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P11941

- LYSC2_ONCMY

UniProt

P11941 - LYSC2_ONCMY

Protein

Lysozyme C II

Gene
N/A
Organism
Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Status
Reviewed - Annotation score: 5 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. Has antibacterial activity against the Gram positive bacterium P.citreus. Has no antibacterial activity against the Gram negative bacteria E.coli and Y.ruckeri. Does not have hemolytic activity against trout erythrocytes.1 PublicationPROSITE-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.1 Publication

    pH dependencei

    Optimum pH is 4.5-5.5. No activity above pH 8.8.1 Publication

    Temperature dependencei

    Optimum temperature is 33-49 degrees Celsius. Retains 25% of its maximal activity after heating 10 minutes at 80 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei50 – 501
    Active sitei67 – 671

    GO - Molecular functioni

    1. lysozyme activity Source: UniProtKB-EC

    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

    Antibiotic, Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

    Protein family/group databases

    CAZyiGH22. Glycoside Hydrolase Family 22.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysozyme C II (EC:3.2.1.17)
    Alternative name(s):
    1,4-beta-N-acetylmuramidase C
    Lysozyme type II
    OrganismiOncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
    Taxonomic identifieri8022 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiProtacanthopterygiiSalmoniformesSalmonidaeSalmoninaeOncorhynchus

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 15152 PublicationsAdd
    BLAST
    Chaini16 – 144129Lysozyme C IIPRO_0000018501Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi21 ↔ 142
    Disulfide bondi45 ↔ 130
    Disulfide bondi79 ↔ 95
    Disulfide bondi91 ↔ 109

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiP11941.

    Structurei

    Secondary structure

    1
    144
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi20 – 2910
    Helixi40 – 5112
    Beta strandi58 – 603
    Beta strandi66 – 683
    Turni69 – 724
    Turni75 – 773
    Helixi95 – 984
    Beta strandi99 – 1024
    Helixi104 – 11310
    Helixi119 – 1224
    Helixi124 – 1296
    Turni130 – 1323
    Helixi136 – 1383
    Turni139 – 1413

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BB6X-ray2.00A16-144[»]
    1BB7X-ray2.00A16-144[»]
    1LMCX-ray2.00A16-144[»]
    1LMNX-ray1.80A16-144[»]
    1LMOX-ray1.80A16-144[»]
    1LMPX-ray2.00A16-144[»]
    1LMQX-ray1.60A16-144[»]
    ProteinModelPortaliP11941.
    SMRiP11941. Positions 16-144.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11941.

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOVERGENiHBG052297.

    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.

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

    P11941-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRAVVVLLLV AVASAKVYDR CELARALKAS GMDGYAGNSL PNWVCLSKWE    50
    SSYNTQATNR NTDGSTDYGI FQINSRYWCD DGRTPGAKNV CGIRCSQLLT 100
    ADLTVAIRCA KRVVLDPNGI GAWVAWRLHC QNQDLRSYVA GCGV 144
    Length:144
    Mass (Da):15,737
    Last modified:April 1, 1993 - v2
    Checksum:iBF945ADCDCC2D668
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti94 – 941R → H in AAG34564. 1 PublicationCurated
    Sequence conflicti101 – 1011A → D in AAG34564. 1 PublicationCurated

    Mass spectrometryi

    Molecular mass is 14252 Da from positions 16 - 144. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59491 mRNA. Translation: CAA42084.1.
    AF322106 Genomic DNA. Translation: AAG45933.1.
    AF452171 Genomic DNA. Translation: AAL48290.1.
    AF321519 mRNA. Translation: AAG34564.1.
    PIRiI51047.
    RefSeqiNP_001118188.1. NM_001124716.1.
    UniGeneiOmy.11916.

    Genome annotation databases

    GeneIDi100136768.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59491 mRNA. Translation: CAA42084.1 .
    AF322106 Genomic DNA. Translation: AAG45933.1 .
    AF452171 Genomic DNA. Translation: AAL48290.1 .
    AF321519 mRNA. Translation: AAG34564.1 .
    PIRi I51047.
    RefSeqi NP_001118188.1. NM_001124716.1.
    UniGenei Omy.11916.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BB6 X-ray 2.00 A 16-144 [» ]
    1BB7 X-ray 2.00 A 16-144 [» ]
    1LMC X-ray 2.00 A 16-144 [» ]
    1LMN X-ray 1.80 A 16-144 [» ]
    1LMO X-ray 1.80 A 16-144 [» ]
    1LMP X-ray 2.00 A 16-144 [» ]
    1LMQ X-ray 1.60 A 16-144 [» ]
    ProteinModelPortali P11941.
    SMRi P11941. Positions 16-144.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH22. Glycoside Hydrolase Family 22.

    Proteomic databases

    PRIDEi P11941.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100136768.

    Organism-specific databases

    CTDi 17105.

    Phylogenomic databases

    HOVERGENi HBG052297.

    Miscellaneous databases

    EvolutionaryTracei P11941.

    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. "cDNA and amino acid sequences of rainbow trout (Oncorhynchus mykiss) lysozymes and their implications for the evolution of lysozyme and lactalbumin."
      Dautingny A., Prager E.M., Pham-Dinh D., Jolles J., Pakdel F., Grinde B., Jolles P.
      J. Mol. Evol. 32:187-198(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Molecular characterization of lysozyme type II gene from rainbow trout (Oncorhynchus mykiss): an evidence of a duplicate gene."
      Mitra A., Foster-Frey J., Wells K.D., Rexroad C.E. III, Wall R.J.
      Anim. Biotechnol. 14:7-12(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Kamploop.
      Tissue: Kidney.
    3. "A new genetic variant of lysozyme from rainbow trout."
      Mitra A., Wells K.D., Rexroad C.E. III, Wall R.J.
      Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Kidney.
    4. "Purification and characterization of two lysozymes from rainbow trout (Salmo gairdneri)."
      Grinde B., Jolles J., Jolles P.
      Eur. J. Biochem. 173:269-273(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 16-50.
    5. "Two novel muramidases from skin mucosa of rainbow trout (Oncorhynchus mykiss)."
      Fernandes J.M.O., Kemp G.D., Smith V.J.
      Comp. Biochem. Physiol. 138B:53-64(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 16-30, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY.
      Tissue: Skin mucus.
    6. "Refined crystal structure of lysozyme from the rainbow trout (Oncorhynchus mykiss)."
      Karlsen S., Eliassen B.E., Hansen L.K., Larsen R.L., Riise B.W., Smalaas A.O., Hough E., Grinde B.
      Acta Crystallogr. D 51:354-367(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    7. "Structural studies on the binding of 4-methylumbelliferone glycosides of chitin to rainbow trout lysozyme."
      Vollan V.B., Hough E., Karlsen S.
      Acta Crystallogr. D 55:60-66(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

    Entry informationi

    Entry nameiLYSC2_ONCMY
    AccessioniPrimary (citable) accession number: P11941
    Secondary accession number(s): P83333, Q9DDK3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 95 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    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