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Q17005 (LYSC1_ANOGA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 c-1

EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase
Gene names
ORF Names:AGAP007347
OrganismAnopheles gambiae (African malaria mosquito) [Reference proteome]
Taxonomic identifier7165 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeAnophelinaeAnopheles

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

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. Ref.2

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

Expressed in salivary glands and Malpighian tubules. Ref.2

Developmental stage

Expressed at all developmental stages, highest expression is in the adult. Ref.2

Induction

By bacterial infection, expression significantly increases 6-12 hours post challenge with bacteria. Ref.2

Sequence similarities

Belongs to the glycosyl hydrolase 22 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 140120Lysozyme c-1
PRO_0000018504

Sites

Active site521 By similarity
Active site691 By similarity

Amino acid modifications

Disulfide bond26 ↔ 139 By similarity
Disulfide bond47 ↔ 128 By similarity
Disulfide bond81 ↔ 94 By similarity
Disulfide bond90 ↔ 108 By similarity

Experimental info

Sequence conflict51S → F in AAC47326. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q17005 [UniParc].

Last modified May 16, 2006. Version 2.
Checksum: D30D604699316D24

FASTA14015,338
        10         20         30         40         50         60 
MKVFSTVLLA IVACCAVAEA KTFGKCELAK ALANNGIAKA SLPDWVCLVQ NESAFSTSAT 

        70         80         90        100        110        120 
NKNKNGSTDY GIFQINNKYW CDSGYGSNDC KIACKNLLND DITDDIKCAK LIHKRHGFNA 

       130        140 
WYGWKNHCNG KKLPNVSSCF 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of a lysozyme gene from the malaria vector mosquito, Anopheles gambiae."
Kang D., Romans P., Lee J.Y.
Gene 174:239-244(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Characterization of the c-type lysozyme gene family in Anopheles gambiae."
Li B., Calvo E., Marinotti O., James A.A., Paskewitz S.M.
Gene 360:131-139(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
Strain: Pinkeye.
[3]"The genome sequence of the malaria mosquito Anopheles gambiae."
Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R., Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R., Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z., Kraft C.L., Abril J.F. expand/collapse author list , Anthouard V., Arensburger P., Atkinson P.W., Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C., Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K., Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V., Dana A., Delcher A., Dew I., Evans C.A., Flanigan M., Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R., Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J., Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I., Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A., McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D., O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H., Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B., Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I., Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J., Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M., Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C., Collins F.H., Hoffman S.L.
Science 298:129-149(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PEST.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U28809 Genomic DNA. Translation: AAC47326.1.
DQ007317 mRNA. Translation: AAY24699.1.
AAAB01008807 Genomic DNA. Translation: EAA45417.1.
PIRJC5003.

3D structure databases

ProteinModelPortalQ17005.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7165.AGAP007347-PA.

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaAGAP007347-RA; AGAP007347-PA; AGAP007347.
KEGGaga:AgaP_AGAP007347.
VectorBaseAGAP007347. Anopheles gambiae.

Organism-specific databases

CTD1269831.

Phylogenomic databases

eggNOGNOG85133.
HOGENOMHOG000037357.
InParanoidQ4ZIL2.
KOK13915.
OMAWQRYCRN.
OrthoDBEOG7BW0M5.
PhylomeDBQ17005.

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...

Entry information

Entry nameLYSC1_ANOGA
AccessionPrimary (citable) accession number: Q17005
Secondary accession number(s): Q4ZIL2, Q7PF88
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 16, 2006
Last modified: April 16, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries