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Protein

Lysozyme C, milk isozyme

Gene

LYZ

Organism
Equus caballus (Horse)
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.

Cofactori

Ca2+Note: Binds 1 Ca2+ ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei35 – 351PROSITE-ProRule annotation
Active sitei53 – 531PROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi81 – 9212PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. lysozyme activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

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

Keywords - Ligandi

Calcium, Metal-binding

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme C, milk isozyme (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase C
Gene namesi
Name:LYZ
OrganismiEquus caballus (Horse)
Taxonomic identifieri9796 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus
ProteomesiUP000002281: Unplaced

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 129129Lysozyme C, milk isozymePRO_0000208851Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi6 ↔ 127PROSITE-ProRule annotation
Disulfide bondi30 ↔ 115PROSITE-ProRule annotation
Disulfide bondi65 ↔ 80PROSITE-ProRule annotation
Disulfide bondi76 ↔ 94PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi9796.ENSECAP00000008172.

Structurei

Secondary structure

1
129
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 139Combined sources
Turni14 – 196Combined sources
Helixi20 – 223Combined sources
Helixi25 – 3612Combined sources
Beta strandi37 – 393Combined sources
Beta strandi43 – 453Combined sources
Beta strandi52 – 543Combined sources
Turni55 – 584Combined sources
Helixi61 – 644Combined sources
Beta strandi68 – 714Combined sources
Helixi80 – 834Combined sources
Beta strandi84 – 863Combined sources
Helixi89 – 9810Combined sources
Helixi104 – 1074Combined sources
Helixi109 – 1146Combined sources
Turni115 – 1173Combined sources
Turni121 – 1266Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EQLX-ray2.50A1-129[»]
ProteinModelPortaliP11376.
SMRiP11376. Positions 1-129.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11376.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 22 family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG85133.
HOGENOMiHOG000037357.
HOVERGENiHBG052297.
InParanoidiP11376.

Family and domain databases

InterProiIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
IPR030056. Lysozyme_C.
[Graphical view]
PANTHERiPTHR11407:SF22. PTHR11407:SF22. 1 hit.
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.

P11376-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
KVFSKCELAH KLKAQEMDGF GGYSLANWVC MAEYESNFNT RAFNGKNANG
60 70 80 90 100
SSDYGLFQLN NKWWCKDNKR SSSNACNIMC SKLLDENIDD DISCAKRVVR
110 120
DPKGMSAWKA WVKHCKDKDL SEYLASCNL
Length:129
Mass (Da):14,653
Last modified:July 1, 1989 - v1
Checksum:i87040531F4B60F46
GO

Sequence databases

PIRiS07435.

Cross-referencesi

Sequence databases

PIRiS07435.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EQLX-ray2.50A1-129[»]
ProteinModelPortaliP11376.
SMRiP11376. Positions 1-129.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9796.ENSECAP00000008172.

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiNOG85133.
HOGENOMiHOG000037357.
HOVERGENiHBG052297.
InParanoidiP11376.

Miscellaneous databases

EvolutionaryTraceiP11376.

Family and domain databases

InterProiIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
IPR030056. Lysozyme_C.
[Graphical view]
PANTHERiPTHR11407:SF22. PTHR11407:SF22. 1 hit.
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...

Publicationsi

  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.

Entry informationi

Entry nameiLYSC1_HORSE
AccessioniPrimary (citable) accession number: P11376
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: January 7, 2015
This is version 101 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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.