Anpep alanyl aminopeptidase, membrane [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Anpepprovided by RGD
Official Full Name: alanyl aminopeptidase, membraneprovided by RGD
Primary source: RGD:2991
See related: Ensembl:ENSRNOG00000014610 AllianceGenome:RGD:2991
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: Apm; Apn; KZP; AP-M; AP-N; Lap1; rAPN
Summary: Enables aminopeptidase activity and peptide binding activity. Involved in negative regulation of renal sodium excretion; peptide catabolic process; and proteolysis. Located in brush border membrane. Orthologous to human ANPEP (alanyl aminopeptidase, membrane). [provided by Alliance of Genome Resources, Apr 2022]
Expression: Biased expression in Kidney (RPKM 747.7), Lung (RPKM 169.0) and 2 other tissues See more
Orthologs: human mouse all
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Genomic context

Location:: 1q31

Exon count:: 23

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	1	NC_086019.1 (143176645..143219447, complement)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	1	NC_051336.1 (133767332..133810137, complement)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	1	NC_005100.4 (141561364..141604249, complement)

Chromosome 1 - NC_086019.1 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?

The effect of APN, hs-CRP and APN/hs-CRP in periodontitis with DAA.
Title: The effect of APN, hs-CRP and APN/hs-CRP in periodontitis with DAA.
In standard light/dark conditions, the results demonstrated an opposite daily rhythm in hypothalamus and pituitary. While the highest levels of AlaAP or enkephalinase activities were measured in hypothalamus during the dark period, they were the highest in the pituitary during the light one.
Title: Light-dark influence on enkephalinase activity in hypothalamus and pituitary.
Data indicate that fluorogenic substrates can be successfully used to identify aminopeptidase N and to measure their activity in cell lysates.
Title: Activity profiling of aminopeptidases in cell lysates using a fluorogenic substrate library.
the LAP1 gene (TOR1AIP1) undergoes alternative splicing to originate three LAP1 isoforms (LAP1A, B and C).
Title: Identification of a novel human LAP1 isoform that is regulated by protein phosphorylation.
the anti-oxidant potential of APN in oxidative stress-associated cardiovascular diseases, such as hypertension-induced HF-preserved EF.
Title: Adiponectin modulates oxidative stress-induced autophagy in cardiomyocytes.
This study demonistrated that aminopeptidase N were up-regulated ipsilaterally from 6 h to 7 days post ischemia
Title: Dipeptidyl peptidase IV, aminopeptidase N and DPIV/APN-like proteases in cerebral ischemia.
APN and DPPIV activity levels are related to the development of arthritis, being protective or inducer of the susceptibility
Title: Neutral aminopeptidase and dipeptidyl peptidase IV in the development of collagen II-induced arthritis.
Results suggest that the upregulation of serotonergic activity may be related to a lowered brain dipeptidyl peptidase III, alanyl- and arginyl aminopeptidase activity which may influence the cleavage of their substrates.
Title: Central aminopeptidase and serotonin system activities: possible relationship.
hypothalamic CD13 plays a role in the regulation of energy metabolism not by means of puromycin-insensitive membrane-bound neutral aminopeptidase enzyme activity.
Title: APM/CD13 and FOS in the hypothalamus of monosodium glutamate obese and food deprived rats.
APM and DPPIV-DI are respectively related to the downregulation of somatostatin in food-deprived rats, and to the recovery of energy balance in monosodium glutamate obese rats during food deprivation
Title: Neutral aminopeptidase and dipeptidyl peptidase IV activities in plasma of monosodium glutamate obese and food-deprived rats.

Submit: New GeneRIF Correction See all GeneRIFs (15)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

D1Rat350 (e-PCR), detects polymorphism
- UniSTS:227146

RH94699 (e-PCR)
- UniSTS:119946

RH130139 (e-PCR)
- UniSTS:213426

Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables aminopeptidase activity	IDA Inferred from Direct Assay more info	PubMed
enables metalloaminopeptidase activity	IBA Inferred from Biological aspect of Ancestor 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
involved_in cell differentiation	IEA Inferred from Electronic Annotation more info
involved_in metanephric proximal tubule development	IEP Inferred from Expression Pattern more info	PubMed
involved_in peptide catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in peptide catabolic process	IMP Inferred from Mutant Phenotype 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

Component	Evidence Code	Pubs
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 endoplasmic reticulum-Golgi intermediate compartment	IEA Inferred from Electronic Annotation more info
located_in endoplasmic reticulum-Golgi intermediate compartment	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
located_in extracellular exosome	IEA Inferred from Electronic Annotation more info
located_in extracellular exosome	ISO Inferred from Sequence Orthology more info
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
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: aminopeptidase N

Names: alanyl (membrane) aminopeptidase; aminopeptidase M; cluster of differentiation antigen 13 (CD13); kidney Zn peptidase; kidney aminopeptidase M; leucine arylaminopeptidase 1; membrane alanine aminopeptidase; microsomal aminopeptidase

NP_112274.1

EC 3.4.11.2

XP_006229469.1

EC 3.4.11.2

XP_006229470.1

EC 3.4.11.2

XP_006229471.1

EC 3.4.11.2

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_031012.1 → NP_112274.1 aminopeptidase N precursor

See identical proteins and their annotated locations for NP_112274.1

Status: PROVISIONAL

Source sequence(s)

M25073

UniProtKB/Swiss-Prot

P15684, Q9JHP4

UniProtKB/TrEMBL

A0A0G2JVE6

Related

ENSRNOP00000020002.5, ENSRNOT00000020002.6

Conserved Domains (3) summary

cd09601
Location:84 → 550

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

pfam01433
Location:75 → 479

Peptidase_M1; Peptidase family M1

pfam11838
Location:619 → 942

ERAP1_C; ERAP1-like C-terminal domain

RefSeqs of Annotated Genomes: GCF_036323735.1-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCr8

Genomic

NC_086019.1 Reference GRCr8

Range

143176645..143219447 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_006229409.3 → XP_006229471.1 aminopeptidase N isoform X1

See identical proteins and their annotated locations for XP_006229471.1

UniProtKB/TrEMBL

A0A0G2JVE6, A6JC72, G3V7W7

Conserved Domains (3) summary

cd09601
Location:84 → 550

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

pfam01433
Location:75 → 479

Peptidase_M1; Peptidase family M1

pfam11838
Location:619 → 942

ERAP1_C; ERAP1-like C-terminal domain
XM_006229407.5 → XP_006229469.1 aminopeptidase N isoform X1

See identical proteins and their annotated locations for XP_006229469.1

UniProtKB/TrEMBL

A0A0G2JVE6, A6JC72, G3V7W7

Conserved Domains (3) summary

cd09601
Location:84 → 550

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

pfam01433
Location:75 → 479

Peptidase_M1; Peptidase family M1

pfam11838
Location:619 → 942

ERAP1_C; ERAP1-like C-terminal domain
XM_006229408.5 → XP_006229470.1 aminopeptidase N isoform X1

See identical proteins and their annotated locations for XP_006229470.1

UniProtKB/TrEMBL

A0A0G2JVE6, A6JC72, G3V7W7

Conserved Domains (3) summary

cd09601
Location:84 → 550

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

pfam01433
Location:75 → 479

Peptidase_M1; Peptidase family M1

pfam11838
Location:619 → 942

ERAP1_C; ERAP1-like C-terminal domain