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Q06283

- LYSC2_BOVIN

UniProt

Q06283 - LYSC2_BOVIN

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Protein

Lysozyme C-2

Gene

LYZ2

Organism
Bos taurus (Bovine)
Status
Reviewed - 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.

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. lysozyme activity Source: UniProtKB-EC

GO - Biological processi

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

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Keywords - Biological processi

Digestion

Enzyme and pathway databases

ReactomeiREACT_206540. 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
Gene namesi
Name:LYZ2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 5

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818By similarityAdd
BLAST
Chaini19 – 147129Lysozyme C-2PRO_0000018455Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 1451 PublicationPROSITE-ProRule annotation
Disulfide bondi48 ↔ 1331 PublicationPROSITE-ProRule annotation
Disulfide bondi83 ↔ 991 PublicationPROSITE-ProRule annotation
Disulfide bondi95 ↔ 1131 PublicationPROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Stomach-specific.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
147
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi23 – 3210Combined sources
Helixi43 – 5412Combined sources
Beta strandi61 – 644Combined sources
Turni65 – 684Combined sources
Beta strandi69 – 724Combined sources
Turni73 – 764Combined sources
Turni79 – 813Combined sources
Beta strandi82 – 843Combined sources
Beta strandi88 – 903Combined sources
Beta strandi96 – 983Combined sources
Helixi99 – 1035Combined sources
Beta strandi104 – 1063Combined sources
Helixi108 – 12114Combined sources
Helixi123 – 1253Combined sources
Helixi127 – 1326Combined sources
Turni133 – 1353Combined sources
Helixi139 – 1424Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Z2FX-ray1.50A19-147[»]
ProteinModelPortaliQ06283.
SMRiQ06283. Positions 19-147.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06283.

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG85133.
GeneTreeiENSGT00550000074398.
HOGENOMiHOG000037357.
HOVERGENiHBG052297.
InParanoidiQ06283.
KOiK13915.
OMAiSCELART.
OrthoDBiEOG7BW0M5.
TreeFamiTF324882.

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.

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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95098 Unassigned DNA. Translation: AAC37311.1 .
PIRi C34277. LZBO.
RefSeqi NP_851342.1. NM_180999.1.
UniGenei Bt.29367.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2Z2F X-ray 1.50 A 19-147 [» ]
ProteinModelPortali Q06283.
SMRi Q06283. Positions 19-147.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000007924 ; ENSBTAP00000007924 ; ENSBTAG00000026088 .
GeneIDi 280849.
KEGGi bta:280849.

Organism-specific databases

CTDi 17105.

Phylogenomic databases

eggNOGi NOG85133.
GeneTreei ENSGT00550000074398.
HOGENOMi HOG000037357.
HOVERGENi HBG052297.
InParanoidi Q06283.
KOi K13915.
OMAi SCELART.
OrthoDBi EOG7BW0M5.
TreeFami TF324882.

Enzyme and pathway databases

Reactomei REACT_206540. Amyloids.

Miscellaneous databases

EvolutionaryTracei Q06283.
NextBioi 20804997.

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. "Characterization of the cow stomach lysozyme genes: repetitive DNA and concerted evolution."
    Irwin D.M., White R.T., Wilson A.C.
    J. Mol. Evol. 37:355-366(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "X-ray crystallography and structural stability of digestive lysozyme from cow stomach."
    Nonaka Y., Akieda D., Aizawa T., Watanabe N., Kamiya M., Kumaki Y., Mizuguchi M., Kikukawa T., Demura M., Kawano K.
    FEBS J. 276:2192-2200(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 19-147, DISULFIDE BONDS.

Entry informationi

Entry nameiLYSC2_BOVIN
AccessioniPrimary (citable) accession number: Q06283
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 27, 2003
Last sequence update: January 1, 1999
Last modified: November 26, 2014
This is version 96 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.
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.

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

External Data

Dasty 3