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P05105

- LYS_HYACE

UniProt

P05105 - LYS_HYACE

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Protein
Lysozyme
Gene
N/A
Organism
Hyalophora cecropia (Cecropia moth)
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 sitei51 – 511 By similarity
Active sitei69 – 691 By similarity

GO - Molecular functioni

  1. lysozyme activity Source: UniProtKB-EC
Complete GO annotation...

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

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase
OrganismiHyalophora cecropia (Cecropia moth)
Taxonomic identifieri7123 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaBombycoideaSaturniidaeSaturniinaeAttaciniHyalophora

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919 By similarity
Add
BLAST
Chaini20 – 139120Lysozyme
PRO_0000018506Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi25 ↔ 139 By similarity
Disulfide bondi46 ↔ 129 By similarity
Disulfide bondi81 ↔ 95 By similarity
Disulfide bondi91 ↔ 109 By similarity

Keywords - PTMi

Disulfide bond

Structurei

3D structure databases

ProteinModelPortaliP05105.
SMRiP05105. Positions 20-139.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

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.

P05105-1 [UniParc]FASTAAdd to Basket

« Hide

MTKYVILLAV LAFALHCDAK RFTRCGLVQE LRRLGFDETL MSNWVCLVEN    50
ESGRFTDKIG KVNKNGSRDY GLFQINDKYW CSKGTTPGKD CNVTCNQLLT 100
DDISVAATCA KKIYKRHKFD AWYGWKNHCQ HGLPDISDC 139
Length:139
Mass (Da):15,877
Last modified:May 1, 1992 - v2
Checksum:iE8AF5C2CE561F641
GO

Sequence cautioni

The sequence AAA29190.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAA26542.1 differs from that shown. Reason: Erroneous initiation.

Polymorphismi

3 allelic variants of cecropia moth lysozyme have been found. The sequence shown is that of lysozyme 1.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti34 – 341L → R in lysozyme-2.
Natural varianti85 – 851T → S in lysozyme-2 and lysozyme-3.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M60914 Genomic DNA. Translation: AAA29189.1.
X02765 mRNA. Translation: CAA26542.1. Different initiation.
M34923 mRNA. Translation: AAA29190.1. Different initiation.
PIRiA24649. LZWK.
A38744.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M60914 Genomic DNA. Translation: AAA29189.1 .
X02765 mRNA. Translation: CAA26542.1 . Different initiation.
M34923 mRNA. Translation: AAA29190.1 . Different initiation.
PIRi A24649. LZWK.
A38744.

3D structure databases

ProteinModelPortali P05105.
SMRi P05105. Positions 20-139.
ModBasei Search...

Protein family/group databases

CAZyi GH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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. "Organization and expression of the immunoresponsive lysozyme gene in the giant silk moth, Hyalophora cecropia."
    Sun S.-C., Aasling B., Faye I.
    J. Biol. Chem. 266:6644-6649(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Amino acid and cDNA sequences of lysozyme from Hyalophora cecropia."
    Engstroem A., Xanthopoulos K.G., Boman H.G., Bennich H.
    EMBO J. 4:2119-2122(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 13-139.
  3. "On the primary structures of lysozyme, cecropins and attacins from Hyalophora cecropia."
    Boman H.G., Faye I., von Hofsten P., Kockum K., Lee J.-Y., Xanthopoulos K.G., Bennich H., Engstroem A., Merrifield R.B., Andreu D.
    Dev. Comp. Immunol. 9:551-558(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 13-139.

Entry informationi

Entry nameiLYS_HYACE
AccessioniPrimary (citable) accession number: P05105
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: May 1, 1992
Last modified: October 16, 2013
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

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

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