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P11941

- LYSC2_ONCMY

UniProt

P11941 - LYSC2_ONCMY

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Protein

Lysozyme C II

Gene
N/A
Organism
Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
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. Has antibacterial activity against the Gram positive bacterium P.citreus. Has no antibacterial activity against the Gram negative bacteria E.coli and Y.ruckeri. Does not have hemolytic activity against trout erythrocytes.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.1 Publication

pH dependencei

Optimum pH is 4.5-5.5. No activity above pH 8.8.1 Publication

Temperature dependencei

Optimum temperature is 33-49 degrees Celsius. Retains 25% of its maximal activity after heating 10 minutes at 80 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei50 – 501
Active sitei67 – 671

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
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme C II (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase C
Lysozyme type II
OrganismiOncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Taxonomic identifieri8022 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiProtacanthopterygiiSalmoniformesSalmonidaeSalmoninaeOncorhynchus

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 15152 PublicationsAdd
BLAST
Chaini16 – 144129Lysozyme C IIPRO_0000018501Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi21 ↔ 142
Disulfide bondi45 ↔ 130
Disulfide bondi79 ↔ 95
Disulfide bondi91 ↔ 109

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP11941.

Structurei

Secondary structure

1
144
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi20 – 2910Combined sources
Helixi40 – 5112Combined sources
Beta strandi58 – 603Combined sources
Beta strandi66 – 683Combined sources
Turni69 – 724Combined sources
Turni75 – 773Combined sources
Helixi95 – 984Combined sources
Beta strandi99 – 1024Combined sources
Helixi104 – 11310Combined sources
Helixi119 – 1224Combined sources
Helixi124 – 1296Combined sources
Turni130 – 1323Combined sources
Helixi136 – 1383Combined sources
Turni139 – 1413Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BB6X-ray2.00A16-144[»]
1BB7X-ray2.00A16-144[»]
1LMCX-ray2.00A16-144[»]
1LMNX-ray1.80A16-144[»]
1LMOX-ray1.80A16-144[»]
1LMPX-ray2.00A16-144[»]
1LMQX-ray1.60A16-144[»]
ProteinModelPortaliP11941.
SMRiP11941. Positions 16-144.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11941.

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG052297.

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.

P11941-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRAVVVLLLV AVASAKVYDR CELARALKAS GMDGYAGNSL PNWVCLSKWE
60 70 80 90 100
SSYNTQATNR NTDGSTDYGI FQINSRYWCD DGRTPGAKNV CGIRCSQLLT
110 120 130 140
ADLTVAIRCA KRVVLDPNGI GAWVAWRLHC QNQDLRSYVA GCGV
Length:144
Mass (Da):15,737
Last modified:April 1, 1993 - v2
Checksum:iBF945ADCDCC2D668
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941R → H in AAG34564. 1 PublicationCurated
Sequence conflicti101 – 1011A → D in AAG34564. 1 PublicationCurated

Mass spectrometryi

Molecular mass is 14252 Da from positions 16 - 144. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59491 mRNA. Translation: CAA42084.1.
AF322106 Genomic DNA. Translation: AAG45933.1.
AF452171 Genomic DNA. Translation: AAL48290.1.
AF321519 mRNA. Translation: AAG34564.1.
PIRiI51047.
RefSeqiNP_001118188.1. NM_001124716.1.
UniGeneiOmy.11916.

Genome annotation databases

GeneIDi100136768.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59491 mRNA. Translation: CAA42084.1 .
AF322106 Genomic DNA. Translation: AAG45933.1 .
AF452171 Genomic DNA. Translation: AAL48290.1 .
AF321519 mRNA. Translation: AAG34564.1 .
PIRi I51047.
RefSeqi NP_001118188.1. NM_001124716.1.
UniGenei Omy.11916.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BB6 X-ray 2.00 A 16-144 [» ]
1BB7 X-ray 2.00 A 16-144 [» ]
1LMC X-ray 2.00 A 16-144 [» ]
1LMN X-ray 1.80 A 16-144 [» ]
1LMO X-ray 1.80 A 16-144 [» ]
1LMP X-ray 2.00 A 16-144 [» ]
1LMQ X-ray 1.60 A 16-144 [» ]
ProteinModelPortali P11941.
SMRi P11941. Positions 16-144.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH22. Glycoside Hydrolase Family 22.

Proteomic databases

PRIDEi P11941.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100136768.

Organism-specific databases

CTDi 17105.

Phylogenomic databases

HOVERGENi HBG052297.

Miscellaneous databases

EvolutionaryTracei P11941.

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. "cDNA and amino acid sequences of rainbow trout (Oncorhynchus mykiss) lysozymes and their implications for the evolution of lysozyme and lactalbumin."
    Dautingny A., Prager E.M., Pham-Dinh D., Jolles J., Pakdel F., Grinde B., Jolles P.
    J. Mol. Evol. 32:187-198(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Molecular characterization of lysozyme type II gene from rainbow trout (Oncorhynchus mykiss): an evidence of a duplicate gene."
    Mitra A., Foster-Frey J., Wells K.D., Rexroad C.E. III, Wall R.J.
    Anim. Biotechnol. 14:7-12(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Kamploop.
    Tissue: Kidney.
  3. "A new genetic variant of lysozyme from rainbow trout."
    Mitra A., Wells K.D., Rexroad C.E. III, Wall R.J.
    Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  4. "Purification and characterization of two lysozymes from rainbow trout (Salmo gairdneri)."
    Grinde B., Jolles J., Jolles P.
    Eur. J. Biochem. 173:269-273(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 16-50.
  5. "Two novel muramidases from skin mucosa of rainbow trout (Oncorhynchus mykiss)."
    Fernandes J.M.O., Kemp G.D., Smith V.J.
    Comp. Biochem. Physiol. 138B:53-64(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 16-30, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY.
    Tissue: Skin mucus.
  6. "Refined crystal structure of lysozyme from the rainbow trout (Oncorhynchus mykiss)."
    Karlsen S., Eliassen B.E., Hansen L.K., Larsen R.L., Riise B.W., Smalaas A.O., Hough E., Grinde B.
    Acta Crystallogr. D 51:354-367(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
  7. "Structural studies on the binding of 4-methylumbelliferone glycosides of chitin to rainbow trout lysozyme."
    Vollan V.B., Hough E., Karlsen S.
    Acta Crystallogr. D 55:60-66(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Entry informationi

Entry nameiLYSC2_ONCMY
AccessioniPrimary (citable) accession number: P11941
Secondary accession number(s): P83333, Q9DDK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: April 1, 1993
Last modified: November 26, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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