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P17607

- LYSC1_SHEEP

UniProt

P17607 - LYSC1_SHEEP

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Protein

Lysozyme C-1

Gene
N/A
Organism
Ovis aries (Sheep)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript 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

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
OrganismiOvis aries (Sheep)
Taxonomic identifieri9940 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis
ProteomesiUP000002356: Unplaced

Subcellular locationi

Secreted By similarity

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 – 1818By similarityAdd
BLAST
Chaini19 – 147129Lysozyme C-1PRO_0000018488Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 145PROSITE-ProRule annotation
Disulfide bondi48 ↔ 133PROSITE-ProRule annotation
Disulfide bondi83 ↔ 99PROSITE-ProRule annotation
Disulfide bondi95 ↔ 113PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed in stomach.

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP17607.
SMRiP17607. Positions 19-147.
ModBaseiSearch...
MobiDBiSearch...

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.

P17607-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKALIILGLL CLSVAVQGKV FERCELARTL KELGLDGYKG VSLANWLCLT
60 70 80 90 100
KWESSYNTKA TNYNPGSEST DYGIFQINSK WWCNDGKTPN AVDGCHVSCS
110 120 130 140
ELMENNIAKA VACAKHIVSE QGITAWVAWK SHCRDHDVSS YVEGCSL
Length:147
Mass (Da):16,195
Last modified:January 27, 2003 - v2
Checksum:i065D72BC42B0A6E0
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321E → K in isozyme 3A and isozyme 4A/4B.
Natural varianti37 – 371G → D in isozyme 4A/4B.
Natural varianti55 – 551S → G in isozyme 3A.
Natural varianti101 – 1011E → A in isozyme 2A, isozyme 3A and isozyme 4A/4B.
Natural varianti106 – 1061N → D in isozyme 2A, isozyme 3A and isozyme 4A/4B.
Natural varianti108 – 1081A → E in isozyme 2A, isozyme 3A and isozyme 4A/4B.
Natural varianti146 – 1461S → T in isozyme 2A, isozyme 3A and isozyme 4A/4B.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF170555
, AF170552, AF170553, AF170554 Genomic DNA. Translation: AAD51636.1.
M32492 mRNA. Translation: AAA31557.1.
M32493 mRNA. Translation: AAA31558.1.
M32494 mRNA. Translation: AAA31559.1.
M32495 mRNA. Translation: AAA31560.1.
M32496 mRNA. Translation: AAA31561.1.
M32497 mRNA. Translation: AAA31562.1.
M32498 mRNA. Translation: AAA31563.1.
PIRiD35558.
E35558.
F35558.
UniGeneiOar.378.
Oar.379.
Oar.380.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF170555
, AF170552 , AF170553 , AF170554 Genomic DNA. Translation: AAD51636.1 .
M32492 mRNA. Translation: AAA31557.1 .
M32493 mRNA. Translation: AAA31558.1 .
M32494 mRNA. Translation: AAA31559.1 .
M32495 mRNA. Translation: AAA31560.1 .
M32496 mRNA. Translation: AAA31561.1 .
M32497 mRNA. Translation: AAA31562.1 .
M32498 mRNA. Translation: AAA31563.1 .
PIRi D35558.
E35558.
F35558.
UniGenei Oar.378.
Oar.379.
Oar.380.

3D structure databases

ProteinModelPortali P17607.
SMRi P17607. 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...

Phylogenomic databases

HOVERGENi HBG052297.

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. "Mosaic evolution of ruminant stomach lysozyme genes."
    Wen Y., Irwin D.M.
    Mol. Phylogenet. Evol. 13:474-482(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Concerted evolution of ruminant stomach lysozymes. Characterization of lysozyme cDNA clones from sheep and deer."
    Irwin D.M., Wilson A.C.
    J. Biol. Chem. 265:4944-4952(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-147.

Entry informationi

Entry nameiLYSC1_SHEEP
AccessioniPrimary (citable) accession number: P17607
Secondary accession number(s): Q9TUN2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 27, 2003
Last modified: October 29, 2014
This is version 86 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 sequence of isozyme 1A/1B/1C is shown.

Keywords - Technical termi

Complete proteome, 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