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P11376

- LYSC1_HORSE

UniProt

P11376 - LYSC1_HORSE

Protein

Lysozyme C, milk isozyme

Gene

LYZ

Organism
Equus caballus (Horse)
Status
Reviewed - Annotation score: 4 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.

    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 – 9212PROSITE-ProRule annotationAdd
    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

    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
    Gene namesi
    Name:LYZ
    OrganismiEquus caballus (Horse)
    Taxonomic identifieri9796 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus
    ProteomesiUP000002281: Unplaced

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 129129Lysozyme C, milk isozymePRO_0000208851Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    STRINGi9796.ENSECAP00000008172.

    Structurei

    Secondary structure

    1
    129
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 139
    Turni14 – 196
    Helixi20 – 223
    Helixi25 – 3612
    Beta strandi37 – 393
    Beta strandi43 – 453
    Beta strandi52 – 543
    Turni55 – 584
    Helixi61 – 644
    Beta strandi68 – 714
    Helixi80 – 834
    Beta strandi84 – 863
    Helixi89 – 9810
    Helixi104 – 1074
    Helixi109 – 1146
    Turni115 – 1173
    Turni121 – 1266

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EQLX-ray2.50A1-129[»]
    ProteinModelPortaliP11376.
    SMRiP11376. Positions 1-129.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11376.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG85133.
    HOGENOMiHOG000037357.
    HOVERGENiHBG052297.
    InParanoidiP11376.

    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.

    P11376-1 [UniParc]FASTAAdd to Basket

    « Hide

    KVFSKCELAH KLKAQEMDGF GGYSLANWVC MAEYESNFNT RAFNGKNANG    50
    SSDYGLFQLN NKWWCKDNKR SSSNACNIMC SKLLDENIDD DISCAKRVVR 100
    DPKGMSAWKA WVKHCKDKDL SEYLASCNL 129
    Length:129
    Mass (Da):14,653
    Last modified:July 1, 1989 - v1
    Checksum:i87040531F4B60F46
    GO

    Sequence databases

    PIRiS07435.

    Cross-referencesi

    Sequence databases

    PIRi S07435.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EQL X-ray 2.50 A 1-129 [» ]
    ProteinModelPortali P11376.
    SMRi P11376. Positions 1-129.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9796.ENSECAP00000008172.

    Protein family/group databases

    CAZyi GH22. Glycoside Hydrolase Family 22.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi NOG85133.
    HOGENOMi HOG000037357.
    HOVERGENi HBG052297.
    InParanoidi P11376.

    Miscellaneous databases

    EvolutionaryTracei P11376.

    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. "The amino acid sequence of equine milk lysozyme."
      McKenzie H.A., Shaw D.C.
      Biochem. Int. 10:23-31(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
      Tissue: Milk.
    2. "The calcium-binding property of equine lysozyme."
      Nitta K., Tsuge H., Sugai S., Shimazaki K.
      FEBS Lett. 223:405-408(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: CALCIUM-BINDING DATA.
      Tissue: Milk.
    3. "Crystallization of a calcium-binding lysozyme from horse milk."
      Zeng J., Rao K.R., Brew K., Fenna R.
      J. Biol. Chem. 265:14886-14887(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-35, CRYSTALLIZATION.
      Tissue: Milk.
    4. "A structural study of calcium-binding equine lysozyme by two-dimensional 1H-NMR."
      Tsuge H., Koseki K., Miyano M., Shimazaki K., Chuman T., Matsumoto T., Noma M., Nitta K., Sugai S.
      Biochim. Biophys. Acta 1078:77-84(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
      Tissue: Milk.
    5. "Crystallographic studies of a calcium binding lysozyme from equine milk at 2.5-A resolution."
      Tsuge H., Ago H., Noma M., Nitta K., Sugai S., Miyano M.
      J. Biochem. 111:141-143(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
      Tissue: Milk.

    Entry informationi

    Entry nameiLYSC1_HORSE
    AccessioniPrimary (citable) accession number: P11376
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 99 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.

    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