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P81708

- LYSC1_CANFA

UniProt

P81708 - LYSC1_CANFA

Protein

Lysozyme C, milk isozyme

Gene
N/A
Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.PROSITE-ProRule annotation

    Catalytic activityi

    Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.

    Cofactori

    Binds 1 calcium ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei35 – 351PROSITE-ProRule annotation
    Active sitei53 – 531PROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi81 – 9212Add
    BLAST

    GO - Molecular functioni

    1. lysozyme activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. cell wall macromolecule catabolic process Source: InterPro
    2. cytolysis Source: UniProtKB-KW
    3. defense response to bacterium Source: UniProtKB-KW

    Keywords - Molecular functioni

    Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase, Milk protein

    Keywords - Ligandi

    Calcium, Metal-binding

    Protein family/group databases

    CAZyiGH22. Glycoside Hydrolase Family 22.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysozyme C, milk isozyme (EC:3.2.1.17)
    Alternative name(s):
    1,4-beta-N-acetylmuramidase C
    OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
    Taxonomic identifieri9615 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
    ProteomesiUP000002254: Unplaced

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 129129Lysozyme C, milk isozymePRO_0000208845Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi6 ↔ 127
    Disulfide bondi30 ↔ 115
    Disulfide bondi65 ↔ 80
    Disulfide bondi76 ↔ 94

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP81708.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi9615.ENSCAFP00000013141.

    Structurei

    Secondary structure

    1
    129
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 1410
    Helixi25 – 3612
    Beta strandi43 – 464
    Beta strandi48 – 503
    Beta strandi52 – 543
    Turni55 – 584
    Turni61 – 644
    Beta strandi68 – 703
    Helixi80 – 845
    Helixi89 – 9810
    Beta strandi101 – 1033
    Helixi104 – 1074
    Helixi109 – 1146
    Turni115 – 1173
    Turni121 – 1266

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EL1X-ray1.90A/B1-129[»]
    1I56NMR-A1-129[»]
    1QQYX-ray1.85A1-129[»]
    2CWIX-ray1.94A/B1-129[»]
    2Z2EX-ray2.01A/B1-129[»]
    ProteinModelPortaliP81708.
    SMRiP81708. Positions 1-129.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP81708.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 22 family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG85133.
    HOGENOMiHOG000037357.
    HOVERGENiHBG052297.
    InParanoidiP81708.
    OrthoDBiEOG7BW0M5.

    Family and domain databases

    InterProiIPR001916. Glyco_hydro_22.
    IPR019799. Glyco_hydro_22_CS.
    IPR000974. Glyco_hydro_22_lys.
    IPR023346. Lysozyme-like_dom.
    [Graphical view]
    PfamiPF00062. Lys. 1 hit.
    [Graphical view]
    PRINTSiPR00137. LYSOZYME.
    PR00135. LYZLACT.
    SMARTiSM00263. LYZ1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53955. SSF53955. 1 hit.
    PROSITEiPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
    PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P81708-1 [UniParc]FASTAAdd to Basket

    « Hide

    KIFSKCELAR KLKSMGMDGF HGYSLANWVC MAEYESNFNT QAFNGRNSNG    50
    SSDYGIFQLN SKWWCKSNSH SSANACNIMC SKFLDDNIDD DIACAKRVVK 100
    DPNGMSAWVA WVKHCKGKDL SKYLASCNL 129
    Length:129
    Mass (Da):14,471
    Last modified:December 1, 2000 - v1
    Checksum:i64CD8C3F9C80359A
    GO

    Sequence databases

    PIRiS48641.

    Cross-referencesi

    Sequence databases

    PIRi S48641.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EL1 X-ray 1.90 A/B 1-129 [» ]
    1I56 NMR - A 1-129 [» ]
    1QQY X-ray 1.85 A 1-129 [» ]
    2CWI X-ray 1.94 A/B 1-129 [» ]
    2Z2E X-ray 2.01 A/B 1-129 [» ]
    ProteinModelPortali P81708.
    SMRi P81708. Positions 1-129.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9615.ENSCAFP00000013141.

    Protein family/group databases

    CAZyi GH22. Glycoside Hydrolase Family 22.

    Proteomic databases

    PaxDbi P81708.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi NOG85133.
    HOGENOMi HOG000037357.
    HOVERGENi HBG052297.
    InParanoidi P81708.
    OrthoDBi EOG7BW0M5.

    Miscellaneous databases

    EvolutionaryTracei P81708.

    Family and domain databases

    InterProi IPR001916. Glyco_hydro_22.
    IPR019799. Glyco_hydro_22_CS.
    IPR000974. Glyco_hydro_22_lys.
    IPR023346. Lysozyme-like_dom.
    [Graphical view ]
    Pfami PF00062. Lys. 1 hit.
    [Graphical view ]
    PRINTSi PR00137. LYSOZYME.
    PR00135. LYZLACT.
    SMARTi SM00263. LYZ1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53955. SSF53955. 1 hit.
    PROSITEi PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
    PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequences of two highly divergent canine type c lysozymes: implications for the evolutionary origins of the lysozyme/alpha-lactalbumin superfamily."
      Grobler J.A., Rao K.R., Pervaiz S., Brew K.
      Arch. Biochem. Biophys. 313:360-366(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
      Tissue: Milk.
    2. "Structure and thermodynamics of the extraordinarily stable molten globule state of canine milk lysozyme."
      Koshiba T., Yao M., Kobashigawa Y., Demura M., Nakagawa A., Tanaka I., Kuwajima K., Nitta K.
      Biochemistry 39:3248-3257(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), DISULFIDE BONDS.
    3. "Different folding pathways taken by highly homologous proteins, goat alpha-lactalbumin and canine milk lysozyme."
      Nakamura T., Makabe K., Tomoyori K., Maki K., Mukaiyama A., Kuwajima K.
      J. Mol. Biol. 396:1361-1378(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), CALCIUM-BINDING REGION, DISULFIDE BONDS.

    Entry informationi

    Entry nameiLYSC1_CANFA
    AccessioniPrimary (citable) accession number: P81708
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: December 1, 2000
    Last modified: October 1, 2014
    This is version 92 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Lysozyme C is capable of both hydrolysis and transglycosylation; it shows also a slight esterase activity. It acts rapidly on both peptide-substituted and unsubstituted peptidoglycan, and slowly on chitin oligosaccharides By similarity.By similarity

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3