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UniProtKB/Swiss-Prot entry P00705


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LYSC1_ANAPL
Primary accession number P00705
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 21, 1986 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 62)
Name and origin of the protein
Protein name Lysozyme C-1 [Precursor]
Synonyms EC 3.2.1.17
1,4-beta-N-acetylmuramidase C
Gene name None
From
Anas platyrhynchos (Domestic duck) [TaxID: 8839] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; Neognathae; Anseriformes; Anatidae; Anas.
Protein existence 1: Evidence at protein level;
References
[1]
PROTEIN SEQUENCE OF 1-18.
STRAIN=Pekin breed;
PubMed=3511061 [NCBI, ExPASy, EBI, Israel, Japan]
Weisman L.S., Krummel B.M., Wilson A.C.;
"Evolutionary shift in the site of cleavage of prelysozyme.";
J. Biol. Chem. 261:2309-2313(1986).
[2]
PROTEIN SEQUENCE OF 19-147 (DL-1; DL-2 AND DL-3).
STRAIN=Pekin breed;
PubMed=7068576 [NCBI, ExPASy, EBI, Israel, Japan]
Kondo K., Fujio H., Amano T.;
"Chemical and immunological properties and amino acid sequences of three lysozymes from Peking-duck egg white.";
J. Biochem. 91:571-587(1982).
[3]
PROTEIN SEQUENCE OF 19-147 (LYSOZYME II).
PubMed=5138644 [NCBI, ExPASy, EBI, Israel, Japan]
Hermann J., Jolles J., Jolles P.;
"Multiple forms of duck-egg white lysozyme. Primary structure of two duck lysozymes.";
Eur. J. Biochem. 24:12-17(1971).
[4]
DISULFIDE BONDS.
DOI=10.1016/0003-9861(73)90631-0; PubMed=4580844 [NCBI, ExPASy, EBI, Israel, Japan]
Hermann J., Jolles J., Jolles P.;
"The disulfide bridges of duck egg-white lysozyme II.";
Arch. Biochem. Biophys. 158:355-358(1973).
[5]
CHARACTERIZATION OF VARIANTS DL-1; DL-2 AND DL-3C.
STRAIN=Pekin breed;
PubMed=5542021 [NCBI, ExPASy, EBI, Israel, Japan]
Prager E.M., Wilson A.C.;
"Multiple lysozymes of duck egg white.";
J. Biol. Chem. 246:523-530(1971).
Comments
  • FUNCTION: 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 ACTIVITY: 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.
  • 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.
  • MISCELLANEOUS: The sequence of the DL-2 variant of lysozyme C from Pekin duck is shown. As only one lysozyme, or any combination of 2 lysozymes, but never all 3, occurred in one egg, the existence of 3 alleles at one locus has been suggested.
  • MISCELLANEOUS: The amino acid compositions of DL-1, DL-2, and DL-3 are identical with those of lysozymes A, B, and C, respectively. DL-1 and DL-2 are electrophoretically and immunologically indistinguishable from lysozymes A and B, respectively.
  • SIMILARITY: Belongs to the glycosyl hydrolase 22 family [view classification].
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
PIR D92574; LZDK.
3D structure databases
HSSP P00698; 1AT6. [HSSP ENTRY / PDB]
SMR P00705; 19-147.
ModBase P00705.
Ontologies
GO
GO:0019835; Biological process: cytolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0042742; Biological process: defense response to bacterium (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001916; Glyco_hydro_22.
IPR000974; Glyco_hydro_22_lys.
Graphical view of domain structure.
Pfam PF00062; Lys; 1.
Pfam graphical view of domain structure.
PRINTS PR00137; LYSOZYME.
PR00135; LYZLACT.
SMART SM00263; LYZ1; 1.
SMART graphical view of domain structure.
PROSITE PS00128; LACTALBUMIN_LYSOZYME_1; 1.
PS51348; LACTALBUMIN_LYSOZYME_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P00705.
ProtoNet P00705.
Phylogenomic databases
HOVERGEN P00705; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Antimicrobial; Bacteriolytic enzyme; Direct protein sequencing; Glycosidase; Hydrolase; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
SIGNAL   1    18  18      
CHAIN   19   147  129     Lysozyme C-1. PRO_0000018494
ACT_SITE   53    53        By similarity. 
ACT_SITE   70    70        By similarity. 
DISULFID   24   145         
DISULFID   48   133         
DISULFID   82    98         
DISULFID   94   112         
VARIANT   43    43  1     L -> I (in DL3). 
VARIANT   55    55  1     G -> S (in DL1 and lysozyme II). 
VARIANT   75    75  1     Q -> E (in lysozyme II). 
VARIANT   89    89  1     R -> G (in DL1 and lysozyme II). 
VARIANT   97    97  1     P -> R (in DL3). 
Sequence information
Length: 147 AA [This is the length of the unprocessed precursor] Molecular weight: 16363 Da [This is the MW of the unprocessed precursor] CRC64: B0F2B6A9F7DA3978 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKALLTLVFC LLPLAAQGKV YSRCELAAAM KRLGLDNYRG YSLGNWVCAA NYESGFNTQA 

        70         80         90        100        110        120 
TNRNTDGSTD YGILQINSRW WCDNGKTPRS KNACGIPCSV LLRSDITEAV RCAKRIVSDG 

       130        140 
DGMNAWVAWR NRCRGTDVSK WIRGCRL 

P00705 in FASTA format

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