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Protein

Lysozyme C, milk isozyme

Gene
N/A
Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed-Annotation score: Annotation score: 3 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.PROSITE-ProRule annotation

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 – 9212Add
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. cytolysis Source: UniProtKB-KW
  2. defense response to bacterium Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase, Milk protein

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
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254: Unplaced

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 129129Lysozyme C, milk isozymePRO_0000208845Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP81708.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000013141.

Structurei

Secondary structure

1
129
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1410Combined sources
Helixi25 – 3612Combined sources
Beta strandi43 – 464Combined sources
Beta strandi48 – 503Combined sources
Beta strandi52 – 543Combined sources
Turni55 – 584Combined sources
Turni61 – 644Combined sources
Beta strandi68 – 703Combined sources
Helixi80 – 845Combined sources
Helixi89 – 9810Combined sources
Beta strandi101 – 1033Combined 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
1EL1X-ray1.90A/B1-129[»]
1I56NMR-A1-129[»]
1QQYX-ray1.85A1-129[»]
2CWIX-ray1.94A/B1-129[»]
2Z2EX-ray2.01A/B1-129[»]
ProteinModelPortaliP81708.
SMRiP81708. Positions 1-129.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP81708.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG85133.
HOGENOMiHOG000037357.
HOVERGENiHBG052297.
OrthoDBiEOG7BW0M5.

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.

P81708-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
KIFSKCELAR KLKSMGMDGF HGYSLANWVC MAEYESNFNT QAFNGRNSNG
60 70 80 90 100
SSDYGIFQLN SKWWCKSNSH SSANACNIMC SKFLDDNIDD DIACAKRVVK
110 120
DPNGMSAWVA WVKHCKGKDL SKYLASCNL
Length:129
Mass (Da):14,471
Last modified:December 1, 2000 - v1
Checksum:i64CD8C3F9C80359A
GO

Sequence databases

PIRiS48641.

Cross-referencesi

Sequence databases

PIRiS48641.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP81708.
SMRiP81708. Positions 1-129.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000013141.

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Proteomic databases

PaxDbiP81708.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiNOG85133.
HOGENOMiHOG000037357.
HOVERGENiHBG052297.
OrthoDBiEOG7BW0M5.

Miscellaneous databases

EvolutionaryTraceiP81708.

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. "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.

Entry informationi

Entry nameiLYSC1_CANFA
AccessioniPrimary (citable) accession number: P81708
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: March 4, 2015
This is version 96 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 (By similarity).By similarity

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.