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P81708 (LYSC1_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysozyme C, milk isozyme

EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase C
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length129 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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 By similarity.

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.

Cofactor

Binds 1 calcium ion per subunit.

Subunit structure

Monomer By similarity.

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 By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 22 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 129129Lysozyme C, milk isozyme
PRO_0000208845

Regions

Calcium binding81 – 9212 Ref.3

Sites

Active site351 By similarity
Active site531 By similarity

Amino acid modifications

Disulfide bond6 ↔ 127 Ref.2 Ref.3
Disulfide bond30 ↔ 115 Ref.2 Ref.3
Disulfide bond65 ↔ 80 Ref.2 Ref.3
Disulfide bond76 ↔ 94 Ref.2 Ref.3

Secondary structure

............................ 129
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P81708 [UniParc].

Last modified December 1, 2000. Version 1.
Checksum: 64CD8C3F9C80359A

FASTA12914,471
        10         20         30         40         50         60 
KIFSKCELAR KLKSMGMDGF HGYSLANWVC MAEYESNFNT QAFNGRNSNG SSDYGIFQLN 

        70         80         90        100        110        120 
SKWWCKSNSH SSANACNIMC SKFLDDNIDD DIACAKRVVK DPNGMSAWVA WVKHCKGKDL 


SKYLASCNL 

« Hide

References

[1]"Sequences of two highly divergent canine type c lysozymes: implications for the evolutionary origins of the lysozyme/alpha-lactalbumin superfamily."
Grobler J.A., Rao K.R., Pervaiz S., Brew K.
Arch. Biochem. Biophys. 313:360-366(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Milk.
[2]"Structure and thermodynamics of the extraordinarily stable molten globule state of canine milk lysozyme."
Koshiba T., Yao M., Kobashigawa Y., Demura M., Nakagawa A., Tanaka I., Kuwajima K., Nitta K.
Biochemistry 39:3248-3257(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), DISULFIDE BONDS.
[3]"Different folding pathways taken by highly homologous proteins, goat alpha-lactalbumin and canine milk lysozyme."
Nakamura T., Makabe K., Tomoyori K., Maki K., Mukaiyama A., Kuwajima K.
J. Mol. Biol. 396:1361-1378(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), CALCIUM-BINDING REGION, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRS48641.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EL1X-ray1.90A/B1-129[»]
1I56NMR-A1-129[»]
1QQYX-ray1.85A1-129[»]
2CWIX-ray1.94A/B1-129[»]
2Z2EX-ray2.01A/B1-129[»]
ProteinModelPortalP81708.
SMRP81708. Positions 1-129.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9615.ENSCAFP00000013141.

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Proteomic databases

PaxDbP81708.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG85133.
HOGENOMHOG000037357.
HOVERGENHBG052297.
InParanoidP81708.
OrthoDBEOG7BW0M5.

Family and domain databases

InterProIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamPF00062. Lys. 1 hit.
[Graphical view]
PRINTSPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMSSF53955. SSF53955. 1 hit.
PROSITEPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP81708.

Entry information

Entry nameLYSC1_CANFA
AccessionPrimary (citable) accession number: P81708
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: November 13, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries