Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lysozyme C-2

Gene

LYZ2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -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 ruminant gastric lysozymes, which digest symbiotic bacteria coming with cud from the rumen, are much more resistant to inactivation by pepsin than are other lysozymes.

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

Enzyme and pathway databases

BRENDAi3.2.1.17 908
ReactomeiR-BTA-6798695 Neutrophil degranulation
R-BTA-6803157 Antimicrobial peptides

Protein family/group databases

CAZyiGH22 Glycoside Hydrolase Family 22

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme C-2 (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase C
Gene namesi
Name:LYZ2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18By similarityAdd BLAST18
ChainiPRO_000001845519 – 147Lysozyme C-2Add BLAST129

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi24 ↔ 145PROSITE-ProRule annotation1 Publication
Disulfide bondi48 ↔ 133PROSITE-ProRule annotation1 Publication
Disulfide bondi83 ↔ 99PROSITE-ProRule annotation1 Publication
Disulfide bondi95 ↔ 113PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ06283
PRIDEiQ06283

Expressioni

Tissue specificityi

Stomach-specific.

Gene expression databases

BgeeiENSBTAG00000026088

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000007924

Structurei

Secondary structure

1147
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi23 – 32Combined sources10
Helixi43 – 54Combined sources12
Beta strandi61 – 64Combined sources4
Turni65 – 68Combined sources4
Beta strandi69 – 72Combined sources4
Turni73 – 76Combined sources4
Turni79 – 81Combined sources3
Beta strandi82 – 84Combined sources3
Beta strandi88 – 90Combined sources3
Beta strandi96 – 98Combined sources3
Helixi99 – 103Combined sources5
Beta strandi104 – 106Combined sources3
Helixi108 – 121Combined sources14
Helixi123 – 125Combined sources3
Helixi127 – 132Combined sources6
Turni133 – 135Combined sources3
Helixi139 – 142Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Z2FX-ray1.50A19-147[»]
ProteinModelPortaliQ06283
SMRiQ06283
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06283

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
InParanoidiQ06283
KOiK13915
OMAiSYRTDVV
OrthoDBiEOG091G0R9V
TreeFamiTF324882

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.

Q06283-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKALVILGFL FLSVAVQGKV FERCELARTL KKLGLDGYKG VSLANWLCLT
60 70 80 90 100
KWESSYNTKA TNYNPSSEST DYGIFQINSK WWCNDGKTPN AVDGCHVSCS
110 120 130 140
ELMENDIAKA VACAKHIVSE QGITAWVAWK SHCRDHDVSS YVEGCTL
Length:147
Mass (Da):16,304
Last modified:January 1, 1999 - v2
Checksum:iB0A38B9ECE1E66BE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95098 Unassigned DNA Translation: AAC37311.1
PIRiC34277 LZBO
RefSeqiNP_851342.1, NM_180999.1
UniGeneiBt.29367

Genome annotation databases

EnsembliENSBTAT00000007924; ENSBTAP00000007924; ENSBTAG00000026088
GeneIDi280849
KEGGibta:280849

Similar proteinsi

Entry informationi

Entry nameiLYSC2_BOVIN
AccessioniPrimary (citable) accession number: Q06283
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 27, 2003
Last sequence update: January 1, 1999
Last modified: May 23, 2018
This is version 120 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health