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P91885

- AMPN_MANSE

UniProt

P91885 - AMPN_MANSE

Protein

Aminopeptidase N

Gene

APN2

Organism
Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    Functioni

    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 bindingi340 – 3401Zinc; catalyticPROSITE-ProRule annotation
    Active sitei341 – 3411Proton acceptorPROSITE-ProRule annotation
    Metal bindingi344 – 3441Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi363 – 3631Zinc; catalyticPROSITE-ProRule annotation
    Sitei425 – 4251Transition state stabilizerBy similarity

    GO - Molecular functioni

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

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM01.030.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aminopeptidase N (EC:3.4.11.2)
    Short name:
    AP-N
    Alternative name(s):
    Apn2
    Microsomal aminopeptidase
    Gene namesi
    Name:APN2
    OrganismiManduca sexta (Tobacco hawkmoth) (Tobacco hornworm)
    Taxonomic identifieri7130 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaBombycoideaSphingidaeSphinginaeSphinginiManduca

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei? – 942Removed in mature formSequence AnalysisPRO_0000026742
    Signal peptidei1 – 1515Sequence AnalysisAdd
    BLAST
    Chaini16 – ?Aminopeptidase NPRO_0000026741

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi62 – 621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi121 – 1211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi544 – 5441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi601 – 6011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi678 – 6781N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi711 ↔ 718By similarity
    Disulfide bondi747 ↔ 783By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Interactioni

    Subunit structurei

    Binds to CRY1AB5.

    Structurei

    3D structure databases

    ProteinModelPortaliP91885.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni304 – 3085Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the peptidase M1 family.Curated

    Keywords - Domaini

    Signal

    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.

    P91885-1 [UniParc]FASTAAdd to Basket

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    MYSLIFLALI GAAFGVPLST NEDSTRNQNL AALYVLPQTS YPTFYDVRLF    50
    IDPGYTEAFH GNVSIRIIPN INIDQITIHA MAMRIDSIRV VSDVNPNEDL 100
    FSDFTLATDD THLLTIRLTR NITALQPHVI HIDYVAQYAD DMFGVYVSTY 150
    EENGRTVNLV TSQLQPTFAR RAFPCYDEPA LKAVFRTTIY APAAYATVRS 200
    NTPERRDSLK PNEPGYVKHE FEDTLVMSTY LIAYLVSNFN YIENSQNPIY 250
    PIPFRVYSRP GTQNTAEFAL EFGQQNMIAL EEYTEFPYAF PKIDKAAVPD 300
    FAAGAMENWG LVIYREVALL VREGVTTTSV KQNIGRIICH ENTHMWFGNE 350
    VGPMSWTYTW LNEGFANFFE NYATDFVRPQ WRMMDQFVIA MQNVFQSDAV 400
    LSVNPMTHPV YTPSQIIGTF NAVAYQKSGS VIRMLQHFMT PEIFRRGLVI 450
    YIKANSRAAA APSDLYVALQ QALDESSHRI PKPISTIMTE WSTQGGFPVL 500
    TVRRTAPNAD SVFVAQERYL TDRSLTSTDR WHVPVNWVIS SNVNFSDTSP 550
    QAWILPTFPA TAVDVPGLSN ADWYIFNKQQ TGYYRVNYDV ENWVALARVL 600
    NNSHEIIHVL NRAQIVDDAF NLARNGRLHY KNAFEISRYL EMEKDYIPWA 650
    AANPAFNYLD IVLSGANSYN LYRYYLLNLT APMFEDLGFD VKSGEEFVTP 700
    YHRNIILDIN CRFGNQRCIS RAQEILQAFK NNPNQRPNPD IQTLVYCSSL 750
    RAGNVENFNF LWNMYLGTSD SSEQSILLSA LGCTSNAERR NFYLNQIIDD 800
    NSAVREQDRH SIAVSVINSS PEGMNVALDF VVENFHRIQP RVQALTGTTN 850
    ILNTFARRLT TSAHNEKIDE LVRRHESIFS AGERASIAAI RENIAASIAW 900
    SNSNAGIVEN WLKENYGPPS GAKSLTAGLL VLISLFVAIF NH 942
    Length:942
    Mass (Da):106,780
    Last modified:May 30, 2000 - v2
    Checksum:iEFD4D906600E17B9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X97877 mRNA. Translation: CAA66466.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X97877 mRNA. Translation: CAA66466.2 .

    3D structure databases

    ProteinModelPortali P91885.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M01.030.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Cloning and characterization of Manduca sexta and Plutella xylostella midgut aminopeptidase N related to Bacillus thuringiensis toxin-binding proteins."
      Denolf P.H., Hendrickx K., van Damme J., Jansens S., Peferoen M., Degheele D., van Rie J.
      Eur. J. Biochem. 248:748-761(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 68-72; 187-199; 460-475; 602-612; 693-703; 875-884 AND 893-908, CHARACTERIZATION.
      Tissue: Midgut.
    2. Denolf P.H.
      Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.

    Entry informationi

    Entry nameiAMPN_MANSE
    AccessioniPrimary (citable) accession number: P91885
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 87 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    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