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

    Gene ID: 80897, updated on 9-Dec-2024

    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, Dec 2024]
    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

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

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