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Erap1 endoplasmic reticulum aminopeptidase 1 [ Rattus norvegicus (Norway rat) ]

Gene ID: 80897, updated on 4-Jan-2025

Summary

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Official Symbol
Erap1provided by RGD
Official Full Name
endoplasmic reticulum aminopeptidase 1provided by RGD
Primary source
RGD:708542
See related
EnsemblRapid:ENSRNOG00000009997 AllianceGenome:RGD:708542
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
Also known as
Arts1; Appils
Summary
Enables aminopeptidase activity; tumor necrosis factor receptor binding activity; and zinc ion binding activity. Involved in protein catabolic process. Located in endoplasmic reticulum lumen. Human ortholog(s) of this gene implicated in cervix carcinoma. Orthologous to human ERAP1 (endoplasmic reticulum aminopeptidase 1). [provided by Alliance of Genome Resources, Jan 2025]
Expression
Biased expression in Adrenal (RPKM 180.9), Lung (RPKM 177.2) and 9 other tissues See more
Orthologs
human mouse all
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Genomic context

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See Erap1 in Genome Data Viewer
Location:
2q11
Exon count:
21
Annotation release Status Assembly Chr Location
RS_2024_02 current GRCr8 (GCF_036323735.1) 2 NC_086020.1 (5666337..5705256)
RS_2023_06 previous assembly mRatBN7.2 (GCF_015227675.2) 2 NC_051337.1 (3931817..3970735)
106 previous assembly Rnor_6.0 (GCF_000001895.5) 2 NC_005101.4 (1410877..1449734)

Chromosome 2 - NC_086020.1Genomic Context describing neighboring genes Neighboring gene ATP synthase peripheral stalk subunit F6, pseudogene 4 Neighboring gene uncharacterized LOC102548635 Neighboring gene calpastatin Neighboring gene uncharacterized LOC134485561 Neighboring gene RNA, U6 small nuclear 1303

Genomic regions, transcripts, and products

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Go to nucleotide: Graphics FASTA GenBank

Expression

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  • 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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Related articles in PubMed

  1. Molecular characterization of a puromycin-insensitive leucyl-specific aminopeptidase, PILS-AP. Schomburg L, et al. Eur J Biochem, 2000 Jun. PMID 10824104, Free PMC Article
  2. Possible involvement of adipocyte-derived leucine aminopeptidase via angiotensin II in endometrial carcinoma. Shibata K, et al. Tumour Biol, 2005 Jan-Feb. PMID 15741767
  3. All the peptides that fit: the beginning, the middle, and the end of the MHC class I antigen-processing pathway. Shastri N, et al. Immunol Rev, 2005 Oct. PMID 16181325
  4. Molecular cloning of adipocyte-derived leucine aminopeptidase highly related to placental leucine aminopeptidase/oxytocinase. Hattori A, et al. J Biochem, 1999 May. PMID 10220586
  5. Characterization of recombinant human adipocyte-derived leucine aminopeptidase expressed in Chinese hamster ovary cells. Hattori A, et al. J Biochem, 2000 Nov. PMID 11056387

See all (19) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. stimulates the processing and presentation of an antigenic precursor in the endoplasmic reticulum
    Title: An IFN-gamma-induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I-presented peptides.
Submit: New GeneRIF Correction

Pathways from PubChem

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General gene information

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Markers

Homology

Clone Names

  • MGC112613

Gene Ontology Provided by RGD

Function Evidence Code Pubs
enables aminopeptidase activity IEA
Inferred from Electronic Annotation
more info
  
enables aminopeptidase activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables aminopeptidase activity ISO
Inferred from Sequence Orthology
more info
  
enables aminopeptidase activity ISS
Inferred from Sequence or Structural Similarity
more info
  
enables endopeptidase activity ISO
Inferred from Sequence Orthology
more info
  
enables interleukin-6 receptor binding ISO
Inferred from Sequence Orthology
more info
  
enables interleukin-6 receptor binding ISS
Inferred from Sequence or Structural Similarity
more info
  
enables metalloaminopeptidase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables metalloexopeptidase activity ISO
Inferred from Sequence Orthology
more info
  
enables metalloexopeptidase 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 tumor necrosis factor receptor binding IPI
Inferred from Physical Interaction
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
  
enables zinc ion binding IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Process Evidence Code Pubs
involved_in adaptive immune response IEA
Inferred from Electronic Annotation
more info
  
involved_in antigen processing and presentation TAS
Traceable Author Statement
more info
 PubMed 
involved_in membrane protein ectodomain proteolysis ISO
Inferred from Sequence Orthology
more info
  
involved_in membrane protein ectodomain proteolysis ISS
Inferred from Sequence or Structural Similarity
more info
  
involved_in peptide catabolic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in positive regulation of angiogenesis IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within positive regulation of angiogenesis ISO
Inferred from Sequence Orthology
more info
  
involved_in protein catabolic process IMP
Inferred from Mutant Phenotype
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
  
acts_upstream_of_or_within proteolysis ISO
Inferred from Sequence Orthology
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 cytoplasm ISO
Inferred from Sequence Orthology
more info
  
located_in endoplasmic reticulum lumen IDA
Inferred from Direct Assay
more info
 PubMed 
located_in endoplasmic reticulum membrane IEA
Inferred from Electronic Annotation
more info
  
located_in extracellular region ISO
Inferred from Sequence Orthology
more info
  
located_in extracellular region ISS
Inferred from Sequence or Structural Similarity
more info
  
is_active_in extracellular space IBA
Inferred from Biological aspect of Ancestor
more info
  
is_active_in membrane IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in membrane IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
endoplasmic reticulum aminopeptidase 1
Names
A-LAP
ARTS-1
ER-aminopeptidase 1
PILS-AP
adipocyte-derived leucine aminopeptidase
aminopeptidase PILS
leucyl-specific aminopeptidase PILS
puromycin-insensitive leucyl-specific aminopeptidase
type 1 tumor necrosis factor receptor shedding aminopeptidase regulator

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)

  1. NM_001399166.1 → NP_001386095.1  endoplasmic reticulum aminopeptidase 1 precursor

    Status: VALIDATED

    Source sequence(s)
    JAXUCZ010000002
    UniProtKB/Swiss-Prot
    Q9JJ22, Q9JJ23
    UniProtKB/TrEMBL
    Q4KMA8
    Related
    ENSRNOP00000104412.1, ENSRNOT00000133925.1
    Conserved Domains (2) summary
    cd09601
    Location:50 → 515
    M1_APN-Q_like; Peptidase M1 aminopeptidase N catalytic domain family which includes aminopeptidase N (APN), aminopeptidase Q (APQ), tricorn interacting factor F3, and endoplasmic reticulum aminopeptidase 1 (ERAP1)
    pfam11838
    Location:586 → 905
    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

  1. NC_086020.1 Reference GRCr8

    Range
    5666337..5705256
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_008760601.4 → XP_008758823.1  endoplasmic reticulum aminopeptidase 1 isoform X2

    UniProtKB/TrEMBL
    A0A0G2K2Y3, A6I4D9
    Conserved Domains (3) summary
    cd09601
    Location:50 → 544
    M1_APN_2; Peptidase M1 Aminopeptidase N family incudes tricorn interacting factor F3, Endoplasmic reticulum aminopeptidase 1 (ERAP1), Aminopeptidase Q (APQ)
    pfam01433
    Location:42 → 454
    Peptidase_M1; Peptidase family M1
    pfam11838
    Location:611 → 919
    ERAP1_C; ERAP1-like C-terminal domain

  2. XM_006231701.5 → XP_006231763.1  endoplasmic reticulum aminopeptidase 1 isoform X1

    See identical proteins and their annotated locations for XP_006231763.1

    UniProtKB/Swiss-Prot
    Q9JJ22, Q9JJ23
    UniProtKB/TrEMBL
    F7F4R3
    Related
    ENSRNOP00000013625.5, ENSRNOT00000013625.7
    Conserved Domains (3) summary
    cd09601
    Location:50 → 544
    M1_APN_2; Peptidase M1 Aminopeptidase N family incudes tricorn interacting factor F3, Endoplasmic reticulum aminopeptidase 1 (ERAP1), Aminopeptidase Q (APQ)
    pfam01433
    Location:42 → 454
    Peptidase_M1; Peptidase family M1
    pfam11838
    Location:611 → 927
    ERAP1_C; ERAP1-like C-terminal domain

  3. XM_063282613.1 → XP_063138683.1  endoplasmic reticulum aminopeptidase 1 isoform X4

    UniProtKB/TrEMBL
    A0A0G2K2Y3, A0A8I5ZYK5, A6I4D9
    Related
    ENSRNOP00000072424.1, ENSRNOT00000080222.3

  4. XM_063282612.1 → XP_063138682.1  endoplasmic reticulum aminopeptidase 1 isoform X3

    UniProtKB/Swiss-Prot
    Q9JJ22, Q9JJ23
    UniProtKB/TrEMBL
    Q4KMA8

  5. XM_006231700.3 → XP_006231762.1  endoplasmic reticulum aminopeptidase 1 isoform X1

    See identical proteins and their annotated locations for XP_006231762.1

    UniProtKB/Swiss-Prot
    Q9JJ22, Q9JJ23
    UniProtKB/TrEMBL
    F7F4R3
    Conserved Domains (3) summary
    cd09601
    Location:50 → 544
    M1_APN_2; Peptidase M1 Aminopeptidase N family incudes tricorn interacting factor F3, Endoplasmic reticulum aminopeptidase 1 (ERAP1), Aminopeptidase Q (APQ)
    pfam01433
    Location:42 → 454
    Peptidase_M1; Peptidase family M1
    pfam11838
    Location:611 → 927
    ERAP1_C; ERAP1-like C-terminal domain

  6. XM_063282614.1 → XP_063138684.1  endoplasmic reticulum aminopeptidase 1 isoform X5

Suppressed Reference Sequence(s)

The following Reference Sequences have been suppressed. Explain

  1. NM_030836.1: Suppressed sequence

    Description
    NM_030836.1: This RefSeq was removed because currently there is insufficient support for the transcript and the protein.
Nucleotide Protein Strain
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
Q9JJ22.2 GenPept UniProtKB/Swiss-Prot:Q9JJ22

Gene LinkOut

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