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 24-JAN-2024, entry version 138.
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; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; 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 RefSeq; XP_308481.1; XM_308481.3.
DR AlphaFoldDB; Q17005; -.
DR SMR; Q17005; -.
DR STRING; 7165.Q17005; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR PaxDb; 7165-AGAP007347-PA; -.
DR EnsemblMetazoa; AGAP007347-RA; AGAP007347-PA; AGAP007347.
DR GeneID; 1269831; -.
DR KEGG; aga:AgaP_AGAP007347; -.
DR CTD; 1269831; -.
DR VEuPathDB; VectorBase:AGAP007347; -.
DR eggNOG; ENOG502S4CB; Eukaryota.
DR HOGENOM; CLU_111620_0_1_1; -.
DR InParanoid; Q17005; -.
DR OMA; NTQAFNG; -.
DR OrthoDB; 5361006at2759; -.
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 GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd16899; LYZ_C_invert; 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
//
