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Protein

Elastase-1

Gene
N/A
Organism
Salmo salar (Atlantic salmon)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts upon elastin.1 Publication

Catalytic activityi

Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-Xaa.1 Publication

Cofactori

Ca2+1 PublicationNote: Binds 1 Ca2+ ion per subunit.1 Publication

Kineticsi

  1. KM=1.47 mM for Suc-AAA-pNA (at 22 degrees Celsius)1 Publication
  2. KM=1.34 mM for Suc-AAPL-pNA (at 22 degrees Celsius)1 Publication
  3. KM=0.82 mM for Suc-AAPV-pNA (at 22 degrees Celsius)1 Publication
  4. KM=0.83 mM for Suc-AAPA-pNA (at 22 degrees Celsius)1 Publication
  5. KM=0.15 mM for Suc-AAPI-pNA (at 22 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 8.1 at 22 degrees Celsius with Suc-AAA-pNA as the substrate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei45 – 451Charge relay system1 Publication
    Metal bindingi59 – 591Calcium1 Publication
    Metal bindingi61 – 611Calcium; via carbonyl oxygen
    Metal bindingi64 – 641Calcium; via carbonyl oxygen
    Metal bindingi66 – 661Calcium1 Publication
    Metal bindingi69 – 691Calcium1 Publication
    Active sitei93 – 931Charge relay system1 Publication
    Active sitei187 – 1871Charge relay system1 Publication

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elastase-1 (EC:3.4.21.36)
    OrganismiSalmo salar (Atlantic salmon)
    Taxonomic identifieri8030 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiProtacanthopterygiiSalmoniformesSalmonidaeSalmoninaeSalmo

    Subcellular locationi

    • Secreted 1 Publication

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 236236Elastase-1PRO_0000248261Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi30 ↔ 46PROSITE-ProRule annotation1 Publication
    Disulfide bondi127 ↔ 193PROSITE-ProRule annotation1 Publication
    Disulfide bondi158 ↔ 174PROSITE-ProRule annotation1 Publication
    Disulfide bondi183 ↔ 213PROSITE-ProRule annotation1 Publication

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Tissue specificityi

    Pancreas.1 Publication

    Structurei

    Secondary structure

    1
    236
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 65Combined sources
    Beta strandi15 – 228Combined sources
    Beta strandi25 – 3612Combined sources
    Beta strandi39 – 424Combined sources
    Helixi44 – 474Combined sources
    Beta strandi53 – 586Combined sources
    Beta strandi70 – 723Combined sources
    Beta strandi74 – 796Combined sources
    Helixi88 – 903Combined sources
    Beta strandi95 – 1017Combined sources
    Beta strandi106 – 1083Combined sources
    Beta strandi127 – 1326Combined sources
    Beta strandi146 – 1494Combined sources
    Helixi155 – 1584Combined sources
    Turni161 – 1644Combined sources
    Helixi165 – 1673Combined sources
    Beta strandi172 – 1754Combined sources
    Beta strandi190 – 1956Combined sources
    Beta strandi198 – 20710Combined sources
    Beta strandi220 – 2245Combined sources
    Helixi225 – 2284Combined sources
    Helixi229 – 2357Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ELTX-ray1.61A1-236[»]
    ProteinModelPortaliQ7SIG3.
    SMRiQ7SIG3. Positions 1-236.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ7SIG3.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 236236Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family. Elastase subfamily.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

    Phylogenomic databases

    HOVERGENiHBG013304.

    Family and domain databases

    InterProiIPR009003. Peptidase_S1_PA.
    IPR001314. Peptidase_S1A.
    IPR001254. Trypsin_dom.
    IPR018114. TRYPSIN_HIS.
    IPR033116. TRYPSIN_SER.
    [Graphical view]
    PfamiPF00089. Trypsin. 1 hit.
    [Graphical view]
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q7SIG3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    VVGGRVAQPN SWPWQISLQY KSGSSYYHTC GGSLIRQGWV MTAAHCVDSA
    60 70 80 90 100
    RTWRVVLGEH NLNTNEGKEQ IMTVNSVFIH SGWNSDDVAG GYDIALLRLN
    110 120 130 140 150
    TQASLNSAVQ LAALPPSNQI LPNNNPCYIT GWGKTSTGGP LSDSLKQAWL
    160 170 180 190 200
    PSVDHATCSS SGWWGSTVKT TMVCAGGGAN SGCNGDSGGP LNCQVNGSYY
    210 220 230
    VHGVTSFVSS SGCNASKKPT VFTRVSAYIS WMNGIM
    Length:236
    Mass (Da):25,015
    Last modified:December 15, 2003 - v1
    Checksum:i06CF7DB4E1397E97
    GO

    Cross-referencesi

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ELTX-ray1.61A1-236[»]
    ProteinModelPortaliQ7SIG3.
    SMRiQ7SIG3. Positions 1-236.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    HOVERGENiHBG013304.

    Miscellaneous databases

    EvolutionaryTraceiQ7SIG3.

    Family and domain databases

    InterProiIPR009003. Peptidase_S1_PA.
    IPR001314. Peptidase_S1A.
    IPR001254. Trypsin_dom.
    IPR018114. TRYPSIN_HIS.
    IPR033116. TRYPSIN_SER.
    [Graphical view]
    PfamiPF00089. Trypsin. 1 hit.
    [Graphical view]
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "Purification and characterization of pancreatic elastase from North Atlantic salmon (Salmo salar)."
      Berglund G.I., Smalaas A.O., Outzen H., Willassen N.P.
      Mol. Mar. Biol. Biotechnol. 7:105-114(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. "Crystallization and preliminary X-ray crystallographic studies of native elastase from North Atlantic salmon (Salmo salar)."
      Berglund G.I., Smalaas A.O., Hansen L.K., Willassen N.P.
      Acta Crystallogr. D 51:393-394(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CRYSTALLIZATION, X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
    3. "Structure of native pancreatic elastase from North Atlantic salmon at 1.61 A resolution."
      Berglund G.I., Willassen N.P., Hordvik A., Smalaas A.O.
      Acta Crystallogr. D 51:925-937(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS), COFACTOR, DISULFIDE BONDS.

    Entry informationi

    Entry nameiELA1_SALSA
    AccessioniPrimary (citable) accession number: Q7SIG3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2006
    Last sequence update: December 15, 2003
    Last modified: March 16, 2016
    This is version 63 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.