ENSRNOP00000068728.2, ENSRNOT00000087062.3

Conserved Domains (3) summary

cd09601
Location:92 → 537

M1_APN_2; Peptidase M1 Aminopeptidase N family incudes tricorn interacting factor F3, Endoplasmic reticulum aminopeptidase 1 (ERAP1), Aminopeptidase Q (APQ)

pfam01433
Location:84 → 474

Peptidase_M1; Peptidase family M1

pfam11838
Location:608 → 922

ERAP1_C; ERAP1-like C-terminal domain