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Protein

Lysozyme C-1

Gene
N/A
Organism
Ovis aries (Sheep)
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

Keywords - Biological processi

Digestion

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme C-1 (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase C
OrganismiOvis aries (Sheep)
Taxonomic identifieri9940 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis
Proteomesi
  • UP000002356 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18By similarityAdd BLAST18
ChainiPRO_000001848819 – 147Lysozyme C-1Add BLAST129

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi24 ↔ 145PROSITE-ProRule annotation
Disulfide bondi48 ↔ 133PROSITE-ProRule annotation
Disulfide bondi83 ↔ 99PROSITE-ProRule annotation
Disulfide bondi95 ↔ 113PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed in stomach.

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP17607.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG052297.
KOiK13915.

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.

P17607-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKALIILGLL CLSVAVQGKV FERCELARTL KELGLDGYKG VSLANWLCLT
60 70 80 90 100
KWESSYNTKA TNYNPGSEST DYGIFQINSK WWCNDGKTPN AVDGCHVSCS
110 120 130 140
ELMENNIAKA VACAKHIVSE QGITAWVAWK SHCRDHDVSS YVEGCSL
Length:147
Mass (Da):16,195
Last modified:January 27, 2003 - v2
Checksum:i065D72BC42B0A6E0
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti32E → K in isozyme 3A and isozyme 4A/4B. 1
Natural varianti37G → D in isozyme 4A/4B. 1
Natural varianti55S → G in isozyme 3A. 1
Natural varianti101E → A in isozyme 2A, isozyme 3A and isozyme 4A/4B. 1
Natural varianti106N → D in isozyme 2A, isozyme 3A and isozyme 4A/4B. 1
Natural varianti108A → E in isozyme 2A, isozyme 3A and isozyme 4A/4B. 1
Natural varianti146S → T in isozyme 2A, isozyme 3A and isozyme 4A/4B. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF170555
, AF170552, AF170553, AF170554 Genomic DNA. Translation: AAD51636.1.
M32492 mRNA. Translation: AAA31557.1.
M32493 mRNA. Translation: AAA31558.1.
M32494 mRNA. Translation: AAA31559.1.
M32495 mRNA. Translation: AAA31560.1.
M32496 mRNA. Translation: AAA31561.1.
M32497 mRNA. Translation: AAA31562.1.
M32498 mRNA. Translation: AAA31563.1.
PIRiD35558.
E35558.
F35558.
RefSeqiNP_001295517.1. NM_001308588.1.
UniGeneiOar.378.
Oar.379.
Oar.380.

Genome annotation databases

GeneIDi443320.
KEGGioas:443320.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF170555
, AF170552, AF170553, AF170554 Genomic DNA. Translation: AAD51636.1.
M32492 mRNA. Translation: AAA31557.1.
M32493 mRNA. Translation: AAA31558.1.
M32494 mRNA. Translation: AAA31559.1.
M32495 mRNA. Translation: AAA31560.1.
M32496 mRNA. Translation: AAA31561.1.
M32497 mRNA. Translation: AAA31562.1.
M32498 mRNA. Translation: AAA31563.1.
PIRiD35558.
E35558.
F35558.
RefSeqiNP_001295517.1. NM_001308588.1.
UniGeneiOar.378.
Oar.379.
Oar.380.

3D structure databases

ProteinModelPortaliP17607.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi443320.
KEGGioas:443320.

Phylogenomic databases

HOVERGENiHBG052297.
KOiK13915.

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 nameiLYSC1_SHEEP
AccessioniPrimary (citable) accession number: P17607
Secondary accession number(s): Q9TUN2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 27, 2003
Last modified: October 5, 2016
This is version 95 of the entry and version 2 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.
The sequence of isozyme 1A/1B/1C is shown.

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.