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Protein

Lysozyme C

Gene

LYZ

Organism
Callithrix jacchus (White-tufted-ear marmoset)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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)DescriptionActionsGraphical viewLength
Active sitei53PROSITE-ProRule annotation1
Active sitei71PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

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
Synonyms:LZM
OrganismiCallithrix jacchus (White-tufted-ear marmoset)
Taxonomic identifieri9483 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniPlatyrrhiniCebidaeCallitrichinaeCallithrix
Proteomesi
  • UP000008225 Componenti: Chromosome 9

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18By similarityAdd BLAST18
ChainiPRO_000001845919 – 148Lysozyme CAdd BLAST130

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi24 ↔ 146PROSITE-ProRule annotation
Disulfide bondi48 ↔ 134PROSITE-ProRule annotation
Disulfide bondi83 ↔ 99PROSITE-ProRule annotation
Disulfide bondi95 ↔ 113PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi9483.ENSCJAP00000003201.

Structurei

3D structure databases

ProteinModelPortaliP79158.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IXGD. Eukaryota.
ENOG4111QHM. LUCA.
GeneTreeiENSGT00550000074398.
HOGENOMiHOG000037357.
HOVERGENiHBG052297.
InParanoidiP79158.
KOiK13915.
OMAiHCFRRRH.
OrthoDBiEOG091G0R9V.
TreeFamiTF324882.

Family and domain databases

CDDicd00119. LYZ1. 1 hit.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P79158-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVLIILGLV LLSVMVQGKV FERCELARTL KRFGLDGYRG ISLANWMCLA
60 70 80 90 100
KWESDYNTRA TNYNPGDQST DYGIFQINSH YWCNNGRTPG AVNACHISCN
110 120 130 140
ALLQDDITEA VACAKRVVRD PQGIRAWVAW KAHCQNRDVS QYVQGCGV
Length:148
Mass (Da):16,602
Last modified:May 1, 1997 - v1
Checksum:iC79BB37557B1E951
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U76923 mRNA. Translation: AAB41203.1.
RefSeqiXP_002752792.1. XM_002752746.3.

Genome annotation databases

EnsembliENSCJAT00000003379; ENSCJAP00000003201; ENSCJAG00000001788.
GeneIDi100393686.
KEGGicjc:100393686.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U76923 mRNA. Translation: AAB41203.1.
RefSeqiXP_002752792.1. XM_002752746.3.

3D structure databases

ProteinModelPortaliP79158.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9483.ENSCJAP00000003201.

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSCJAT00000003379; ENSCJAP00000003201; ENSCJAG00000001788.
GeneIDi100393686.
KEGGicjc:100393686.

Organism-specific databases

CTDi4069.

Phylogenomic databases

eggNOGiENOG410IXGD. Eukaryota.
ENOG4111QHM. LUCA.
GeneTreeiENSGT00550000074398.
HOGENOMiHOG000037357.
HOVERGENiHBG052297.
InParanoidiP79158.
KOiK13915.
OMAiHCFRRRH.
OrthoDBiEOG091G0R9V.
TreeFamiTF324882.

Family and domain databases

CDDicd00119. LYZ1. 1 hit.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiLYSC_CALJA
AccessioniPrimary (citable) accession number: P79158
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: October 5, 2016
This is version 92 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, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.