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Protein

Lysozyme c-1

Gene

AGAP007347

Organism
Anopheles gambiae (African malaria mosquito)
Status
Reviewed-Annotation score: Annotation score: 3 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.PROSITE-ProRule annotation1 Publication

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 sitei52 – 521PROSITE-ProRule annotation
Active sitei69 – 691PROSITE-ProRule annotation

GO - Molecular functioni

  1. lysozyme activity Source: UniProtKB-EC

GO - Biological processi

  1. cytolysis Source: UniProtKB-KW
  2. defense response to bacterium Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.17. 358.

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme c-1 (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase
Gene namesi
ORF Names:AGAP007347
OrganismiAnopheles gambiae (African malaria mosquito)
Taxonomic identifieri7165 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeAnophelinaeAnopheles
ProteomesiUP000007062 Componenti: Chromosome 2L

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 140120Lysozyme c-1PRO_0000018504Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 139PROSITE-ProRule annotation
Disulfide bondi47 ↔ 128PROSITE-ProRule annotation
Disulfide bondi81 ↔ 94PROSITE-ProRule annotation
Disulfide bondi90 ↔ 108PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed in salivary glands and Malpighian tubules.1 Publication

Developmental stagei

Expressed at all developmental stages, highest expression is in the adult.1 Publication

Inductioni

By bacterial infection, expression significantly increases 6-12 hours post challenge with bacteria.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi7165.AGAP007347-PA.

Structurei

3D structure databases

ProteinModelPortaliQ17005.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG85133.
HOGENOMiHOG000037357.
InParanoidiQ17005.
KOiK13915.
OMAiCFRRKHR.
OrthoDBiEOG7BW0M5.
PhylomeDBiQ17005.

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.

Q17005-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVFSTVLLA IVACCAVAEA KTFGKCELAK ALANNGIAKA SLPDWVCLVQ
60 70 80 90 100
NESAFSTSAT NKNKNGSTDY GIFQINNKYW CDSGYGSNDC KIACKNLLND
110 120 130 140
DITDDIKCAK LIHKRHGFNA WYGWKNHCNG KKLPNVSSCF
Length:140
Mass (Da):15,338
Last modified:May 16, 2006 - v2
Checksum:iD30D604699316D24
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51S → F in AAC47326 (PubMed:8890741).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28809 Genomic DNA. Translation: AAC47326.1.
DQ007317 mRNA. Translation: AAY24699.1.
AAAB01008807 Genomic DNA. Translation: EAA45417.1.
PIRiJC5003.
RefSeqiXP_308481.1. XM_308481.3.

Genome annotation databases

EnsemblMetazoaiAGAP007347-RA; AGAP007347-PA; AGAP007347.
GeneIDi1269831.
KEGGiaga:AgaP_AGAP007347.
VectorBaseiAGAP007347. Anopheles gambiae.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28809 Genomic DNA. Translation: AAC47326.1.
DQ007317 mRNA. Translation: AAY24699.1.
AAAB01008807 Genomic DNA. Translation: EAA45417.1.
PIRiJC5003.
RefSeqiXP_308481.1. XM_308481.3.

3D structure databases

ProteinModelPortaliQ17005.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7165.AGAP007347-PA.

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiAGAP007347-RA; AGAP007347-PA; AGAP007347.
GeneIDi1269831.
KEGGiaga:AgaP_AGAP007347.
VectorBaseiAGAP007347. Anopheles gambiae.

Organism-specific databases

CTDi1269831.

Phylogenomic databases

eggNOGiNOG85133.
HOGENOMiHOG000037357.
InParanoidiQ17005.
KOiK13915.
OMAiCFRRKHR.
OrthoDBiEOG7BW0M5.
PhylomeDBiQ17005.

Enzyme and pathway databases

BRENDAi3.2.1.17. 358.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiLYSC1_ANOGA
AccessioniPrimary (citable) accession number: Q17005
Secondary accession number(s): Q4ZIL2, Q7PF88
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 16, 2006
Last modified: April 1, 2015
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.