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P00705

- LYSC1_ANAPL

UniProt

P00705 - LYSC1_ANAPL

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Protein

Lysozyme C-1

Gene
N/A
Organism
Anas platyrhynchos (Domestic duck) (Anas boschas)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei53 – 531PROSITE-ProRule annotation
Active sitei70 – 701PROSITE-ProRule annotation

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
Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme C-1 (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase C
OrganismiAnas platyrhynchos (Domestic duck) (Anas boschas)
Taxonomic identifieri8839 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeAnseriformesAnatidaeAnas
ProteomesiUP000016666: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18182 PublicationsAdd
BLAST
Chaini19 – 147129Lysozyme C-1PRO_0000018494Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 1451 PublicationPROSITE-ProRule annotation
Disulfide bondi48 ↔ 1331 PublicationPROSITE-ProRule annotation
Disulfide bondi82 ↔ 981 PublicationPROSITE-ProRule annotation
Disulfide bondi94 ↔ 1121 PublicationPROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP00705.

Structurei

3D structure databases

ProteinModelPortaliP00705.
SMRiP00705. Positions 19-147.
ModBaseiSearch...
MobiDBiSearch...

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.

P00705-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKALLTLVFC LLPLAAQGKV YSRCELAAAM KRLGLDNYRG YSLGNWVCAA
60 70 80 90 100
NYESGFNTQA TNRNTDGSTD YGILQINSRW WCDNGKTPRS KNACGIPCSV
110 120 130 140
LLRSDITEAV RCAKRIVSDG DGMNAWVAWR NRCRGTDVSK WIRGCRL
Length:147
Mass (Da):16,363
Last modified:July 21, 1986 - v1
Checksum:iB0F2B6A9F7DA3978
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti43 – 431L → I in DL3.
Natural varianti55 – 551G → S in DL1 and lysozyme II.
Natural varianti75 – 751Q → E in lysozyme II.
Natural varianti89 – 891R → G in DL1 and lysozyme II.
Natural varianti97 – 971P → R in DL3.

Sequence databases

PIRiD92574. LZDK.

Cross-referencesi

Sequence databases

PIRi D92574. LZDK.

3D structure databases

ProteinModelPortali P00705.
SMRi P00705. Positions 19-147.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH22. Glycoside Hydrolase Family 22.

Proteomic databases

PRIDEi P00705.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG052297.

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. "Evolutionary shift in the site of cleavage of prelysozyme."
    Weisman L.S., Krummel B.M., Wilson A.C.
    J. Biol. Chem. 261:2309-2313(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-18.
    Strain: Pekin breed.
  2. "Chemical and immunological properties and amino acid sequences of three lysozymes from Peking-duck egg white."
    Kondo K., Fujio H., Amano T.
    J. Biochem. 91:571-587(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-147 (DL-1; DL-2 AND DL-3).
    Strain: Pekin breed.
  3. "Multiple forms of duck-egg white lysozyme. Primary structure of two duck lysozymes."
    Hermann J., Jolles J., Jolles P.
    Eur. J. Biochem. 24:12-17(1971) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-147 (LYSOZYME II).
  4. "The disulfide bridges of duck egg-white lysozyme II."
    Hermann J., Jolles J., Jolles P.
    Arch. Biochem. Biophys. 158:355-358(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  5. "Multiple lysozymes of duck egg white."
    Prager E.M., Wilson A.C.
    J. Biol. Chem. 246:523-530(1971) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS DL-1; DL-2 AND DL-3C.
    Strain: Pekin breed.

Entry informationi

Entry nameiLYSC1_ANAPL
AccessioniPrimary (citable) accession number: P00705
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 29, 2014
This is version 81 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.
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.
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.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3