Reviewed, UniProtKB/Swiss-Prot Q17005 (LYSC1_ANOGA)

Names and origin

Protein names

Recommended name:
    Lysozyme c-1
    EC=3.2.1.17
Alternative name(s):
    1,4-beta-N-acetylmuramidase

Gene names

ORF Names:

AGAP007347

Organism

Anopheles gambiae (African malaria mosquito) [Complete proteome]

Taxonomic identifier

7165 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Nematocera › Culicoidea › Culicidae › Anophelinae › Anopheles

Protein attributes

Sequence length	140 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Domain	Signal
Molecular function	Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell wall macromolecule catabolic process Inferred from electronic annotation. Source: InterPro cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	lysozyme activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 140	120	Lysozyme c-1		PRO_0000018504
Sites
	Active site	52	1	By similarity
	Active site	69	1	By similarity
Amino acid modifications
	Disulfide bond	26 ↔ 139		By similarity
	Disulfide bond	47 ↔ 128		By similarity
	Disulfide bond	81 ↔ 94		By similarity
	Disulfide bond	90 ↔ 108		By similarity
Experimental info
	Sequence conflict	5	1	S → F in AAC47326. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q17005-1 [UniParc]. Last modified May 16, 2006. Version 2. Checksum: D30D604699316D24	FASTA	140	15,338
	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

References

	« Hide 'large scale' referencesShow '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: 8890741] [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: 16137842] [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: 12364791] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PEST.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U28809 Genomic DNA. Translation: AAC47326.1. DQ007317 mRNA. Translation: AAY24699.1. AAAB01008807 Genomic DNA. Translation: EAA45417.1.
PIR	JC5003.
RefSeq	XP_308481.1.
3D structure databases
HSSP	HSSP built from PDB template 1GD6 based on UniProtKB P48816.
ModBase	Search...
Protein family/group databases
CAZy	GH22. Glycoside Hydrolase Family 22.
Genome annotation databases
Ensembl	AGAP007347. Anopheles gambiae. [Contig view]
GeneID	1269831.
KEGG	aga:AgaP_AGAP007347.
VectorBase	AGAP007347. Anopheles gambiae.
Phylogenomic databases
HOGENOM	Q17005.
OMA	Q17005. ICNIKCE.
Enzyme and pathway databases
BRENDA	3.2.1.17. 165157.
Family and domain databases
InterPro	IPR001916. Glyco_hydro_22. IPR019799. Glyco_hydro_22_CS. IPR000974. Glyco_hydro_22_lys. [Graphical view]
Pfam	PF00062. Lys. 1 hit. [Graphical view]
PRINTS	PR00137. LYSOZYME. PR00135. LYZLACT.
SMART	SM00263. LYZ1. 1 hit. [Graphical view]
PROSITE	PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit. PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LYSC1_ANOGA

Accession

Primary (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:	June 16, 2009
This is version 65 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)