ID   MTK_DROME               Reviewed;          52 AA.
AC   Q24395; Q24396; Q86BV8; Q9V7B9;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   24-JAN-2024, entry version 149.
DE   RecName: Full=Metchnikowin;
DE   Flags: Precursor;
GN   Name=Mtk; ORFNames=CG8175;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 27-52, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=Oregon-R; TISSUE=Abdomen, and Thorax;
RX   PubMed=7588819; DOI=10.1111/j.1432-1033.1995.694_2.x;
RA   Levashina E.A., Ohresser S., Bulet P., Reichhart J.-M., Hetru C.,
RA   Hoffmann J.A.;
RT   "Metchnikowin, a novel immune-inducible proline-rich peptide from
RT   Drosophila with antibacterial and antifungal properties.";
RL   Eur. J. Biochem. 233:694-700(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Oregon-R;
RX   PubMed=9600835; DOI=10.1006/jmbi.1998.1705;
RA   Levashina E.A., Ohresser S., Lemaitre B., Imler J.-L.;
RT   "Two distinct pathways can control expression of the gene encoding the
RT   Drosophila antimicrobial peptide metchnikowin.";
RL   J. Mol. Biol. 278:515-527(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE, AND VARIANTS THR-19 AND ARG-29.
RC   STRAIN=2CPA1, 2CPA103, 2CPA105, 2CPA118, 2CPA12, 2CPA122, 2CPA129,
RC   2CPA14, 2CPA43, 2CPA46, 2CPA51, and 2CPA7;
RX   PubMed=12716986; DOI=10.1093/molbev/msg109;
RA   Lazzaro B.P., Clark A.G.;
RT   "Molecular population genetics of inducible antibacterial peptide genes in
RT   Drosophila melanogaster.";
RL   Mol. Biol. Evol. 20:914-923(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Head;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [7]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY BACTERIA, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=Oregon-R {ECO:0000303|PubMed:9736738};
RC   TISSUE=Hemolymph {ECO:0000303|PubMed:9736738};
RX   PubMed=9736738; DOI=10.1073/pnas.95.19.11342;
RA   Uttenweiler-Joseph S., Moniatte M., Lagueux M., van Dorsselaer A.,
RA   Hoffmann J.A., Bulet P.;
RT   "Differential display of peptides induced during the immune response of
RT   Drosophila: a matrix-assisted laser desorption ionization time-of-flight
RT   mass spectrometry study.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:11342-11347(1998).
CC   -!- FUNCTION: Potent antifungal and antibacterial activity against Gram-
CC       positive bacteria.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9736738}.
CC   -!- TISSUE SPECIFICITY: Hemolymph (at protein level) (PubMed:9736738).
CC       Highest expression in fat body (PubMed:7588819).
CC       {ECO:0000269|PubMed:7588819, ECO:0000269|PubMed:9736738}.
CC   -!- DEVELOPMENTAL STAGE: Expressed rapidly and strongly at all stages.
CC   -!- INDUCTION: By bacterial infection (at protein level) (PubMed:9736738).
CC       Up-regulated in hemolymph 6 hours after immune challenge, levels of
CC       expression increase for first 24 hours and persist for the following
CC       two weeks (at protein level) (PubMed:9736738).
CC       {ECO:0000269|PubMed:9736738}.
CC   -!- MASS SPECTROMETRY: Mass=3045.4; Method=MALDI; Note=Variant Arg-29.;
CC       Evidence={ECO:0000269|PubMed:9736738};
CC   -!- POLYMORPHISM: There are 2 allelic forms (A1 and A2) varying in two
CC       positions. The isoform shown here is A1. {ECO:0000269|PubMed:12716986}.
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DR   EMBL; X91060; CAA62511.1; -; mRNA.
DR   EMBL; X91061; CAA62512.1; -; mRNA.
DR   EMBL; AF030959; AAC64659.1; -; Genomic_DNA.
DR   EMBL; AY224619; AAO72478.1; -; Genomic_DNA.
DR   EMBL; AY224620; AAO72479.1; -; Genomic_DNA.
DR   EMBL; AY224621; AAO72480.1; -; Genomic_DNA.
DR   EMBL; AY224622; AAO72481.1; -; Genomic_DNA.
DR   EMBL; AY224623; AAO72482.1; -; Genomic_DNA.
DR   EMBL; AY224624; AAO72483.1; -; Genomic_DNA.
DR   EMBL; AY224625; AAO72484.1; -; Genomic_DNA.
DR   EMBL; AY224626; AAO72485.1; -; Genomic_DNA.
DR   EMBL; AY224627; AAO72486.1; -; Genomic_DNA.
DR   EMBL; AY224628; AAO72487.1; -; Genomic_DNA.
DR   EMBL; AY224629; AAO72488.1; -; Genomic_DNA.
DR   EMBL; AY224630; AAO72489.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAF58139.1; -; Genomic_DNA.
DR   EMBL; AY075536; AAL68343.1; -; mRNA.
DR   PIR; S63981; S63981.
DR   RefSeq; NP_523752.1; NM_079028.3.
DR   PDB; 4EZS; X-ray; 1.90 A; B=46-52.
DR   PDBsum; 4EZS; -.
DR   AlphaFoldDB; Q24395; -.
DR   SMR; Q24395; -.
DR   DIP; DIP-23804N; -.
DR   STRING; 7227.FBpp0086518; -.
DR   PaxDb; 7227-FBpp0086518; -.
DR   DNASU; 36708; -.
DR   EnsemblMetazoa; FBtr0087386; FBpp0086518; FBgn0014865.
DR   GeneID; 36708; -.
DR   KEGG; dme:Dmel_CG8175; -.
DR   AGR; FB:FBgn0014865; -.
DR   CTD; 36708; -.
DR   FlyBase; FBgn0014865; Mtk.
DR   VEuPathDB; VectorBase:FBgn0014865; -.
DR   eggNOG; ENOG502T9AQ; Eukaryota.
DR   HOGENOM; CLU_214043_0_0_1; -.
DR   InParanoid; Q24395; -.
DR   OMA; SEPHRHQ; -.
DR   PhylomeDB; Q24395; -.
DR   BioGRID-ORCS; 36708; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 36708; -.
DR   PRO; PR:Q24395; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0014865; Expressed in head capsule and 20 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; IDA:FlyBase.
DR   GO; GO:0019731; P:antibacterial humoral response; IEP:FlyBase.
DR   GO; GO:0019732; P:antifungal humoral response; IEP:FlyBase.
DR   GO; GO:0006952; P:defense response; IDA:FlyBase.
DR   GO; GO:0050832; P:defense response to fungus; IDA:FlyBase.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:FlyBase.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:FlyBase.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0009617; P:response to bacterium; IDA:FlyBase.
DR   GO; GO:0009611; P:response to wounding; IEP:FlyBase.
DR   InterPro; IPR012513; Mtk.
DR   Pfam; PF08105; Antimicrobial10; 1.
DR   Genevisible; Q24395; DM.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial; Direct protein sequencing;
KW   Fungicide; Immunity; Innate immunity; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..26
FT                   /evidence="ECO:0000269|PubMed:7588819"
FT                   /id="PRO_0000004983"
FT   PEPTIDE         27..52
FT                   /note="Metchnikowin"
FT                   /id="PRO_0000004984"
FT   REGION          28..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         19
FT                   /note="A -> T (in strain: 2CPA51)"
FT                   /evidence="ECO:0000269|PubMed:12716986"
FT   VARIANT         29
FT                   /note="H -> R (in strain: 2CPA51)"
FT                   /evidence="ECO:0000269|PubMed:12716986"
SQ   SEQUENCE   52 AA;  5654 MW;  0B1E2112BAE03129 CRC64;
     MQLNLGAIFL ALLGVMATAT SVLAEPHRHQ GPIFDTRPSP FNPNQPRPGP IY
//