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Reviewed, UniProtKB/Swiss-Prot P37161 (LYSX_DROME)

Last modified June 16, 2009. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Lysozyme X
    EC=3.2.1.17
Alternative name(s):
    1,4-beta-N-acetylmuramidase X
Gene names
Name: LysX
ORF Names: CG9120
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

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Protein attributes

Sequence length142 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Unlikely to play an active role in the humoral immune defense. May have a function in the digestion of bacteria in the food. May be involved in the clearance of bacteria from the larval gut before metamorphosis.

Catalytic activity

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.

Tissue specificity

Found in the midgut.

Developmental stage

Rises dramatically in the late third instar, then decreases gradually during the pupal stages. Low expression is found in adults.

Sequence similarities

Belongs to the glycosyl hydrolase 22 family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 142123Lysozyme X
PRO_0000018516

Sites

Active site511 By similarity
Active site691 By similarity

Amino acid modifications

Disulfide bond25 ↔ 140 By similarity
Disulfide bond46 ↔ 130 By similarity
Disulfide bond81 ↔ 97 By similarity
Disulfide bond93 ↔ 111 By similarity

Natural variations

Natural variant61G → T in strain: G140. Ref.1
Natural variant781M → L in strain: Canton-S, G02, G130 and G140. Ref.1
Natural variant941D → G in strain: G130 and G140. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P37161-1 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 2A48035364B995BC

FASTA14215,591
        10         20         30         40         50         60 
MRALLGICVL ALVTPAVLGR TMDRCSLARE MANMGVSRDQ LSKWACIAEH ESSYRTGVVG 

        70         80         90        100        110        120 
PPNTDGSNDY GIFQINDMYW CQPSSGKFSH NGCDVSCNAL LTDDIKSSVR CALKVLGQQG 

       130        140 
WSAWSTWHYC SGYLPPIDDC FV

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References

« Hide 'large scale' references
[1]"A screen for immunity genes evolving under positive selection in Drosophila."
Jiggins F.M., Kim K.W.
J. Evol. Biol. 20:965-970(2007) [PubMed: 17465907] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-6; LEU-78 AND GLY-94.
Strain: G02, G130, G140 and G28.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Larva and Pupae.
[5]"The lysozyme locus in Drosophila melanogaster: an expanded gene family adapted for expression in the digestive tract."
Daffre S., Kylsten P., Samakovlis C., Hultmark D.
Mol. Gen. Genet. 242:152-162(1994) [PubMed: 8159165] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 62-142.
Strain: Canton-S.

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Cross-references

Sequence databases

AM412869 Genomic DNA. Translation: CAL85492.1.
AM412870 Genomic DNA. Translation: CAL85493.1.
AM412871 Genomic DNA. Translation: CAL85494.1.
AM412872 Genomic DNA. Translation: CAL85495.1.
AE014296 Genomic DNA. Translation: AAF47445.1.
AY119081 mRNA. Translation: AAM50941.1.
Z22224 mRNA. Translation: CAA80226.1.
PIRS41580.
RefSeqNP_523881.1.
UniGeneDm.19201

3D structure databases

HSSPHSSP built from PDB template 1AT5 based on UniProtKB P00698.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:24095N.
IntActP37161. 1 interaction.

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Genome annotation databases

EnsemblFBgn0004431. Drosophila melanogaster. [Contig view]
GeneID38122.
KEGGdme:Dmel_CG9120.
NMPDRfig|7227.3.peg.7483.

Organism-specific databases

FlyBaseFBgn0004431. LysX.

Phylogenomic databases

HOGENOMP37161.
OMAP37161. KHCQNKD.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-014573-MON.
BRENDA3.2.1.17. 48.

Gene expression databases

ArrayExpressP37161.
GermOnlineCG9120. Drosophila melanogaster.

Family and domain databases

InterProIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
[Graphical view]
PfamPF00062. Lys. 1 hit.
[Graphical view]
PRINTSPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTSM00263. LYZ1. 1 hit.
[Graphical view]
PROSITEPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio807080.

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Entry information

Entry nameLYSX_DROME
AccessionPrimary (citable) accession number: P37161
Secondary accession number(s): A4V9W9 expand/collapse secondary AC list , A4V9X0, A4V9X1, A4V9X2, Q9W0K1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: December 1, 2000
Last modified: June 16, 2009
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

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Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents