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Q9EQH2

- ERAP1_MOUSE

UniProt

Q9EQH2 - ERAP1_MOUSE

Protein

Endoplasmic reticulum aminopeptidase 1

Gene

Erap1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      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 – 3431PROSITE-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. zinc ion binding Source: InterPro

    GO - Biological processi

    1. immune system process Source: UniProtKB-KW
    2. membrane protein ectodomain proteolysis Source: UniProtKB
    3. positive regulation of angiogenesis Source: MGI
    4. response to bacterium Source: Ensembl

    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
    VEGF-induced aminopeptidase
    Gene namesi
    Name:Erap1
    Synonyms:Appils, Arts1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:1933403. Erap1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. extracellular region Source: UniProtKB
    4. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 930930Endoplasmic reticulum aminopeptidase 1PRO_0000026752Add
    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

    MaxQBiQ9EQH2.
    PaxDbiQ9EQH2.
    PRIDEiQ9EQH2.

    PTM databases

    PhosphoSiteiQ9EQH2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9EQH2.
    BgeeiQ9EQH2.
    CleanExiMM_ERAP1.
    GenevestigatoriQ9EQH2.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    IntActiQ9EQH2. 1 interaction.
    MINTiMINT-1863916.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9EQH2.
    SMRiQ9EQH2. Positions 36-928.
    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.
    GeneTreeiENSGT00740000115181.
    HOGENOMiHOG000106482.
    HOVERGENiHBG108296.
    InParanoidiQ6GTP5.
    KOiK09604.
    OMAiLIHANLT.
    OrthoDBiEOG754HNR.
    TreeFamiTF300395.

    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]

    Sequencei

    Sequence statusi: Complete.

    Q9EQH2-1 [UniParc]FASTAAdd to Basket

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    MPSLLPLVLT FLSVSSPSWC QNSDIESLKA SNGDSFPWNN MRLPEYMTPI    50
    HYDLMIHANL STLTFWGKTE VEIIASRPTS TIIMHSHHLQ ISKATLRRGA 100
    GEMLSEEPLK VLEYPAHEQV ALLAAQPLLA GSLYTVIIDY AANLSESFHG 150
    FYKSTYRTQE GEMRILAATQ FEPTAARMAF PCFDEPALKA SFSIKIKRDP 200
    RHLAISNMPL VKSVNVAEGL IEDHFDITVK MSTYLVAFII SDFKSVSKMT 250
    KSGVKVSVYA VPDKINQADY ALDAAVTLLE FYEDYFNIPY PLPKQDLAAI 300
    PDFQSGAMEN WGLTTYRESS LLYDKEKSSA SSKLGITMIV SHELAHQWFG 350
    NLVTMEWWND LWLNEGFAKF MEFVSVTVTH PELKVEDYFF GKCFNAMEVD 400
    ALNSSHPVST PVENPAQIRE MFDDVSYEKG ACILNMLRDY LSADTFKRGI 450
    VQYLQKYSYK NTKNEDLWNS MMHICPTDGT QTMDGFCSRS QHSSSTSHWR 500
    QEVVDVKTMM NTWTLQKGFP LITITVSGRN VHMKQEHYMK GSERFPETGY 550
    LWHVPLTFIT SKSDSVQRFL LKTKTDVLIL PEAVQWIKFN VGMNGYYIVH 600
    YADDGWASLS GLLKEAHTTI SSNDRASLIN NAFQLVSIEK LSIEKALDLT 650
    LYLKNETEIM PIFQALNELI PMYKLMEKRD MIEVETQFKD FLLKLLKDLI 700
    DKQTWTDEGS VSERMLRSQL LLLACVRNYQ PCVQRAERYF REWKSSNGNM 750
    SIPIDVTLAV FAVGAQNTEG WDFLYSKYQS SLSSTEKSQI EFSLCTSKDP 800
    EKLQWLLDQS FKGEIIKTQE FPHILTLIGR NPVGYPLAWK FLRENWNKLV 850
    QKFELGSSSI AHMVMGTTDQ FSTRARLEEV KGFFSSLKEN GSQLRCVQQT 900
    IETIEENIRW MDKNFDKIRL WLQKEKPELL 930
    Length:930
    Mass (Da):106,599
    Last modified:July 27, 2011 - v2
    Checksum:iB5F542EBB30D16EB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti540 – 5412KG → NA in AAG44260. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF227511 mRNA. Translation: AAG44260.1.
    AB047552 mRNA. Translation: BAB11982.1.
    AK030329 mRNA. Translation: BAC26904.1.
    CH466563 Genomic DNA. Translation: EDL37102.1.
    BC046610 mRNA. Translation: AAH46610.1.
    CCDSiCCDS26647.1.
    RefSeqiNP_109636.1. NM_030711.4.
    XP_006517539.1. XM_006517476.1.
    UniGeneiMm.83526.

    Genome annotation databases

    EnsembliENSMUST00000169114; ENSMUSP00000133166; ENSMUSG00000021583.
    GeneIDi80898.
    KEGGimmu:80898.
    UCSCiuc007rfi.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF227511 mRNA. Translation: AAG44260.1 .
    AB047552 mRNA. Translation: BAB11982.1 .
    AK030329 mRNA. Translation: BAC26904.1 .
    CH466563 Genomic DNA. Translation: EDL37102.1 .
    BC046610 mRNA. Translation: AAH46610.1 .
    CCDSi CCDS26647.1.
    RefSeqi NP_109636.1. NM_030711.4.
    XP_006517539.1. XM_006517476.1.
    UniGenei Mm.83526.

    3D structure databases

    ProteinModelPortali Q9EQH2.
    SMRi Q9EQH2. Positions 36-928.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9EQH2. 1 interaction.
    MINTi MINT-1863916.

    Protein family/group databases

    MEROPSi M01.018.

    PTM databases

    PhosphoSitei Q9EQH2.

    Proteomic databases

    MaxQBi Q9EQH2.
    PaxDbi Q9EQH2.
    PRIDEi Q9EQH2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000169114 ; ENSMUSP00000133166 ; ENSMUSG00000021583 .
    GeneIDi 80898.
    KEGGi mmu:80898.
    UCSCi uc007rfi.1. mouse.

    Organism-specific databases

    CTDi 51752.
    MGIi MGI:1933403. Erap1.

    Phylogenomic databases

    eggNOGi COG0308.
    GeneTreei ENSGT00740000115181.
    HOGENOMi HOG000106482.
    HOVERGENi HBG108296.
    InParanoidi Q6GTP5.
    KOi K09604.
    OMAi LIHANLT.
    OrthoDBi EOG754HNR.
    TreeFami TF300395.

    Miscellaneous databases

    NextBioi 350235.
    PROi Q9EQH2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9EQH2.
    Bgeei Q9EQH2.
    CleanExi MM_ERAP1.
    Genevestigatori Q9EQH2.

    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 cloning of murine adipocyte-derived leucine aminopeptidase and its expression in adipocyte cell line, 3T3-L1 cells."
      Hattori A., Kitatani K., Matsumoto H., Mizutani S., Tsujimoto M.
      Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "A mouse orthologue of puromycin-insensitive leucyl-specific aminopeptidase is expressed in endothelial cells and plays an important role in angiogenesis."
      Miyashita H., Yamazaki T., Akada T., Niizeki O., Ogawa M., Nishikawa S., Sato Y.
      Blood 99:3241-3249(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Colon.

    Entry informationi

    Entry nameiERAP1_MOUSE
    AccessioniPrimary (citable) accession number: Q9EQH2
    Secondary accession number(s): Q6GTP5, Q9ET63
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 5, 2002
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 115 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3