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Q9JJ22

- ERAP1_RAT

UniProt

Q9JJ22 - ERAP1_RAT

Protein

Endoplasmic reticulum aminopeptidase 1

Gene

Erap1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (05 Mar 2002)
      Previous versions | rss
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    Functioni

    Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney By similarity.By similarity

    Catalytic activityi

    Release of an N-terminal amino acid, Xaa-|-Xbb-, in which Xaa is preferably Leu, but may be other amino acids including Met, Cys and Phe.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei172 – 1721SubstrateBy similarity
    Metal bindingi342 – 3421Zinc; catalyticPROSITE-ProRule annotation
    Active sitei343 – 3431Proton acceptorPROSITE-ProRule annotation
    Metal bindingi346 – 3461Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi365 – 3651Zinc; catalyticPROSITE-ProRule annotation
    Sitei427 – 4271Transition state stabilizerBy similarity

    GO - Molecular functioni

    1. aminopeptidase activity Source: UniProtKB
    2. interleukin-6 receptor binding Source: UniProtKB
    3. metalloexopeptidase activity Source: UniProtKB
    4. tumor necrosis factor receptor binding Source: RGD
    5. zinc ion binding Source: RGD

    GO - Biological processi

    1. antigen processing and presentation Source: RGD
    2. membrane protein ectodomain proteolysis Source: UniProtKB
    3. proteolysis Source: RGD

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Adaptive immunity, Immunity

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM01.018.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoplasmic reticulum aminopeptidase 1 (EC:3.4.11.-)
    Alternative name(s):
    ARTS-1
    Adipocyte-derived leucine aminopeptidase
    Short name:
    A-LAP
    Aminopeptidase PILS
    Puromycin-insensitive leucyl-specific aminopeptidase
    Short name:
    PILS-AP
    Gene namesi
    Name:Erap1
    Synonyms:Appils, Arts1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi708542. Erap1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: RGD
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. extracellular region Source: UniProtKB
    4. integral component of membrane Source: UniProtKB-KW
    5. intracellular membrane-bounded organelle Source: RGD

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 930930Endoplasmic reticulum aminopeptidase 1PRO_0000026753Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi59 – 591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi143 – 1431N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi393 ↔ 432By similarity
    Glycosylationi403 – 4031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi655 – 6551N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi725 ↔ 732By similarity
    Glycosylationi749 – 7491N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi890 – 8901N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9JJ22.
    PRIDEiQ9JJ22.

    PTM databases

    PhosphoSiteiQ9JJ22.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    GenevestigatoriQ9JJ22.

    Interactioni

    Subunit structurei

    Monomer. May also exist as a heterodimer; with ERAP2. Interacts with RBMX By similarity.By similarity

    Protein-protein interaction databases

    MINTiMINT-4568526.
    STRINGi10116.ENSRNOP00000013625.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JJ22.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 22CytoplasmicSequence Analysis
    Topological domaini24 – 930907LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei3 – 2321Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni306 – 3105Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the peptidase M1 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0308.
    HOGENOMiHOG000106482.
    HOVERGENiHBG108296.
    InParanoidiQ9JJ22.
    KOiK09604.
    PhylomeDBiQ9JJ22.

    Family and domain databases

    InterProiIPR024571. ERAP1-like_C_dom.
    IPR001930. Peptidase_M1.
    IPR014782. Peptidase_M1_N.
    [Graphical view]
    PANTHERiPTHR11533. PTHR11533. 1 hit.
    PfamiPF11838. ERAP1_C. 1 hit.
    PF01433. Peptidase_M1. 1 hit.
    [Graphical view]
    PRINTSiPR00756. ALADIPTASE.
    PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9JJ22-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPSLLSLVLT FLAVSSPSCC QNSDTASPKA SNGASFPWNN MRLPEYITPI    50
    HYDLMIHANL STLTFWGKTE VEITVSQPTS TIIMHSHQLQ ISKATLRRGA 100
    EEMLPEEPLK LMEYSAHEQV ALLTAQPLLA GSVYTVIITY AANLSENFHG 150
    FYKSTYRTQE GERRILAATQ FEPTAARMAF PCFDEPALKA SFSIKIKRDP 200
    RHLAISNMPL VKSVTVAEGL IEDHFDITVK MSTYLVAFII SDFKSVSKMT 250
    KSGVKVSVYA VPDKINQADY ALDAAVTLLE FYEDYFSIPY PLPKQDLAAI 300
    PDFQSGAMEN WGLTTYRESA LLYDKEKSSA SSKLGITMTV SHELAHQWFG 350
    NLVTMEWWND LWLNEGFAKF MEFVSVTVTH PELKVEEYFF GKCFNAMEVD 400
    ALNSSHPVST PVENPAQIRE MFDEVSYEKG ACILNMLRDY LSADTFKRGI 450
    VQYLQKYSYK NTKNEDLWNS MMHICPTDGT QTMDGFCSRN QHSSSTSHWR 500
    QEVIDIKSMM NTWTLQKGFP LITITVRGRN VHLKQEHYMK GSECFPETGS 550
    LWHVPLTFIT SKSDSVQRFL LKTKTDVIIL PEAVEWIKFN VGMNGYYIVH 600
    YGDDGWASLN GLLKEAHTTI SSNDRASLIN NAFQLVSIGK LSIEKALDLI 650
    LYLKNETEIM PIFQGLNELI PMYKLMEKRD MVEVETQFKD FLLRLLKDLI 700
    NKQTWTDEGS VSERMLRSQL LLLACVHRYQ LCVQRAERYF REWKASNGNM 750
    SLPIDVTLAV FAVGAQNTEG WDFLYSKYQS SLSSTEKSQI EFSLCISQDP 800
    EKLQWLLDQS FKGEIIKTQE FPHILTLIGR NPVGYPLAWK FLKENWNKIV 850
    QKFELGSSSI AHMVMGTTNQ FSTRARLEEV KGFFSSLKKN GSQLRCVQQT 900
    IETIEENIRW MDKNFDKIRL WLQKERQELL 930
    Length:930
    Mass (Da):106,419
    Last modified:March 5, 2002 - v2
    Checksum:i928E7143CBD0EE7F
    GO
    Isoform 2 (identifier: Q9JJ22-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         883-884: FF → CM
         885-930: Missing.

    Show »
    Length:884
    Mass (Da):100,730
    Checksum:iCD2F195A7B72FAB0
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei883 – 8842FF → CM in isoform 2. 1 PublicationVSP_005451
    Alternative sequencei885 – 93046Missing in isoform 2. 1 PublicationVSP_005452Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF148323 mRNA. Translation: AAF73106.1.
    AF148324 mRNA. Translation: AAF73107.1.
    RefSeqiNP_110463.1. NM_030836.1. [Q9JJ22-2]
    UniGeneiRn.22516.

    Genome annotation databases

    GeneIDi80897.
    KEGGirno:80897.
    UCSCiRGD:708542. rat. [Q9JJ22-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF148323 mRNA. Translation: AAF73106.1 .
    AF148324 mRNA. Translation: AAF73107.1 .
    RefSeqi NP_110463.1. NM_030836.1. [Q9JJ22-2 ]
    UniGenei Rn.22516.

    3D structure databases

    ProteinModelPortali Q9JJ22.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-4568526.
    STRINGi 10116.ENSRNOP00000013625.

    Protein family/group databases

    MEROPSi M01.018.

    PTM databases

    PhosphoSitei Q9JJ22.

    Proteomic databases

    PaxDbi Q9JJ22.
    PRIDEi Q9JJ22.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 80897.
    KEGGi rno:80897.
    UCSCi RGD:708542. rat. [Q9JJ22-1 ]

    Organism-specific databases

    CTDi 51752.
    RGDi 708542. Erap1.

    Phylogenomic databases

    eggNOGi COG0308.
    HOGENOMi HOG000106482.
    HOVERGENi HBG108296.
    InParanoidi Q9JJ22.
    KOi K09604.
    PhylomeDBi Q9JJ22.

    Miscellaneous databases

    NextBioi 614912.
    PROi Q9JJ22.

    Gene expression databases

    Genevestigatori Q9JJ22.

    Family and domain databases

    InterProi IPR024571. ERAP1-like_C_dom.
    IPR001930. Peptidase_M1.
    IPR014782. Peptidase_M1_N.
    [Graphical view ]
    PANTHERi PTHR11533. PTHR11533. 1 hit.
    Pfami PF11838. ERAP1_C. 1 hit.
    PF01433. Peptidase_M1. 1 hit.
    [Graphical view ]
    PRINTSi PR00756. ALADIPTASE.
    PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular characterization of a puromycin-insensitive leucyl-specific aminopeptidase, PILS-AP."
      Schomburg L., Kollmus H., Friedrichsen S., Bauer K.
      Eur. J. Biochem. 267:3198-3207(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
      Strain: Sprague-Dawley.
      Tissue: Pineal gland.

    Entry informationi

    Entry nameiERAP1_RAT
    AccessioniPrimary (citable) accession number: Q9JJ22
    Secondary accession number(s): Q9JJ23
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 5, 2002
    Last sequence update: March 5, 2002
    Last modified: October 1, 2014
    This is version 107 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3