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Q10737

- AMPN_HAECO

UniProt

Q10737 - AMPN_HAECO

Protein

Aminopeptidase N

Gene
N/A
Organism
Haemonchus contortus (Barber pole worm)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      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
    Binding sitei208 – 2081SubstrateBy similarity
    Metal bindingi379 – 3791Zinc; catalyticPROSITE-ProRule annotation
    Active sitei380 – 3801Proton acceptorPROSITE-ProRule annotation
    Metal bindingi383 – 3831Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi402 – 4021Zinc; catalyticPROSITE-ProRule annotation
    Sitei466 – 4661Transition 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

    MEROPSiM01.015.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aminopeptidase N (EC:3.4.11.2)
    Short name:
    AP-N
    Alternative name(s):
    Membrane glycoprotein H11
    Microsomal aminopeptidase
    OrganismiHaemonchus contortus (Barber pole worm)
    Taxonomic identifieri6289 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaStrongylidaTrichostrongyloideaHaemonchidaeHaemonchinaeHaemonchus

    Subcellular locationi

    Membrane By similarity; Single-pass type II membrane protein By similarity

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 972971Aminopeptidase NPRO_0000095087Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi99 – 991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi227 – 2271N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi549 – 5491N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi759 ↔ 766By similarity
    Disulfide bondi804 ↔ 840By similarity
    Glycosylationi858 – 8581N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiQ10737.

    Structurei

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 1716CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini40 – 972933ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei18 – 3922Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni343 – 3475Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the peptidase M1 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    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.

    Q10737-1 [UniParc]FASTAAdd to Basket

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    MTSQGRTRTL LNLTPIRLIV ALFLVAAAVG LSIGLTYYFT RKAFDTSEKP    50
    GKDDTGGKDK DNSPSAAELL LPSNIKPLSY DLTIKTYLPG YVDFPPEKNL 100
    TFDGRVEISM VVIEPTKSIV LNSKKISVIP QECELVSGDK KLEIESVKEH 150
    PRLEKVEFLI KSQLEKDQQI LLKVGYIGLI SNSFGGIYQT TYTTPDGTPK 200
    IAAVSQNEPI DARRMVPCMD EPKYKANWTV TVIHPKGTKA VSNGIEVNGD 250
    GEISGDWITS KFLTTPRMSS YLLAVMVSEF EYIEGETKTG VRFRIWSRPE 300
    AKKMTQYALQ SGIKCIEFYE DFFDIRFPLK KQDMIALPDF SAGAMENWGL 350
    ITYRENSLLY DDRFYAPMNK QRIARIVAHE LAHQWFGDLV TMKWWDNLWL 400
    NEGFARFTEF IGAGQITQDD ARMRNYFLID VLERALKADS VASSHPLSFR 450
    IDKAAEVEEA FDDITYAKGA SVLTMLRALI GEEKHKHAVS QYLKKFSYSN 500
    AEATDLWAVF DEVVTDVEGP DGKPMKTTEF ASQWTTQMGF PVISVAEFNS 550
    TTLKLTQSRY EANKDAVEKE KYRHPKYGFK WDIPLWYQEG DKKEIKRTWL 600
    RRDEPLYLHV SDAGAPFVVN ADRYGFYRQN HDANGWKKII KQLKDNHEVY 650
    SPRTRNAIIS DAFAAAATDA IEYETVFELL NYAEKETEYL PLEIAMSGIS 700
    SILKYFGTEP EAKPAQTYMM NILKPMYEKS SIDFIANNYR NDKLFFQINL 750
    QKDVIDMFCA LGSQDCRKKY KKLFDDEVMN KCRDGQAATE CVRIAAPLRS 800
    SVYCYGVKEG GDYASDKVME LYTAETLALE KDFLRLALGC HKDVTALKGL 850
    LLRALDRNSS FVRMQDIPSA FNDVAANPIG GEFIFNFLIE RWPDIIESIG 900
    TKHTYVEKVI PACTSGIRSQ QQIDQLKNLQ KNGMNARQFG AFDKAIERAQ 950
    NRVDWIKKHF QKLAAFFKKA TL 972
    Length:972
    Mass (Da):110,674
    Last modified:January 23, 2007 - v2
    Checksum:i5964328CC3C80E43
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X94187 mRNA. Translation: CAA63897.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X94187 mRNA. Translation: CAA63897.1 .

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M01.015.

    Proteomic databases

    PRIDEi Q10737.

    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 a microsomal aminopeptidase from the intestine of the nematode Haemonchus contortus."
      Smith T.S., Graham M., Munn E.A., Newton S.E., Knox D.P., Coadwell W.J., McMichael-Phillips D., Smith H., Smith W.D., Oliver J.J.
      Biochim. Biophys. Acta 1338:295-306(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiAMPN_HAECO
    AccessioniPrimary (citable) accession number: Q10737
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 82 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    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