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P15541

- AMPN_RABIT

UniProt

P15541 - AMPN_RABIT

Protein

Aminopeptidase N

Gene

ANPEP

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (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 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 bindingi384 – 3841Zinc; catalyticPROSITE-ProRule annotation
    Active sitei385 – 3851Proton acceptorPROSITE-ProRule annotation
    Metal bindingi388 – 3881Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi407 – 4071Zinc; catalyticPROSITE-ProRule annotation
    Sitei473 – 4731Transition 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

    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:
    rbAPN
    Alternative name(s):
    Alanyl aminopeptidase
    Aminopeptidase M
    Short name:
    AP-M
    Microsomal aminopeptidase
    CD_antigen: CD13
    Gene namesi
    Name:ANPEP
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 966965Aminopeptidase NPRO_0000095084Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi40 – 401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi125 – 1251N-linked (GlcNAc...)Sequence Analysis
    Modified residuei173 – 1731SulfotyrosineSequence Analysis
    Glycosylationi259 – 2591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi315 – 3151N-linked (GlcNAc...)Sequence Analysis
    Modified residuei415 – 4151SulfotyrosineSequence Analysis
    Modified residuei420 – 4201SulfotyrosineSequence Analysis
    Glycosylationi552 – 5521N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi570 – 5701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi624 – 6241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi734 – 7341N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi760 ↔ 767By similarity
    Disulfide bondi797 ↔ 833By similarity
    Glycosylationi817 – 8171N-linked (GlcNAc...)Sequence Analysis
    Modified residuei852 – 8521PhosphotyrosineBy similarity
    Modified residuei912 – 9121SulfotyrosineSequence Analysis

    Post-translational modificationi

    Sulfated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi9986.ENSOCUP00000015166.

    Structurei

    3D structure databases

    ProteinModelPortaliP15541.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 87CytoplasmicBy similarity
    Topological domaini33 – 966934ExtracellularBy similarityAdd
    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 – 6533Cytosolic Ser/Thr-rich junctionAdd
    BLAST
    Regioni66 – 966901MetalloproteaseAdd
    BLAST
    Regioni348 – 3525Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the peptidase M1 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0308.
    HOGENOMiHOG000106482.
    HOVERGENiHBG006616.

    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.

    P15541-1 [UniParc]FASTAAdd to Basket

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    MAKGFYISKS LGILGILLGV AALCTIVALS VVYRQEKNKN TSQSPSMAPL    50
    NPTATSSPAT TLDQNLPWNR YRLPKTLIPD SYNVVLRPYL SPNSQGLYIF 100
    TGSSTVRFTC QEATNVIIIH SKKLNYTITQ GHRVVLRGVR GSQPPAIAST 150
    ELVELTEYLV VHLQGQLVAG SQYEMDTQFQ GELADDLAGF YRSEYMEGNV 200
    RKVVATTQMQ AADARKSFPC FDEPAMKATF NITPIHPRDY TALSNMLPRS 250
    STALPEDPNW TVTEFHTTPK MSTYLLAYIV SEFTNIEAQS PNNVQIRIWA 300
    RPSAISEGHG QYALNVTGPI LNFFANHYNT PYPLEKSDQI GLPDFNAGAM 350
    ENWGLVTYRE SALLFDPLVS SISNKERVVT VVAHELAHQW FGNLVTVDWW 400
    NDLWLNEGFA SYVEYLGADY AEPTWNLKDL IVLNELHSVM AVDALASSHP 450
    LSSPADEVNT PAQISELFDS ITYSKGASVL RMLSSFLTED LFKEGLASYL 500
    HTFAYQNTIY LDLWEHLQQA VNSQSAIQLP ASVRDIMDRW ILQMGFPVVT 550
    VNTTNGIISQ HHFLLDPTSN VTRPSDFNYL WIVPVSSMRN GVLEQEFWLE 600
    GVEQTQNSLF RVEGDNNWIL ANLNVTGYYQ VNYDEGNWKK LQTQLQTNPS 650
    VIPVINRAQI IHDAFNLASA QKVPVTLALD NTLFLIRETE YMPWQAALSS 700
    LNYFKLMFDR SEVYGPMKNY LSKQVRPLFE HFKNITNDWT RRPDTLMDQY 750
    NEINAISTAC SNGIQECETL VSDLFKQWMD DPSNNPIHPN LRTTVYCNAI 800
    ALGGEREWDF AWEQFRNATL VNEADKLRSA LACSNEVWIL NRYLSYTLNP 850
    DYIRRQDATS TINSIASNVI GQTLVWDFVQ SNWKKLFEDF GGGSFSFANL 900
    IRAVTRRFST EYELQQLEQF RLNNLDTGFG SGTRALEQAL EQTRANIKWV 950
    QENKEAVLAW FTANSA 966
    Length:966
    Mass (Da):109,318
    Last modified:January 23, 2007 - v4
    Checksum:iED12832072B0DB52
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 101S → A AA sequence (PubMed:6120002)Curated
    Sequence conflicti16 – 161I → F AA sequence (PubMed:6120002)Curated
    Sequence conflicti210 – 2101Q → QMQ(PubMed:2574692)Curated
    Sequence conflicti226 – 2261M → S in CAA35873. (PubMed:2574692)Curated
    Sequence conflicti234 – 2341P → L in CAA35873. (PubMed:2574692)Curated
    Sequence conflicti593 – 5942LE → QQ in CAA35873. (PubMed:2574692)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S68687 mRNA. Translation: AAB29534.1.
    X51508 mRNA. Translation: CAA35873.1.
    PIRiS07099.
    RefSeqiNP_001075795.1. NM_001082326.1.
    UniGeneiOcu.2069.

    Genome annotation databases

    GeneIDi100009167.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S68687 mRNA. Translation: AAB29534.1 .
    X51508 mRNA. Translation: CAA35873.1 .
    PIRi S07099.
    RefSeqi NP_001075795.1. NM_001082326.1.
    UniGenei Ocu.2069.

    3D structure databases

    ProteinModelPortali P15541.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9986.ENSOCUP00000015166.

    Protein family/group databases

    MEROPSi M01.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100009167.

    Organism-specific databases

    CTDi 290.

    Phylogenomic databases

    eggNOGi COG0308.
    HOGENOMi HOG000106482.
    HOVERGENi HBG006616.

    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. "Complete sequence of rabbit kidney aminopeptidase N and mRNA localization in rabbit kidney by in situ hybridization."
      Yang X.F., Milhiet P.E., Gaudoux F., Crine P., Boileau G.
      Biochem. Cell Biol. 71:278-287(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Kidney.
    2. "The amino acid sequence of the hydrophobic anchor of rabbit intestinal brush border aminopeptidase N."
      Feracci H., Maroux S., Bonicel J., Desnuelle P.
      Biochim. Biophys. Acta 684:133-136(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 6-19.
    3. "Onset of transcription of the aminopeptidase N (leukemia antigen CD 13) gene at the crypt/villus transition zone during rabbit enterocyte differentiation."
      Noren O., Dabelsteen E., Hoeyer P.E., Olsen J., Sjoestroem H., Hansen G.H.
      FEBS Lett. 259:107-112(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 178-966.

    Entry informationi

    Entry nameiAMPN_RABIT
    AccessioniPrimary (citable) accession number: P15541
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 120 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. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3