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Protein

Lysozyme C-3

Gene
N/A
Organism
Sus scrofa (Pig)
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.

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

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-3 (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase C
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 181 PublicationAdd BLAST18
ChainiPRO_000001848019 – 148Lysozyme C-3Add 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

Proteomic databases

PeptideAtlasiP12069.
PRIDEiP12069.

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP12069.
SMRiP12069.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000037357.
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.

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

P12069-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTLLVLALL LLSVSVQAKV YDRCEFARIL KKSGMDGYRG VSLANWVCLA
60 70 80 90 100
KWESNFNTKA TNYNPGSQST DYGIFQINSR YWCNDGKTPK AVNACHISCK
110 120 130 140
VLLDDDLSQD IECAKRVVRD PQGIKAWVAW KAHCQNKDVS QYIRGCKL
Length:148
Mass (Da):16,711
Last modified:November 1, 1997 - v2
Checksum:i76AA67BFABBD64E6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U44435 mRNA. Translation: AAA86644.1.
PIRiS10047.
UniGeneiSsc.670.

Similar proteinsi

Entry informationi

Entry nameiLYSC3_PIG
AccessioniPrimary (citable) accession number: P12069
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 1, 1997
Last modified: September 27, 2017
This is version 96 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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