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Protein

Lysozyme C-1/C-2

Gene
N/A
Organism
Axis axis (Axis deer) (Chital)
Status
Reviewed-Annotation score: 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.

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 1 is shown.

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 sitei35PROSITE-ProRule annotation1
Active sitei53PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAntimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase
Biological processDigestion

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme C-1/C-2 (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase C
OrganismiAxis axis (Axis deer) (Chital)
Taxonomic identifieri30531 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraCervidaeCervinaeAxis

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002088431 – 129Lysozyme C-1/C-2Add BLAST129

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi6 ↔ 127PROSITE-ProRule annotation
Disulfide bondi30 ↔ 115PROSITE-ProRule annotation
Disulfide bondi65 ↔ 81PROSITE-ProRule annotation
Disulfide bondi77 ↔ 95PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP12066.

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP12066.
SMRiP12066.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOVERGENiHBG052297.

Family and domain databases

CDDicd00119. LYZ1. 1 hit.
InterProiView protein in InterPro
IPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
IPR030056. Lysozyme_C.
PANTHERiPTHR11407:SF39. PTHR11407:SF39. 1 hit.
PfamiView protein in Pfam
PF00062. Lys. 1 hit.
PRINTSiPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTiView protein in SMART
SM00263. LYZ1. 1 hit.
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiView protein in PROSITE
PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.

Sequencei

Sequence statusi: Complete.

P12066-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
KVFERCELAR TLKELGLDGY KGVSLANWLC LTKWESSYNT KATNYNPGSE
60 70 80 90 100
STDYGIFQIN SKWWCDDGKT PNAVDGCHVA CSELMENNID KAVTCAKQIV
110 120
REQGITAWVA WKSHCRGHDV SSYVEGCTL
Length:129
Mass (Da):14,446
Last modified:October 1, 1989 - v1
Checksum:iA0AA48E69C2EB383
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti66D → N in isozyme 2. 1
Natural varianti88N → D in isozyme 2. 1
Natural varianti90D → A in isozyme 2. 1
Natural varianti94T → A in isozyme 2. 1
Natural varianti117G → H in isozyme 2. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32499 mRNA. Translation: AAA30344.1.
M32500 mRNA. Translation: AAA30345.1.
PIRiG35558.
H35558.

Similar proteinsi

Entry informationi

Entry nameiLYSC_AXIAX
AccessioniPrimary (citable) accession number: P12066
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: September 27, 2017
This is version 90 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

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