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P97449

- AMPN_MOUSE

UniProt

P97449 - AMPN_MOUSE

Protein

Aminopeptidase N

Gene

Anpep

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May be involved in the metabolism of regulatory peptides of diverse cell types, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. May have a role in angiogenesis By similarity. Found to cleave antigen peptides bound to major histocompatibility complex class II molecules of presenting cells.By similarity1 Publication

    Catalytic activityi

    Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi387 – 3871Zinc; catalyticPROSITE-ProRule annotation
    Active sitei388 – 3881Proton acceptorPROSITE-ProRule annotation
    Metal bindingi391 – 3911Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi410 – 4101Zinc; catalyticPROSITE-ProRule annotation
    Sitei476 – 4761Transition state stabilizerBy similarity

    GO - Molecular functioni

    1. aminopeptidase activity Source: UniProtKB-KW
    2. metallopeptidase activity Source: UniProtKB-KW
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. cell differentiation Source: UniProtKB-KW

    Keywords - Molecular functioni

    Aminopeptidase, Developmental protein, Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Angiogenesis, Differentiation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_196539. Metabolism of Angiotensinogen to Angiotensins.

    Protein family/group databases

    MEROPSiM01.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aminopeptidase N (EC:3.4.11.2)
    Short name:
    AP-N
    Short name:
    mAPN
    Alternative name(s):
    Alanyl aminopeptidase
    Aminopeptidase M
    Short name:
    AP-M
    Membrane protein p161
    Microsomal aminopeptidase
    CD_antigen: CD13
    Gene namesi
    Name:Anpep
    Synonyms:Lap-1, Lap1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:5000466. Anpep.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum-Golgi intermediate compartment Source: Ensembl
    2. external side of plasma membrane Source: MGI
    3. integral component of membrane Source: UniProtKB-KW
    4. lysosomal membrane Source: Ensembl

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 966965Aminopeptidase NPRO_0000095082Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi106 – 1061N-linked (GlcNAc...)2 Publications
    Glycosylationi114 – 1141N-linked (GlcNAc...)1 Publication
    Glycosylationi128 – 1281N-linked (GlcNAc...)1 Publication
    Modified residuei176 – 1761SulfotyrosineSequence Analysis
    Glycosylationi234 – 2341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi288 – 2881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi318 – 3181N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi332 – 3321N-linked (GlcNAc...)1 Publication
    Modified residuei418 – 4181SulfotyrosineSequence Analysis
    Modified residuei423 – 4231SulfotyrosineSequence Analysis
    Glycosylationi573 – 5731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi606 – 6061N-linked (GlcNAc...)2 Publications
    Glycosylationi624 – 6241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi666 – 6661N-linked (GlcNAc...); atypical1 Publication
    Glycosylationi734 – 7341N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi760 ↔ 767By similarity
    Glycosylationi783 – 7831N-linked (GlcNAc...); atypical2 Publications
    Glycosylationi784 – 7841N-linked (GlcNAc...)2 Publications
    Glycosylationi785 – 7851N-linked (GlcNAc...); atypical2 Publications
    Glycosylationi790 – 7901N-linked (GlcNAc...); atypical1 Publication
    Disulfide bondi797 ↔ 833By similarity
    Glycosylationi817 – 8171N-linked (GlcNAc...)2 Publications
    Modified residuei852 – 8521Phosphotyrosine1 Publication

    Post-translational modificationi

    Sulfated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation

    Proteomic databases

    MaxQBiP97449.
    PaxDbiP97449.
    PRIDEiP97449.

    PTM databases

    PhosphoSiteiP97449.

    Expressioni

    Tissue specificityi

    Highly expressed in intestinal tract and kidney, present in liver, lymph node, spleen, and brain. Found as well in monocytes, macrophages, dendritic cells, veiled cells and B-cells but not on T-cells and thymocytes.1 Publication

    Gene expression databases

    ArrayExpressiP97449.
    BgeeiP97449.
    CleanExiMM_ANPEP.
    GenevestigatoriP97449.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    IntActiP97449. 10 interactions.
    MINTiMINT-1870305.

    Structurei

    3D structure databases

    ProteinModelPortaliP97449.
    SMRiP97449. Positions 66-965.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 87Cytoplasmic
    Topological domaini33 – 966934ExtracellularAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei9 – 3224Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni33 – 6836Cytosolic Ser/Thr-rich junctionAdd
    BLAST
    Regioni69 – 966898MetalloproteaseAdd
    BLAST
    Regioni351 – 3555Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the peptidase M1 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0308.
    GeneTreeiENSGT00740000114965.
    HOGENOMiHOG000106482.
    HOVERGENiHBG006616.
    InParanoidiP97449.
    KOiK11140.
    OMAiWVLLNLN.
    OrthoDBiEOG754HNR.
    PhylomeDBiP97449.
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P97449-1 [UniParc]FASTAAdd to Basket

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    MAKGFYISKT LGILGILLGV AAVCTIIALS VVYAQEKNRN AENSATAPTL    50
    PGSTSATTAT TTPAVDESKP WNQYRLPKTL IPDSYRVILR PYLTPNNQGL 100
    YIFQGNSTVR FTCNQTTDVI IIHSKKLNYT LKGNHRVVLR TLDGTPAPNI 150
    DKTELVERTE YLVVHLQGSL VEGRQYEMDS QFQGELADDL AGFYRSEYME 200
    GDVKKVVATT QMQAADARKS FPCFDEPAMK AMFNITLIYP NNLIALSNML 250
    PKESKPYPED PSCTMTEFHS TPKMSTYLLA YIVSEFKNIS SVSANGVQIG 300
    IWARPSAIDE GQGDYALNVT GPILNFFAQH YNTSYPLPKS DQIALPDFNA 350
    GAMENWGLVT YRESSLVFDS QSSSISNKER VVTVIAHELA HQWFGNLVTV 400
    AWWNDLWLNE GFASYVEYLG ADYAEPTWNL KDLMVLNDVY RVMAVDALAS 450
    SHPLSSPADE IKTPDQIMEL FDSITYSKGA SVIRMLSSFL TEDLFKKGLS 500
    SYLHTYQYSN TVYLDLWEHL QKAVNQQTAV QPPATVRTIM DRWILQMGFP 550
    VITVNTNTGE ISQKHFLLDS KSNVTRPSEF NYIWIAPIPF LKSGQEDHYW 600
    LDVEKNQSAK FQTSSNEWIL LNINVTGYYL VNYDENNWKK LQNQLQTDLS 650
    VIPVINRAQI IHDSFNLASA KMIPITLALD NTLFLVKEAE YMPWQAALSS 700
    LNYFTLMFDR SEVYGPMKRY LKKQVTPLFF YFQNRTNNWV NRPPTLMEQY 750
    NEINAISTAC SSGLKECRDL VVELYSQWMK NPNNNTIHPN LRSTVYCNAI 800
    AFGGEEEWNF AWEQFRNATL VNEADKLRSA LACSKDVWIL NRYLSYTLNP 850
    DYIRKQDTTS TIISIASNVA GHPLVWDFVR SNWKKLFENY GGGSFSFANL 900
    IQGVTRRFSS EFELQQLEQF KADNSATGFG TGTRALEQAL EKTRANIDWV 950
    KENKDAVFKW FTENSS 966
    Length:966
    Mass (Da):109,651
    Last modified:January 23, 2007 - v4
    Checksum:iFD837F7ACE705835
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti62 – 621T → TATTTATTT in AAH17011. (PubMed:15489334)Curated
    Sequence conflicti62 – 621T → TATTTATTT in AAH40792. (PubMed:15489334)Curated
    Sequence conflicti84 – 841S → A in AAB19065. (PubMed:8805662)Curated
    Sequence conflicti106 – 1061N → S in AAH17011. (PubMed:15489334)Curated
    Sequence conflicti106 – 1061N → S in AAH40792. (PubMed:15489334)Curated
    Sequence conflicti181 – 1811Q → E in AAH17011. (PubMed:15489334)Curated
    Sequence conflicti181 – 1811Q → E in AAH40792. (PubMed:15489334)Curated
    Sequence conflicti202 – 2021D → G in AAH17011. (PubMed:15489334)Curated
    Sequence conflicti202 – 2021D → G in AAH40792. (PubMed:15489334)Curated
    Sequence conflicti532 – 5321P → L in AAH17011. (PubMed:15489334)Curated
    Sequence conflicti532 – 5321P → L in AAH40792. (PubMed:15489334)Curated
    Sequence conflicti557 – 5571N → S in AAH17011. (PubMed:15489334)Curated
    Sequence conflicti557 – 5571N → S in AAH40792. (PubMed:15489334)Curated
    Sequence conflicti557 – 5571Missing AA sequence (PubMed:8805662)Curated
    Sequence conflicti689 – 6891A → T in AAH17011. (PubMed:15489334)Curated
    Sequence conflicti689 – 6891A → T in AAH40792. (PubMed:15489334)Curated
    Sequence conflicti726 – 7261T → M in AAH17011. (PubMed:15489334)Curated
    Sequence conflicti726 – 7261T → M in AAH40792. (PubMed:15489334)Curated
    Sequence conflicti966 – 9661S → G in AAH17011. (PubMed:15489334)Curated
    Sequence conflicti966 – 9661S → G in AAH40792. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U77083 mRNA. Translation: AAB19065.1.
    BC005431 mRNA. Translation: AAH05431.1.
    BC017011 mRNA. Translation: AAH17011.1.
    BC040792 mRNA. Translation: AAH40792.1.
    CCDSiCCDS21388.1.
    RefSeqiNP_032512.2. NM_008486.2.
    XP_006540741.1. XM_006540678.1.
    UniGeneiMm.4487.

    Genome annotation databases

    EnsembliENSMUST00000049004; ENSMUSP00000035943; ENSMUSG00000039062.
    ENSMUST00000107392; ENSMUSP00000103015; ENSMUSG00000039062.
    GeneIDi16790.
    KEGGimmu:16790.
    UCSCiuc009hzd.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U77083 mRNA. Translation: AAB19065.1 .
    BC005431 mRNA. Translation: AAH05431.1 .
    BC017011 mRNA. Translation: AAH17011.1 .
    BC040792 mRNA. Translation: AAH40792.1 .
    CCDSi CCDS21388.1.
    RefSeqi NP_032512.2. NM_008486.2.
    XP_006540741.1. XM_006540678.1.
    UniGenei Mm.4487.

    3D structure databases

    ProteinModelPortali P97449.
    SMRi P97449. Positions 66-965.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P97449. 10 interactions.
    MINTi MINT-1870305.

    Chemistry

    ChEMBLi CHEMBL2189140.

    Protein family/group databases

    MEROPSi M01.001.

    PTM databases

    PhosphoSitei P97449.

    Proteomic databases

    MaxQBi P97449.
    PaxDbi P97449.
    PRIDEi P97449.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000049004 ; ENSMUSP00000035943 ; ENSMUSG00000039062 .
    ENSMUST00000107392 ; ENSMUSP00000103015 ; ENSMUSG00000039062 .
    GeneIDi 16790.
    KEGGi mmu:16790.
    UCSCi uc009hzd.1. mouse.

    Organism-specific databases

    CTDi 290.
    MGIi MGI:5000466. Anpep.

    Phylogenomic databases

    eggNOGi COG0308.
    GeneTreei ENSGT00740000114965.
    HOGENOMi HOG000106482.
    HOVERGENi HBG006616.
    InParanoidi P97449.
    KOi K11140.
    OMAi WVLLNLN.
    OrthoDBi EOG754HNR.
    PhylomeDBi P97449.
    TreeFami TF300395.

    Enzyme and pathway databases

    Reactomei REACT_196539. Metabolism of Angiotensinogen to Angiotensins.

    Miscellaneous databases

    ChiTaRSi ANPEP. mouse.
    NextBioi 290654.
    PROi P97449.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P97449.
    Bgeei P97449.
    CleanExi MM_ANPEP.
    Genevestigatori P97449.

    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. "p161, a murine membrane protein expressed on mast cells and some macrophages, is mouse CD13/aminopeptidase N."
      Chen H., Kinzer C.A., Paul W.E.
      J. Immunol. 157:2593-2600(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 538-564; 886-908; 922-942 AND 961-965, TISSUE SPECIFICITY.
    2. "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: Czech II and FVB/N.
      Tissue: Mammary tumor.
    3. "A mouse aminopeptidase N is a marker for antigen-presenting cells and appears to be co-expressed with major histocompatibility complex class II molecules."
      Hansen A.S., Noren O., Sjostrom H., Werdelin O.
      Eur. J. Immunol. 23:2358-2364(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYMATIC CLEAVAGE OF ANTIGEN PEPTIDES BOUND TO CLASS II MHC.
    4. "T cell responses affected by aminopeptidase N (CD13)-mediated trimming of major histocompatibility complex class II-bound peptides."
      Larsen S.L., Pedersen L.O., Buus S., Stryhn A.
      J. Exp. Med. 184:183-189(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYMATIC CLEAVAGE OF ANTIGEN PEPTIDES BOUND TO CLASS II MHC.
    5. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
      Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
      J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-852, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    6. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
      Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
      Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-106; ASN-128; ASN-606; ASN-666; ASN-783; ASN-784; ASN-785; ASN-790 AND ASN-817.
      Tissue: Myoblast.
    7. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-106; ASN-114; ASN-332; ASN-606; ASN-783; ASN-784; ASN-785 AND ASN-817.

    Entry informationi

    Entry nameiAMPN_MOUSE
    AccessioniPrimary (citable) accession number: P97449
    Secondary accession number(s): Q91YH8, Q99K63
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 144 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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