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P82176

- IMPI_GALME

UniProt

P82176 - IMPI_GALME

Protein

Inducible metalloproteinase inhibitor protein

Gene

IMPI

Organism
Galleria mellonella (Greater wax moth)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 2 (15 Aug 2003)
      Previous versions | rss
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    Functioni

    Inhibits thermolysin, bacillolysin and pseudolysin, B.polymyxa metalloprotease and human MMP1 and MMP3. No activity on trypsin or cysteine protease papain.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei88 – 892CleavageCurated

    GO - Molecular functioni

    1. metalloendopeptidase inhibitor activity Source: UniProtKB

    GO - Biological processi

    1. anatomical structure morphogenesis Source: UniProtKB
    2. extracellular matrix organization Source: UniProtKB
    3. negative regulation of endopeptidase activity Source: GOC
    4. wound healing Source: UniProtKB

    Keywords - Molecular functioni

    Metalloenzyme inhibitor, Metalloprotease inhibitor, Protease inhibitor

    Protein family/group databases

    MEROPSiI08.006.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inducible metalloproteinase inhibitor protein
    Cleaved into the following chain:
    Gene namesi
    Name:IMPI
    OrganismiGalleria mellonella (Greater wax moth)
    Taxonomic identifieri7137 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaPyraloideaPyralidaeGalleriinaeGalleria

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 170151Inducible metalloproteinase inhibitor proteinPRO_0000021511Add
    BLAST
    Chaini20 – 8869IMPI alphaPRO_0000021512Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi48 – 481N-linked (GlcNAc...)1 Publication
    Glycosylationi149 – 1491N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Cleaved.Curated
    Five disulfide bonds are present. When artificially cleaved by thermolysin between Asn-56 and Ile-57, the two obtained chains (called heavy and light chains) remain linked.
    The N-terminus is blocked.

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Expressioni

    Inductioni

    During humoral immune response. By lipopolysaccharide (LPS).2 Publications

    Structurei

    Secondary structure

    1
    170
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi26 – 349
    Helixi41 – 433
    Turni44 – 463
    Beta strandi49 – 513
    Beta strandi60 – 656
    Beta strandi69 – 713
    Beta strandi77 – 793
    Helixi80 – 823

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3SSBX-ray1.80C/D19-56[»]
    I/J57-88[»]
    ProteinModelPortaliP82176.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP82176.

    Family & Domainsi

    Keywords - Domaini

    Signal

    Family and domain databases

    InterProiIPR002919. TIL_dom.
    [Graphical view]
    PfamiPF01826. TIL. 1 hit.
    [Graphical view]
    SUPFAMiSSF57567. SSF57567. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P82176-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKCLLYLCLW CYCVLVSSSI VLICNGGHEY YECGGACDNV CADLHIQNKT    50
    NCPIINIRCN DKCYCEDGYA RDVNGKCIPI KDCPKIRSRR SIGIPVDKKC 100
    CTGPNEHYDE EKVSCPPETC ISLVAKFSCI DSPPPSPGCS CNSGYLRLNL 150
    TSPCIPICDC PQMQHSPDCQ 170
    Length:170
    Mass (Da):18,759
    Last modified:August 15, 2003 - v2
    Checksum:i1A5B272846AD129A
    GO

    Mass spectrometryi

    Molecular mass is 8360 Da from positions 20 - 88. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY330624 mRNA. Translation: AAQ73240.1.
    AJ577749 mRNA. Translation: CAE12200.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY330624 mRNA. Translation: AAQ73240.1 .
    AJ577749 mRNA. Translation: CAE12200.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3SSB X-ray 1.80 C/D 19-56 [» ]
    I/J 57-88 [» ]
    ProteinModelPortali P82176.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi I08.006.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P82176.

    Family and domain databases

    InterProi IPR002919. TIL_dom.
    [Graphical view ]
    Pfami PF01826. TIL. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57567. SSF57567. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of an inhibitor of microbial metalloproteinases from insects contributing to innate immunity."
      Clermont A., Wedde M., Seitz V., Podsiadlowski L., Lenze D., Hummel M., Vilcinskas A.
      Biochem. J. 382:315-322(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION.
    2. "Hemolymph proteins of the greater wax moth, Galleria mellonella."
      Weise C., Bender O., Kopacek P., Hucho F.
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Purification and characterization of an inducible metalloprotease inhibitor from the hemolymph of greater wax moth larvae, Galleria mellonella."
      Wedde M., Weise C., Kopacek P., Franke P., Vilcinskas A.
      Eur. J. Biochem. 255:535-543(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 57-82, FUNCTION, INDUCTION, BLOCKAGE OF N-TERMINUS, GLYCOSYLATION.
      Tissue: Larval hemolymph.
    4. Weise C.
      Submitted (JUL-2003) to UniProtKB
      Cited for: SEQUENCE REVISION TO 63, MASS SPECTROMETRY.

    Entry informationi

    Entry nameiIMPI_GALME
    AccessioniPrimary (citable) accession number: P82176
    Secondary accession number(s): Q67FQ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: August 15, 2003
    Last modified: October 1, 2014
    This is version 58 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3