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Protein

Lysozyme C

Gene

LYZ

Organism
Pygathrix nemaeus (Red-shanked douc langur)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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

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
OrganismiPygathrix nemaeus (Red-shanked douc langur)
Taxonomic identifieri54133 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeColobinaePygathrix

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 – 18By similarityAdd BLAST18
ChainiPRO_000001848319 – 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

Proteomic databases

PRIDEiP79847

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP79847
SMRiP79847
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Signal

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_sf
IPR030056 Lysozyme_C
PANTHERiPTHR11407:SF28 PTHR11407:SF28, 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.

P79847-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKALIILGLV LLSVTVQGKI FERCELARTL KKLGLDGYKG VSLANWVCLA
60 70 80 90 100
KWESGYNTEA TNYNPGDEST DYGIFQINSR YWCNNGKTPG AVDACHISCS
110 120 130 140
ALLQNNIADA VACAKRVVSD PQGVRAWVAW RNHCQNKDVS QYVKGCGV
Length:148
Mass (Da):16,217
Last modified:May 1, 1997 - v1
Checksum:iD2D0D48A499370B6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U76944
, U76941, U76942, U76943 Genomic DNA Translation: AAB41217.1

Similar proteinsi

Entry informationi

Entry nameiLYSC_PYGNE
AccessioniPrimary (citable) accession number: P79847
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: May 23, 2018
This is version 76 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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