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Protein

Lysozyme C

Gene

LYZ

Organism
Oryctolagus cuniculus (Rabbit)
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.

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.

Sites

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

GO - Molecular functioni

  1. lysozyme activity Source: UniProtKB-EC

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

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme C (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase C
Gene namesi
Name:LYZ
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 130130Lysozyme CPRO_0000208855Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi6 ↔ 128PROSITE-ProRule annotation
Disulfide bondi30 ↔ 116PROSITE-ProRule annotation
Disulfide bondi65 ↔ 81PROSITE-ProRule annotation
Disulfide bondi77 ↔ 95PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP16973.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000011947.

Structurei

3D structure databases

ProteinModelPortaliP16973.
SMRiP16973. Positions 1-130.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG85133.
HOGENOMiHOG000037357.
HOVERGENiHBG052297.
InParanoidiP16973.

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.

P16973-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
KIYERCELAR TLKKLGLDGY KGVSLANWMC LAKWESSYNT RATNYNPGDK
60 70 80 90 100
STDYGIFQIN SRYWCNDGKT PRAVNACHIP CSDLLKDDIT QAVACAKRVV
110 120 130
SDPQGIRAWV AWRNHCQNQD LTPYIRGCGV
Length:130
Mass (Da):14,722
Last modified:July 31, 1990 - v1
Checksum:i000A3330EDB26C25
GO

Sequence databases

PIRiJC2506.
JX0104.
JX0367.

Cross-referencesi

Sequence databases

PIRiJC2506.
JX0104.
JX0367.

3D structure databases

ProteinModelPortaliP16973.
SMRiP16973. Positions 1-130.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000011947.

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Proteomic databases

PRIDEiP16973.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiNOG85133.
HOGENOMiHOG000037357.
HOVERGENiHBG052297.
InParanoidiP16973.

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. "Purification, amino acid sequence, and some properties of rabbit kidney lysozyme."
    Ito Y., Yamada H., Nakamura S., Imoto T.
    J. Biochem. 107:236-241(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Kidney.

Entry informationi

Entry nameiLYSC_RABIT
AccessioniPrimary (citable) accession number: P16973
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 31, 1990
Last sequence update: July 31, 1990
Last modified: March 3, 2015
This is version 85 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. 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.