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P07584

- ASTA_ASTAS

UniProt

P07584 - ASTA_ASTAS

Protein

Astacin

Gene
N/A
Organism
Astacus astacus (Noble crayfish) (Astacus fluviatilis)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    This protease prefers to cleave in front of small aliphatic residues (P1'). The presence of Lys or Arg in the P1 and P2 position yields high-turnover substrates. In the P3 position the enzyme prefers Pro > Val > Leu > Ala > Gly.

    Catalytic activityi

    Hydrolysis of peptide bonds in substrates containing five or more amino acids, preferentially with Ala in P1', and Pro in P2'.1 Publication

    Cofactori

    Binds 1 zinc ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi141 – 1411Zinc; catalytic1 PublicationPROSITE-ProRule annotation
    Active sitei142 – 1421
    Metal bindingi145 – 1451Zinc; catalytic1 PublicationPROSITE-ProRule annotation
    Metal bindingi151 – 1511Zinc; catalytic1 PublicationPROSITE-ProRule annotation

    GO - Molecular functioni

    1. aspartic-type peptidase activity Source: UniProtKB
    2. glutamic-type peptidase activity Source: UniProtKB
    3. metalloendopeptidase activity Source: InterPro
    4. peptidase activity Source: UniProtKB
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cell adhesion Source: UniProtKB
    2. fertilization Source: UniProtKB
    3. negative regulation of binding of sperm to zona pellucida Source: UniProtKB
    4. positive regulation of protein processing Source: UniProtKB
    5. prevention of polyspermy Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    SABIO-RKP07584.

    Protein family/group databases

    MEROPSiM12.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Astacin (EC:3.4.24.21)
    Alternative name(s):
    Crayfish small molecule proteinase
    OrganismiAstacus astacus (Noble crayfish) (Astacus fluviatilis)
    Taxonomic identifieri6715 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaCrustaceaMalacostracaEumalacostracaEucaridaDecapodaPleocyemataAstacideaAstacoideaAstacidaeAstacus

    Subcellular locationi

    GO - Cellular componenti

    1. cortical granule Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. plasma membrane Source: UniProtKB

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1515Sequence AnalysisAdd
    BLAST
    Propeptidei16 – 4934Activation peptide1 PublicationPRO_0000028872Add
    BLAST
    Chaini50 – 249200Astacin1 PublicationPRO_0000028873Add
    BLAST
    Propeptidei250 – 2512PRO_0000028874

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi91 ↔ 2471 Publication
    Disulfide bondi113 ↔ 1331 Publication

    Keywords - PTMi

    Disulfide bond, Zymogen

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    Secondary structure

    1
    251
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi21 – 277
    Turni34 – 363
    Beta strandi46 – 483
    Beta strandi51 – 533
    Helixi55 – 573
    Helixi60 – 623
    Beta strandi63 – 708
    Helixi73 – 8917
    Beta strandi93 – 964
    Beta strandi101 – 11818
    Beta strandi121 – 1288
    Turni130 – 1334
    Helixi136 – 14712
    Helixi152 – 1543
    Helixi158 – 1603
    Beta strandi162 – 1643
    Helixi166 – 1683
    Helixi174 – 1774
    Beta strandi181 – 1844
    Turni200 – 2034
    Turni205 – 2095
    Beta strandi212 – 2176
    Helixi225 – 2273
    Helixi233 – 24210
    Helixi244 – 2496

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ASTX-ray1.80A50-249[»]
    1IAAX-ray1.90A50-249[»]
    1IABX-ray1.79A50-249[»]
    1IACX-ray2.10A50-249[»]
    1IADX-ray2.30A50-249[»]
    1IAEX-ray1.83A50-249[»]
    1QJIX-ray2.14A50-249[»]
    1QJJX-ray1.86A50-249[»]
    3LQ0X-ray1.45A16-250[»]
    ProteinModelPortaliP07584.
    SMRiP07584. Positions 50-249.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07584.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M12A family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.40.390.10. 1 hit.
    InterProiIPR024079. MetalloPept_cat_dom.
    IPR001506. Peptidase_M12A.
    IPR006026. Peptidase_Metallo.
    [Graphical view]
    PfamiPF01400. Astacin. 1 hit.
    [Graphical view]
    PRINTSiPR00480. ASTACIN.
    SMARTiSM00235. ZnMc. 1 hit.
    [Graphical view]
    PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P07584-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQCAVLLVLL GVVAASPIIP EAARALYYND GMFEGDIKLR AGRQPARVGA    50
    AILGDEYLWS GGVIPYTFAG VSGADQSAIL SGMQELEEKT CIRFVPRTTE 100
    SDYVEIFTSG SGCWSYVGRI SGAQQVSLQA NGCVYHGTII HELMHAIGFY 150
    HEHTRMDRDN YVTINYQNVD PSMTSNFDID TYSRYVGEDY QYYSIMHYGK 200
    YSFSIQWGVL ETIVPLQNGI DLTDPYDKAH MLQTDANQIN NLYTNECSLR 250
    H 251
    Length:251
    Mass (Da):28,093
    Last modified:October 1, 1996 - v2
    Checksum:i00E76C704334343B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X95684 Genomic DNA. Translation: CAA64981.1.
    PIRiA58830. HYCY.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X95684 Genomic DNA. Translation: CAA64981.1 .
    PIRi A58830. HYCY.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AST X-ray 1.80 A 50-249 [» ]
    1IAA X-ray 1.90 A 50-249 [» ]
    1IAB X-ray 1.79 A 50-249 [» ]
    1IAC X-ray 2.10 A 50-249 [» ]
    1IAD X-ray 2.30 A 50-249 [» ]
    1IAE X-ray 1.83 A 50-249 [» ]
    1QJI X-ray 2.14 A 50-249 [» ]
    1QJJ X-ray 1.86 A 50-249 [» ]
    3LQ0 X-ray 1.45 A 16-250 [» ]
    ProteinModelPortali P07584.
    SMRi P07584. Positions 50-249.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M12.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P07584.

    Miscellaneous databases

    EvolutionaryTracei P07584.

    Family and domain databases

    Gene3Di 3.40.390.10. 1 hit.
    InterProi IPR024079. MetalloPept_cat_dom.
    IPR001506. Peptidase_M12A.
    IPR006026. Peptidase_Metallo.
    [Graphical view ]
    Pfami PF01400. Astacin. 1 hit.
    [Graphical view ]
    PRINTSi PR00480. ASTACIN.
    SMARTi SM00235. ZnMc. 1 hit.
    [Graphical view ]
    PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genomic organization of the zinc-endopeptidase astacin."
      Geier G., Jacob E., Stoecker W., Zwilling R.
      Arch. Biochem. Biophys. 337:300-307(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Amino acid sequence of a unique protease from the crayfish Astacus fluviatilis."
      Titani K., Torff H.-J., Hormel S., Kumar S., Walsh K.A., Rodl J., Neurath H., Zwilling R.
      Biochemistry 26:222-226(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 50-249.
    3. "Astacus protease, a zinc metalloenzyme."
      Stoecker W., Wolz R.L., Zwilling R., Strydom D.J., Auld D.S.
      Biochemistry 27:5026-5032(1988)
      Cited for: ZINC-BINDING, ENZYME ACTIVITY.
    4. "Fluorescent oligopeptide substrates for kinetic characterization of the specificity of Astacus protease."
      Stoecker W., Ng M., Auld D.S.
      Biochemistry 29:10418-10425(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBSTRATE SPECIFICITY.
    5. "Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases."
      Bode W., Gomis-Rueth F.-X., Huber R., Zwilling R., Stoecker W.
      Nature 358:164-167(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    6. "Refined 1.8 A X-ray crystal structure of astacin, a zinc-endopeptidase from the crayfish Astacus astacus L. Structure determination, refinement, molecular structure and comparison with thermolysin."
      Gomis-Rueth F.-X., Stoecker W., Huber R., Zwilling R., Bode W.
      J. Mol. Biol. 229:945-968(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    7. Cited for: X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) OF 50-249.

    Entry informationi

    Entry nameiASTA_ASTAS
    AccessioniPrimary (citable) accession number: P07584
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 102 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
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3