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
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 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. Lyz2 is active against a range of Gram-positive and Gram-negative bacteria. More effective than Lyz1 in killing Gram-negative bacteria. Lyz1 and Lyz2 are equally effective in killing Gram-positive bacteria.1 PublicationPROSITE-ProRule annotation

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.

pH dependencei

Optimum pH is 5.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei53 – 531PROSITE-ProRule annotation
Active sitei71 – 711PROSITE-ProRule annotation

GO - Molecular functioni

  1. identical protein binding Source: MGI
  2. lysozyme activity Source: UniProtKB

GO - Biological processi

  1. cell wall macromolecule catabolic process Source: InterPro
  2. cytolysis Source: UniProtKB-KW
  3. defense response to bacterium Source: UniProtKB
  4. defense response to Gram-negative bacterium Source: UniProtKB
  5. defense response to Gram-positive bacterium Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase, Milk protein

Enzyme and pathway databases

ReactomeiREACT_198563. Amyloids.

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
Lysozyme C type M
Gene namesi
Name:Lyz2
Synonyms:Lyz, Lyzs
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:96897. Lyz2.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: MGI
  2. extracellular vesicular exosome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Disruption phenotypei

Mice display increased inflammation in response to M.luteus infection, impaired digestion of M.luteus cell walls, decreased clearance of P.aeruginosa from infected airways, increased susceptibility to K.pneumoniae infection and increased bacterial burden and mortality following infection with various Gram-negative bacteria. Lyz2 is non-immunogenic in wild-type mice but is rendered immunogenic in mutants.5 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Chaini19 – 148130Lysozyme C-2PRO_0000018472Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 1461 PublicationPROSITE-ProRule annotation
Disulfide bondi48 ↔ 1341 PublicationPROSITE-ProRule annotation
Disulfide bondi83 ↔ 991 PublicationPROSITE-ProRule annotation
Disulfide bondi95 ↔ 1131 PublicationPROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP08905.
PaxDbiP08905.
PRIDEiP08905.

Expressioni

Tissue specificityi

Expressed weakly in myeloblasts, moderately in immature macrophages, and strongly in both mature macrophages and macrophage-rich tissues.

Gene expression databases

BgeeiP08905.
CleanExiMM_LYZ2.
GenevestigatoriP08905.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

IntActiP08905. 4 interactions.
MINTiMINT-4100851.

Structurei

Secondary structure

1
148
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi23 – 3311Combined sources
Beta strandi39 – 413Combined sources
Helixi43 – 5311Combined sources
Beta strandi56 – 583Combined sources
Beta strandi61 – 644Combined sources
Helixi65 – 673Combined sources
Beta strandi69 – 724Combined sources
Turni73 – 764Combined sources
Turni79 – 813Combined sources
Beta strandi82 – 843Combined sources
Helixi99 – 1024Combined sources
Beta strandi103 – 1053Combined sources
Helixi108 – 11811Combined sources
Beta strandi120 – 1223Combined sources
Helixi124 – 1263Combined sources
Helixi128 – 1314Combined sources
Turni132 – 1365Combined sources
Helixi140 – 1434Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IVMNMR-A19-148[»]
ProteinModelPortaliP08905.
SMRiP08905. Positions 19-148.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08905.

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG85133.
GeneTreeiENSGT00550000074398.
HOGENOMiHOG000037357.
HOVERGENiHBG052297.
InParanoidiP08905.
KOiK13915.
OMAiNHCFRRR.
OrthoDBiEOG7BW0M5.
PhylomeDBiP08905.
TreeFamiTF324882.

Family and domain databases

InterProiIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
IPR030056. Lysozyme_C.
[Graphical view]
PANTHERiPTHR11407:SF22. PTHR11407:SF22. 1 hit.
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.

P08905-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKTLLTLGLL LLSVTAQAKV YERCEFARTL KRNGMAGYYG VSLADWVCLA
60 70 80 90 100
QHESNYNTRA TNYNRGDQST DYGIFQINSR YWCNDGKTPR AVNACGINCS
110 120 130 140
ALLQDDITAA IQCAKRVVRD PQGIRAWVAW RAHCQNRDLS QYIRNCGV
Length:148
Mass (Da):16,689
Last modified:November 1, 1990 - v2
Checksum:i5C768DDCD8071BAF
GO

Sequence cautioni

The sequence BAE30022.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE31835.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE34954.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21050
, M21047, M21048, M21049 Genomic DNA. Translation: AAA39473.1.
AK148516 mRNA. Translation: BAE28595.1.
AK150998 mRNA. Translation: BAE30022.1. Different initiation.
AK153244 mRNA. Translation: BAE31835.1. Different initiation.
AK153475 mRNA. Translation: BAE32025.1.
AK159276 mRNA. Translation: BAE34954.1. Different initiation.
AK159640 mRNA. Translation: BAE35253.1.
BC002069 mRNA. Translation: AAH02069.1.
BC019611 mRNA. Translation: AAH19611.1.
BC054463 mRNA. Translation: AAH54463.1.
CCDSiCCDS48694.1.
PIRiA31239.
RefSeqiNP_059068.1. NM_017372.3.
UniGeneiMm.45436.

Genome annotation databases

EnsembliENSMUST00000092163; ENSMUSP00000089801; ENSMUSG00000069516.
GeneIDi17105.
KEGGimmu:17105.
UCSCiuc007hda.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21050
, M21047, M21048, M21049 Genomic DNA. Translation: AAA39473.1.
AK148516 mRNA. Translation: BAE28595.1.
AK150998 mRNA. Translation: BAE30022.1. Different initiation.
AK153244 mRNA. Translation: BAE31835.1. Different initiation.
AK153475 mRNA. Translation: BAE32025.1.
AK159276 mRNA. Translation: BAE34954.1. Different initiation.
AK159640 mRNA. Translation: BAE35253.1.
BC002069 mRNA. Translation: AAH02069.1.
BC019611 mRNA. Translation: AAH19611.1.
BC054463 mRNA. Translation: AAH54463.1.
CCDSiCCDS48694.1.
PIRiA31239.
RefSeqiNP_059068.1. NM_017372.3.
UniGeneiMm.45436.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IVMNMR-A19-148[»]
ProteinModelPortaliP08905.
SMRiP08905. Positions 19-148.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP08905. 4 interactions.
MINTiMINT-4100851.

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Proteomic databases

MaxQBiP08905.
PaxDbiP08905.
PRIDEiP08905.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000092163; ENSMUSP00000089801; ENSMUSG00000069516.
GeneIDi17105.
KEGGimmu:17105.
UCSCiuc007hda.1. mouse.

Organism-specific databases

CTDi17105.
MGIiMGI:96897. Lyz2.

Phylogenomic databases

eggNOGiNOG85133.
GeneTreeiENSGT00550000074398.
HOGENOMiHOG000037357.
HOVERGENiHBG052297.
InParanoidiP08905.
KOiK13915.
OMAiNHCFRRR.
OrthoDBiEOG7BW0M5.
PhylomeDBiP08905.
TreeFamiTF324882.

Enzyme and pathway databases

ReactomeiREACT_198563. Amyloids.

Miscellaneous databases

EvolutionaryTraceiP08905.
NextBioi291248.
PROiP08905.
SOURCEiSearch...

Gene expression databases

BgeeiP08905.
CleanExiMM_LYZ2.
GenevestigatoriP08905.

Family and domain databases

InterProiIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
IPR030056. Lysozyme_C.
[Graphical view]
PANTHERiPTHR11407:SF22. PTHR11407:SF22. 1 hit.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse lysozyme M gene: isolation, characterization, and expression studies."
    Cross M., Mangelsdorf I., Wedel A., Renkawitz R.
    Proc. Natl. Acad. Sci. U.S.A. 85:6232-6236(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow macrophage and Pancreatic islet.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N and FVB/N-3.
    Tissue: Mammary tumor.
  4. "Sequence studies of mouse lysozyme."
    Riblet R.J.
    (In) Osserman E.F., Canfield R.E., Beychok S. (eds.); Lysozyme, pp.89-93, Academic Press, New York (1974)
    Cited for: PROTEIN SEQUENCE OF 19-78.
  5. "Increased inflammation in lysozyme M-deficient mice in response to Micrococcus luteus and its peptidoglycan."
    Ganz T., Gabayan V., Liao H.-I., Liu L., Oren A., Graf T., Cole A.M.
    Blood 101:2388-2392(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  6. "Mouse lysozyme M is important in pulmonary host defense against Klebsiella pneumoniae infection."
    Markart P., Korfhagen T.R., Weaver T.E., Akinbi H.T.
    Am. J. Respir. Crit. Care Med. 169:454-458(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  7. "Comparison of the microbicidal and muramidase activities of mouse lysozyme M and P."
    Markart P., Faust N., Graf T., Na C.-L., Weaver T.E., Akinbi H.T.
    Biochem. J. 380:385-392(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  8. "Mouse lysozyme-M knockout mice reveal how the self-determinant hierarchy shapes the T cell repertoire against this circulating self antigen in wild-type mice."
    Sinha P., Chi H.H., Kim H.R., Clausen B.E., Pederson B., Sercarz E.E., Forster I., Moudgil K.D.
    J. Immunol. 173:1763-1771(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  9. "Decreased clearance of Pseudomonas aeruginosa from airways of mice deficient in lysozyme M."
    Cole A.M., Thapa D.R., Gabayan V., Liao H.-I., Liu L., Ganz T.
    J. Leukoc. Biol. 78:1081-1085(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  10. "Solution structure and activity of mouse lysozyme M."
    Obita T., Ueda T., Imoto T.
    Cell. Mol. Life Sci. 60:176-184(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 19-148, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISULFIDE BONDS.

Entry informationi

Entry nameiLYZ2_MOUSE
AccessioniPrimary (citable) accession number: P08905
Secondary accession number(s): Q3TXG2
, Q3U5Q2, Q3U690, Q8VE78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1990
Last modified: February 4, 2015
This is version 140 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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.