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P11376 (LYSC1_HORSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 98. 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
Gene names
Name:LYZ
OrganismEquus caballus (Horse) [Reference proteome]
Taxonomic identifier9796 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus

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.

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.

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.

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_0000208851

Regions

Calcium binding81 – 9212 By similarity

Sites

Active site351 By similarity
Active site531 By similarity

Amino acid modifications

Disulfide bond6 ↔ 127 By similarity
Disulfide bond30 ↔ 115 By similarity
Disulfide bond65 ↔ 80 By similarity
Disulfide bond76 ↔ 94 By similarity

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P11376 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 87040531F4B60F46

FASTA12914,653
        10         20         30         40         50         60 
KVFSKCELAH KLKAQEMDGF GGYSLANWVC MAEYESNFNT RAFNGKNANG SSDYGLFQLN 

        70         80         90        100        110        120 
NKWWCKDNKR SSSNACNIMC SKLLDENIDD DISCAKRVVR DPKGMSAWKA WVKHCKDKDL 


SEYLASCNL 

« Hide

References

[1]"The amino acid sequence of equine milk lysozyme."
McKenzie H.A., Shaw D.C.
Biochem. Int. 10:23-31(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Milk.
[2]"The calcium-binding property of equine lysozyme."
Nitta K., Tsuge H., Sugai S., Shimazaki K.
FEBS Lett. 223:405-408(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: CALCIUM-BINDING DATA.
Tissue: Milk.
[3]"Crystallization of a calcium-binding lysozyme from horse milk."
Zeng J., Rao K.R., Brew K., Fenna R.
J. Biol. Chem. 265:14886-14887(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-35, CRYSTALLIZATION.
Tissue: Milk.
[4]"A structural study of calcium-binding equine lysozyme by two-dimensional 1H-NMR."
Tsuge H., Koseki K., Miyano M., Shimazaki K., Chuman T., Matsumoto T., Noma M., Nitta K., Sugai S.
Biochim. Biophys. Acta 1078:77-84(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
Tissue: Milk.
[5]"Crystallographic studies of a calcium binding lysozyme from equine milk at 2.5-A resolution."
Tsuge H., Ago H., Noma M., Nitta K., Sugai S., Miyano M.
J. Biochem. 111:141-143(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Tissue: Milk.

Cross-references

Sequence databases

PIRS07435.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EQLX-ray2.50A1-129[»]
ProteinModelPortalP11376.
SMRP11376. Positions 1-129.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9796.ENSECAP00000008172.

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG85133.
HOGENOMHOG000037357.
HOVERGENHBG052297.
InParanoidP11376.

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

EvolutionaryTraceP11376.

Entry information

Entry nameLYSC1_HORSE
AccessionPrimary (citable) accession number: P11376
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: March 19, 2014
This is version 98 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