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Protein

Lysozyme C-1

Gene
N/A
Organism
Anas platyrhynchos (Mallard) (Anas boschas)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei53PROSITE-ProRule annotation1
Active sitei70PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

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 (Mallard) (Anas boschas)
Taxonomic identifieri8839 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeAnseriformesAnatidaeAnas
Proteomesi
  • UP000016666 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 182 PublicationsAdd BLAST18
ChainiPRO_000001849419 – 147Lysozyme C-1Add BLAST129

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi24 ↔ 145PROSITE-ProRule annotation1 Publication
Disulfide bondi48 ↔ 133PROSITE-ProRule annotation1 Publication
Disulfide bondi82 ↔ 98PROSITE-ProRule annotation1 Publication
Disulfide bondi94 ↔ 112PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP00705.

Structurei

3D structure databases

ProteinModelPortaliP00705.
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

CDDicd00119. LYZ1. 1 hit.
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)DescriptionActionsGraphical viewLength
Natural varianti43L → I in DL3. 1
Natural varianti55G → S in DL1 and lysozyme II. 1
Natural varianti75Q → E in lysozyme II. 1
Natural varianti89R → G in DL1 and lysozyme II. 1
Natural varianti97P → R in DL3. 1

Sequence databases

PIRiD92574. LZDK.

Cross-referencesi

Sequence databases

PIRiD92574. LZDK.

3D structure databases

ProteinModelPortaliP00705.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Proteomic databases

PRIDEiP00705.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG052297.

Family and domain databases

CDDicd00119. LYZ1. 1 hit.
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]
ProtoNetiSearch...

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 5, 2016
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.
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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.