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P12069

- LYSC3_PIG

UniProt

P12069 - LYSC3_PIG

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Protein

Lysozyme C-3

Gene
N/A
Organism
Sus scrofa (Pig)
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

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme C-3 (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase C
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

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 – 18181 PublicationAdd
BLAST
Chaini19 – 148130Lysozyme C-3PRO_0000018480Add
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

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP12069.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000037357.
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.

P12069-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKTLLVLALL LLSVSVQAKV YDRCEFARIL KKSGMDGYRG VSLANWVCLA
60 70 80 90 100
KWESNFNTKA TNYNPGSQST DYGIFQINSR YWCNDGKTPK AVNACHISCK
110 120 130 140
VLLDDDLSQD IECAKRVVRD PQGIKAWVAW KAHCQNKDVS QYIRGCKL
Length:148
Mass (Da):16,711
Last modified:November 1, 1997 - v2
Checksum:i76AA67BFABBD64E6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U44435 mRNA. Translation: AAA86644.1.
PIRiS10047.
UniGeneiSsc.670.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U44435 mRNA. Translation: AAA86644.1 .
PIRi S10047.
UniGenei Ssc.670.

3D structure databases

ProteinModelPortali P12069.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOGENOMi HOG000037357.
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. Echetebu Z.O., Nevils M., Bixby J.A., Roberts R.M., Trout W.E.
    Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: PROTEIN SEQUENCE OF 19-148.
    Tissue: Stomach.

Entry informationi

Entry nameiLYSC3_PIG
AccessioniPrimary (citable) accession number: P12069
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 1, 1997
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.

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