ID   LYSC1_ANOGA             Reviewed;         140 AA.
AC   Q17005; Q4ZIL2; Q7PF88;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   02-SEP-2026, entry version 148.
DE   RecName: Full=Lysozyme c-1;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase;
DE   Flags: Precursor;
GN   ORFNames=AGAP007347;
OS   Anopheles gambiae (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8890741; DOI=10.1016/0378-1119(96)00088-1;
RA   Kang D., Romans P., Lee J.Y.;
RT   "Analysis of a lysozyme gene from the malaria vector mosquito, Anopheles
RT   gambiae.";
RL   Gene 174:239-244(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP   STAGE, AND INDUCTION.
RC   STRAIN=Pinkeye;
RX   PubMed=16137842; DOI=10.1016/j.gene.2005.07.001;
RA   Li B., Calvo E., Marinotti O., James A.A., Paskewitz S.M.;
RT   "Characterization of the c-type lysozyme gene family in Anopheles
RT   gambiae.";
RL   Gene 360:131-139(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEST;
RX   PubMed=12364791; DOI=10.1126/science.1076181;
RA   Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA   Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA   Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA   Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA   Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA   Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA   Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA   Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA   Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA   Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA   Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA   Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA   McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA   O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA   Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA   Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA   Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA   Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA   Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA   Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA   Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA   Collins F.H., Hoffman S.L.;
RT   "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL   Science 298:129-149(2002).
CC   -!- FUNCTION: Lysozymes have primarily a bacteriolytic function; those in
CC       tissues and body fluids are associated with the monocyte-macrophage
CC       system and enhance the activity of immunoagents. {ECO:0000255|PROSITE-
CC       ProRule:PRU00680, ECO:0000269|PubMed:16137842}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC         acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC         between N-acetyl-D-glucosamine residues in chitodextrins.;
CC         EC=3.2.1.17;
CC   -!- TISSUE SPECIFICITY: Expressed in salivary glands and Malpighian
CC       tubules. {ECO:0000269|PubMed:16137842}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at all developmental stages, highest
CC       expression is in the adult. {ECO:0000269|PubMed:16137842}.
CC   -!- INDUCTION: By bacterial infection, expression significantly increases
CC       6-12 hours post challenge with bacteria. {ECO:0000269|PubMed:16137842}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR   EMBL; U28809; AAC47326.1; -; Genomic_DNA.
DR   EMBL; DQ007317; AAY24699.1; -; mRNA.
DR   EMBL; AAAB01008807; EAA45417.1; -; Genomic_DNA.
DR   PIR; JC5003; JC5003.
DR   AlphaFoldDB; Q17005; -.
DR   SMR; Q17005; -.
DR   FunCoup; Q17005; 11.
DR   STRING; 7165.Q17005; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   PaxDb; 7165-Q17005; -.
DR   EnsemblMetazoa; AGAMI1_013470.R27993; AGAMI1_013470.P27993; AGAMI1_013470.
DR   EnsemblMetazoa; AGAP007347-RA; AGAP007347-PA; AGAP007347.
DR   GeneID; 1269831; -.
DR   KEGG; aga:1269831; -.
DR   VEuPathDB; VectorBase:AGAMI1_013470; -.
DR   VEuPathDB; VectorBase:AGAP007347; -.
DR   eggNOG; ENOG502S4CB; Eukaryota.
DR   HOGENOM; CLU_111620_0_1_1; -.
DR   InParanoid; Q17005; -.
DR   OMA; YWCSNTS; -.
DR   PhylomeDB; Q17005; -.
DR   BRENDA; 3.2.1.17; 358.
DR   Proteomes; UP000007062; Chromosome 2L.
DR   GO; GO:0003796; F:lysozyme activity; IBA:GO_Central.
DR   CDD; cd16899; LYZ_C_invert; 1.
DR   FunFam; 1.10.530.10:FF:000024; C-type lysozyme; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   InterPro; IPR001916; Glyco_hydro_22.
DR   InterPro; IPR019799; Glyco_hydro_22_CS.
DR   InterPro; IPR000974; Glyco_hydro_22_lys.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   PANTHER; PTHR11407:SF36; GEO02684P1-RELATED; 1.
DR   PANTHER; PTHR11407; LYSOZYME C; 1.
DR   Pfam; PF00062; Lys; 1.
DR   PRINTS; PR00137; LYSOZYME.
DR   PRINTS; PR00135; LYZLACT.
DR   SMART; SM00263; LYZ1; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS00128; GLYCOSYL_HYDROL_F22_1; 1.
DR   PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2; 1.
PE   2: Evidence at transcript level;
KW   Antimicrobial; Bacteriolytic enzyme; Disulfide bond; Glycosidase;
KW   Hydrolase; Reference proteome; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..140
FT                   /note="Lysozyme c-1"
FT                   /id="PRO_0000018504"
FT   DOMAIN          21..140
FT                   /note="C-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        52
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        69
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        26..139
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        47..128
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        81..94
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        90..108
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   CONFLICT        5
FT                   /note="S -> F (in Ref. 1; AAC47326)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   140 AA;  15338 MW;  D30D604699316D24 CRC64;
     MKVFSTVLLA IVACCAVAEA KTFGKCELAK ALANNGIAKA SLPDWVCLVQ NESAFSTSAT
     NKNKNGSTDY GIFQINNKYW CDSGYGSNDC KIACKNLLND DITDDIKCAK LIHKRHGFNA
     WYGWKNHCNG KKLPNVSSCF
//