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P00697

- LYSC1_RAT

UniProt

P00697 - LYSC1_RAT

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Protein

Lysozyme C-1

Gene

Lyz1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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. In the intestine they may also have a digestive function.

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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei53 – 531PROSITE-ProRule annotation
Active sitei71 – 711PROSITE-ProRule annotation

GO - Molecular functioni

  1. hydrolase activity, acting on glycosyl bonds Source: RGD
  2. lysozyme activity Source: RGD

GO - Biological processi

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

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase, Milk protein

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme C-1 (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase C
Gene namesi
Name:Lyz1
Synonyms:Lyz
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi3026. Lyz.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: RGD
  2. endoplasmic reticulum lumen Source: RGD
  3. extracellular region Source: UniProtKB-KW
  4. Golgi cis cisterna Source: RGD
  5. Golgi stack Source: RGD
  6. microvillus Source: RGD
  7. rough endoplasmic reticulum lumen Source: RGD
  8. secretory granule Source: RGD
  9. trans-Golgi network transport vesicle Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Chaini19 – 148130Lysozyme C-1PRO_0000018484Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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

PaxDbiP00697.
PRIDEiP00697.

PTM databases

PhosphoSiteiP00697.

Expressioni

Tissue specificityi

Expressed in lung, small intestine and spleen.

Gene expression databases

GenevestigatoriP00697.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000007747.

Structurei

3D structure databases

ProteinModelPortaliP00697.
SMRiP00697. Positions 19-148.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG85133.
HOGENOMiHOG000037357.
HOVERGENiHBG052297.
InParanoidiP00697.
PhylomeDBiP00697.

Family and domain databases

InterProiIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view]
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.

P00697-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKALLVLGFL LLSASVQAKI YERCQFARTL KRNGMSGYYG VSLADWVCLA
60 70 80 90 100
QHESNYNTQA RNYNPGDQST DYGIFQINSR YWCNDGKTPR AKNACGIPCS
110 120 130 140
ALLQDDITQA IQCAKRVVRD PQGIRAWVAW QRHCKNRDLS GYIRNCGV
Length:148
Mass (Da):16,729
Last modified:October 1, 1994 - v2
Checksum:i8E6E986539BD3EEE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201I → T AA sequence (PubMed:851497)Curated
Sequence conflicti64 – 641N → D AA sequence (PubMed:851497)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L12459 Genomic DNA. Translation: AAA41551.1.
PIRiA40729. LZRT.
UniGeneiRn.2283.

Genome annotation databases

UCSCiRGD:3026. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L12459 Genomic DNA. Translation: AAA41551.1 .
PIRi A40729. LZRT.
UniGenei Rn.2283.

3D structure databases

ProteinModelPortali P00697.
SMRi P00697. Positions 19-148.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000007747.

Chemistry

BindingDBi P00697.
ChEMBLi CHEMBL2297.

Protein family/group databases

CAZyi GH22. Glycoside Hydrolase Family 22.

PTM databases

PhosphoSitei P00697.

Proteomic databases

PaxDbi P00697.
PRIDEi P00697.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi RGD:3026. rat.

Organism-specific databases

RGDi 3026. Lyz.

Phylogenomic databases

eggNOGi NOG85133.
HOGENOMi HOG000037357.
HOVERGENi HBG052297.
InParanoidi P00697.
PhylomeDBi P00697.

Gene expression databases

Genevestigatori P00697.

Family and domain databases

InterProi IPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view ]
Pfami PF00062. Lys. 1 hit.
[Graphical view ]
PRINTSi PR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTi SM00263. LYZ1. 1 hit.
[Graphical view ]
SUPFAMi SSF53955. SSF53955. 1 hit.
PROSITEi PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Evolution of rodent lysozymes: isolation and sequence of the rat lysozyme genes."
    Yeh T.C., Wilson A.C., Irwin D.M.
    Mol. Phylogenet. Evol. 2:65-75(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Sprague-Dawley.
  2. Cited for: PROTEIN SEQUENCE OF 19-148.
    Strain: Wistar.

Entry informationi

Entry nameiLYSC1_RAT
AccessioniPrimary (citable) accession number: P00697
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1994
Last modified: October 29, 2014
This is version 115 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.
Rat has two lysozymes, type 1 and type 2 of which only type 1 is expressed; type 2 being probably a pseudogene.

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

External Data

Dasty 3