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P11376

- LYSC1_HORSE

UniProt

P11376 - LYSC1_HORSE

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Protein

Lysozyme C, milk isozyme

Gene
LYZ
Organism
Equus caballus (Horse)
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.

Cofactori

Binds 1 calcium ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei35 – 351 By similarity
Active sitei53 – 531 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi81 – 9212 By similarityAdd
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 ↔ 127 By similarity
Disulfide bondi30 ↔ 115 By similarity
Disulfide bondi65 ↔ 80 By similarity
Disulfide bondi76 ↔ 94 By similarity

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 – 139
Turni14 – 196
Helixi20 – 223
Helixi25 – 3612
Beta strandi37 – 393
Beta strandi43 – 453
Beta strandi52 – 543
Turni55 – 584
Helixi61 – 644
Beta strandi68 – 714
Helixi80 – 834
Beta strandi84 – 863
Helixi89 – 9810
Helixi104 – 1074
Helixi109 – 1146
Turni115 – 1173
Turni121 – 1266

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EQLX-ray2.50A1-129[»]
ProteinModelPortaliP11376.
SMRiP11376. Positions 1-129.

Miscellaneous databases

EvolutionaryTraceiP11376.

Family & Domainsi

Sequence similaritiesi

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.
[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.

P11376-1 [UniParc]FASTAAdd to Basket

« Hide

KVFSKCELAH KLKAQEMDGF GGYSLANWVC MAEYESNFNT RAFNGKNANG    50
SSDYGLFQLN NKWWCKDNKR SSSNACNIMC SKLLDENIDD DISCAKRVVR 100
DPKGMSAWKA WVKHCKDKDL SEYLASCNL 129
Length:129
Mass (Da):14,653
Last modified:July 1, 1989 - v1
Checksum:i87040531F4B60F46
GO

Sequence databases

PIRiS07435.

Cross-referencesi

Sequence databases

PIRi S07435.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2EQL X-ray 2.50 A 1-129 [» ]
ProteinModelPortali P11376.
SMRi P11376. Positions 1-129.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9796.ENSECAP00000008172.

Protein family/group databases

CAZyi GH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi NOG85133.
HOGENOMi HOG000037357.
HOVERGENi HBG052297.
InParanoidi P11376.

Miscellaneous databases

EvolutionaryTracei P11376.

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. "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: March 19, 2014
This is version 98 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

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