Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P83971 (LYSA_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysozyme A/C

EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase A/C
Gene names
Name:LysA
AND
Name:LysC
ORF Names:CG9111
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length140 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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. Ref.1

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. Ref.1

Developmental stage

Maximal expression is found during the third larval instar, it drops to become undetectable in the late pupal stage. The expression in adults is similar to that of first and second larval instars. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 22 family.

Caution

Strain sequenced by genome project has a known mutation in LysC.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 By similarity
Chain19 – 140122Lysozyme A/C
PRO_0000018511

Sites

Active site501 By similarity
Active site681 By similarity

Amino acid modifications

Disulfide bond24 ↔ 139 By similarity
Disulfide bond45 ↔ 129 By similarity
Disulfide bond80 ↔ 96 By similarity
Disulfide bond92 ↔ 110 By similarity

Sequences

Sequence LengthMass (Da)Tools
P83971 [UniParc].

Last modified June 7, 2004. Version 1.
Checksum: CB1F99FBDE8694B5

FASTA14015,651
        10         20         30         40         50         60 
MKAFIVLVAL ACAAPAFGRT MDRCSLAREM SNLGVPRDQL NKWACIAEHE SSYRTGVVGP 

        70         80         90        100        110        120 
ENYNGSNDYG IFQINDYYWC APPSGRFSYN ECGLSCNALL TDDITHSVRC AQKVLSQQGW 

       130        140 
SAWSTWHYCS GWLPSIDDCF 

« Hide

References

« Hide 'large scale' references
[1]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (LYSA AND LYSC), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: Canton-S.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (LYSC).
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] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z22223 mRNA. Translation: CAA80225.1.
Z22226 Genomic DNA. Translation: CAA80228.1.
AE014296 Genomic DNA. Translation: AAF47449.2.
PIRS41573.
RefSeqNP_524869.1. NM_080130.3.
UniGeneDm.12727.
Dm.33497.

3D structure databases

ProteinModelPortalP83971.
SMRP83971. Positions 19-140.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-1560162.

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Proteomic databases

PaxDbP83971.
PRIDEP83971.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0072629; FBpp0072525; FBgn0004426.
GeneID38126.
KEGGdme:Dmel_CG9111.

Organism-specific databases

CTD38126.
FlyBaseFBgn0011201. LysA.
FBgn0004426. LysC.

Phylogenomic databases

eggNOGNOG85133.
GeneTreeENSGT00550000074398.
InParanoidP83971.
KOK01185.
OMAYVKGCGV.
OrthoDBEOG7BW0M5.
PhylomeDBP83971.

Gene expression databases

BgeeP83971.

Family and domain databases

InterProIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamPF00062. Lys. 1 hit.
[Graphical view]
PRINTSPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMSSF53955. SSF53955. 1 hit.
PROSITEPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi38126.
NextBio807095.

Entry information

Entry nameLYSA_DROME
AccessionPrimary (citable) accession number: P83971
Secondary accession number(s): P29614 expand/collapse secondary AC list , P37157, Q9W0J6, Q9W0J7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: November 13, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Drosophila

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