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P15684

- AMPN_RAT

UniProt

P15684 - AMPN_RAT

Protein

Aminopeptidase N

Gene

Anpep

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (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 and involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis By similarity.By similarity

    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: RGD
    2. metallopeptidase activity Source: UniProtKB-KW
    3. peptide binding Source: RGD
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. cell differentiation Source: UniProtKB-KW
    3. cellular aromatic compound metabolic process Source: RGD
    4. negative regulation of renal sodium excretion Source: RGD
    5. proteolysis Source: RGD

    Keywords - Molecular functioni

    Aminopeptidase, Developmental protein, Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Angiogenesis, Differentiation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-9982.
    SABIO-RKP15684.

    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:
    rAPN
    Alternative name(s):
    Alanyl aminopeptidase
    Aminopeptidase M
    Short name:
    AP-M
    Kidney Zn peptidase
    Short name:
    KZP
    Microsomal aminopeptidase
    CD_antigen: CD13
    Gene namesi
    Name:Anpep
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi2991. Anpep.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. vesicle lumen Source: RGD
    3. vesicle membrane Source: RGD

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 965964Aminopeptidase NPRO_0000095085Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi114 – 1141N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi128 – 1281N-linked (GlcNAc...)Sequence Analysis
    Modified residuei176 – 1761SulfotyrosineSequence Analysis
    Glycosylationi234 – 2341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi242 – 2421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi264 – 2641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi555 – 5551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi606 – 6061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi624 – 6241N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi760 ↔ 767By similarity
    Glycosylationi780 – 7801N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi797 ↔ 833By similarity
    Modified residuei852 – 8521PhosphotyrosineBy similarity

    Post-translational modificationi

    Sulfated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation

    Proteomic databases

    PaxDbiP15684.
    PRIDEiP15684.

    Expressioni

    Tissue specificityi

    Widely distributed throughout the CNS. Particularly abundant in kidney and intestinal microvilli, also detected in lung and liver. Weakly expressed in heart and aorta.1 Publication

    Gene expression databases

    GenevestigatoriP15684.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi249541. 2 interactions.
    IntActiP15684. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP15684.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 87Cytoplasmic
    Topological domaini33 – 965933ExtracellularAdd
    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 – 965897MetalloproteaseAdd
    BLAST
    Regioni351 – 3555Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the peptidase M1 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0308.
    HOGENOMiHOG000106482.
    HOVERGENiHBG006616.
    InParanoidiP15684.
    KOiK11140.
    PhylomeDBiP15684.

    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.

    P15684-1 [UniParc]FASTAAdd to Basket

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    MAKGFYISKT LGILGILLGV AAVCTIIALS VVYAQEKNRN AENSAIAPTL    50
    PGSTSATTST TNPAIDESKP WNQYRLPKTL IPDSYQVTLR PYLTPNEQGL 100
    YIFKGSSTVR FTCNETTNVI IIHSKKLNYT NKGNHRVALR ALGDTPAPNI 150
    DTTELVERTE YLVVHLQGSL VKGHQYEMDS EFQGELADDL AGFYRSEYME 200
    GGNKKVVATT QMQAADARKS FPCFDEPAMK ASFNITLIHP NNLTALSNML 250
    PKDSRTLQED PSWNVTEFHP TPKMSTYLLA YIVSEFKYVE AVSPNRVQIR 300
    IWARPSAIDE GHGDYALQVT GPILNFFAQH YNTAYPLEKS DQIALPDFNA 350
    GAMENWGLVT YRESALVFDP QSSSISNKER VVTVIAHELA HQWFGNLVTV 400
    DWWNDLWLNE GFASYVEFLG ADYAEPTWNL KDLIVLNDVY RVMAVDALAS 450
    SHPLSSPANE VNTPAQISEL FDSITYSKGA SVLRMLSSFL TEDLFKKGLS 500
    SYLHTFQYSN TIYLDLWEHL QQAVDSQTAI KLPASVSTIM DRWILQMGFP 550
    VITVNTSTGE IYQEHFLLDP TSKPTRPSDF NYLWIVPIPY LKNGKEDHYW 600
    LETEKNQSAE FQTSSNEWLL LNINVTGYYQ VNYDENNWRK IQNQLQTDLS 650
    VIPVINRAQI IHDSFNLASA GKLSITLPLS NTLFLASETE YMPWEAALSS 700
    LNYFKLMFDR SEVYGPMKRY LKKQVTPLFA YFKIKTNNWL DRPPTLMEQY 750
    NEINAISTAC SSGLEECRDL VVGLYSQWMN NSDNNPIHPN LRSTVYCNAI 800
    AFGGEEEWNF AWEQFRKATL VNEADKLRSA LACSNEVWIL NRYLSYTLNP 850
    DYIRKQDATS TIVSIANNVV GQTLVWDFVR SNWKKLFEDY GGGSFSFANL 900
    IQGVTRRFSS EFELQQLEQF KEDNSATGFG SGTRALEQAL EKTKANIKWV 950
    KENKDVVLKW FTENS 965
    Length:965
    Mass (Da):109,449
    Last modified:January 23, 2007 - v2
    Checksum:i03A9A14AEFCCE31C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti558 – 5581T → A in CAB93958. 1 PublicationCurated
    Sequence conflicti582 – 5821Y → L in CAB93958. 1 PublicationCurated
    Sequence conflicti590 – 5989YLKNGKEDH → VSQKWKGGS in CAB93958. 1 PublicationCurated
    Sequence conflicti802 – 8043FGG → SC(PubMed:2567164)Curated
    Sequence conflicti807 – 8071E → A(PubMed:2567164)Curated
    Sequence conflicti813 – 8186EQFRKA → ATVPER in AAA57129. (PubMed:2567164)Curated
    Sequence conflicti831 – 8333LAC → VGR in AAA57129. (PubMed:2567164)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25073 mRNA. Translation: AAA41502.1.
    M26710 mRNA. Translation: AAA57129.1.
    Y18765 mRNA. Translation: CAB93958.1.
    PIRiA32852.
    RefSeqiNP_112274.1. NM_031012.1.
    UniGeneiRn.11132.
    Rn.179371.

    Genome annotation databases

    GeneIDi81641.
    KEGGirno:81641.
    UCSCiRGD:2991. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25073 mRNA. Translation: AAA41502.1 .
    M26710 mRNA. Translation: AAA57129.1 .
    Y18765 mRNA. Translation: CAB93958.1 .
    PIRi A32852.
    RefSeqi NP_112274.1. NM_031012.1.
    UniGenei Rn.11132.
    Rn.179371.

    3D structure databases

    ProteinModelPortali P15684.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 249541. 2 interactions.
    IntActi P15684. 1 interaction.

    Chemistry

    BindingDBi P15684.
    ChEMBLi CHEMBL3259.

    Protein family/group databases

    MEROPSi M01.001.

    Proteomic databases

    PaxDbi P15684.
    PRIDEi P15684.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 81641.
    KEGGi rno:81641.
    UCSCi RGD:2991. rat.

    Organism-specific databases

    CTDi 290.
    RGDi 2991. Anpep.

    Phylogenomic databases

    eggNOGi COG0308.
    HOGENOMi HOG000106482.
    HOVERGENi HBG006616.
    InParanoidi P15684.
    KOi K11140.
    PhylomeDBi P15684.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-9982.
    SABIO-RK P15684.

    Miscellaneous databases

    NextBioi 615144.
    PROi P15684.

    Gene expression databases

    Genevestigatori P15684.

    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. "Amino acid sequence deduced from a rat kidney cDNA suggests it encodes the Zn-peptidase aminopeptidase N."
      Watt V.M., Yip C.C.
      J. Biol. Chem. 264:5480-5487(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Kidney.
    2. "Molecular cloning and amino acid sequence of rat kidney aminopeptidase M: a member of a super family of zinc-metallohydrolases."
      Malfroy B., Kado-Fong H., Gros C., Giros B., Schwartz J.C., Hellmiss R.
      Biochem. Biophys. Res. Commun. 161:236-241(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Kidney.
    3. Gal-Gaber O.
      Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 198-754.
    4. "p146 type II alveolar epithelial cell antigen is identical to aminopeptidase N."
      Funkhouser J.D., Tangada S.D., Jones M., O S.J., Peterson R.D.
      Am. J. Physiol. 260:L274-L279(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-19; 68-84; 206-215; 286-299 AND 364-371.
    5. "First discrete autoradiographic distribution of aminopeptidase N in various structures of rat brain and spinal cord using the selective iodinated inhibitor 125IRB 129."
      Noble F., Banisadr G., Jardinaud F., Popovici T., Lai-Kuen R., Chen H., Bischoff L., Parsadaniantz S.M., Fournie-Zaluski M.-C., Roques B.P.
      Neuroscience 105:479-488(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiAMPN_RAT
    AccessioniPrimary (citable) accession number: P15684
    Secondary accession number(s): Q9JHP4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 137 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, Direct protein sequencing, 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