SPZ_DROME
ID SPZ_DROME Reviewed; 326 AA.
AC P48607; Q95SU5; Q9VB84;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Protein spaetzle;
DE Contains:
DE RecName: Full=Protein spaetzle C-106;
DE Flags: Precursor;
GN Name=spz; ORFNames=CG6134;
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 (ISOFORM 11.7), FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=8124709; DOI=10.1016/0092-8674(94)90507-x;
RA Morisato D., Anderson K.V.;
RT "The spatzle gene encodes a component of the extracellular signaling
RT pathway establishing the dorsal-ventral pattern of the Drosophila embryo.";
RL Cell 76:677-688(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING, FUNCTION,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=11212919; DOI=10.1007/s004380000350;
RA DeLotto Y., Smith C., DeLotto R.;
RT "Multiple isoforms of the Drosophila spatzle protein are encoded by
RT alternatively spliced maternal mRNAs in the precellular blastoderm
RT embryo.";
RL Mol. Gen. Genet. 264:643-652(2001).
RN [3]
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 [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 11.6).
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [6]
RP PROTEIN SEQUENCE OF 26-30 AND 221-226 (ISOFORM 8.19), SUBUNIT, CLEAVAGE BY
RP EASTER, DISULFIDE BONDS, AND MUTAGENESIS OF CYS-318.
RX PubMed=9533958; DOI=10.1016/s0925-4773(98)00024-0;
RA DeLotto Y., DeLotto R.;
RT "Proteolytic processing of the Drosophila Spatzle protein by easter
RT generates a dimeric NGF-like molecule with ventralising activity.";
RL Mech. Dev. 72:141-148(1998).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8808632; DOI=10.1016/s0092-8674(00)80172-5;
RA Lemaitre B., Nicolas E., Michaut L., Reichhart J.-M., Hoffmann J.A.;
RT "The dorsoventral regulatory gene cassette spatzle/Toll/cactus controls the
RT potent antifungal response in Drosophila adults.";
RL Cell 86:973-983(1996).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH TL.
RX PubMed=12872120; DOI=10.1038/ni955;
RA Weber A.N., Tauszig-Delamasure S., Hoffmann J.A., Lelievre E., Gascan H.,
RA Ray K.P., Morse M.A., Imler J.L., Gay N.J.;
RT "Binding of the Drosophila cytokine Spatzle to Toll is direct and
RT establishes signaling.";
RL Nat. Immunol. 4:794-800(2003).
RN [9]
RP CLEAVAGE BY SPE, AND MUTAGENESIS OF 220-ARG-VAL-221.
RX PubMed=16399077; DOI=10.1016/j.devcel.2005.11.013;
RA Jang I.H., Chosa N., Kim S.H., Nam H.J., Lemaitre B., Ochiai M.,
RA Kambris Z., Brun S., Hashimoto C., Ashida M., Brey P.T., Lee W.J.;
RT "A Spatzle-processing enzyme required for toll signaling activation in
RT Drosophila innate immunity.";
RL Dev. Cell 10:45-55(2006).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 221-326, AND DISULFIDE BONDS.
RX PubMed=18790733; DOI=10.1074/jbc.m801815200;
RA Hoffmann A., Funkner A., Neumann P., Juhnke S., Walther M., Schierhorn A.,
RA Weininger U., Balbach J., Reuter G., Stubbs M.T.;
RT "Biophysical characterization of refolded Drosophila Spatzle, a cystine
RT knot protein, reveals distinct properties of three isoforms.";
RL J. Biol. Chem. 283:32598-32609(2008).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 221-326, SUBUNIT, AND MUTAGENESIS
RP OF 234-ARG-LYS-235 AND ASP-275.
RX PubMed=24282309; DOI=10.1073/pnas.1317002110;
RA Lewis M., Arnot C.J., Beeston H., McCoy A., Ashcroft A.E., Gay N.J.,
RA Gangloff M.;
RT "Cytokine Spatzle binds to the Drosophila immunoreceptor Toll with a
RT neurotrophin-like specificity and couples receptor activation.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20461-20466(2013).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 221-326, AND SUBUNIT.
RX PubMed=24733933; DOI=10.1073/pnas.1320678111;
RA Parthier C., Stelter M., Ursel C., Fandrich U., Lilie H., Breithaupt C.,
RA Stubbs M.T.;
RT "Structure of the Toll-Spatzle complex, a molecular hub in Drosophila
RT development and innate immunity.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:6281-6286(2014).
CC -!- FUNCTION: The activated form, spaetzle C-106, acts as a ligand for the
CC Toll receptor (PubMed:12872120). Binding to Toll activates the Toll
CC signaling pathway and induces expression of the antifungal peptide
CC drosomycin (PubMed:8808632). Component of the extracellular signaling
CC pathway that establishes dorsal-ventral polarity in the embryo
CC (PubMed:8124709, PubMed:11212919). {ECO:0000269|PubMed:11212919,
CC ECO:0000269|PubMed:12872120, ECO:0000269|PubMed:8124709,
CC ECO:0000269|PubMed:8808632}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:12872120, PubMed:9533958).
CC In the presence of Tl, crystal structures show one Tl molecule bound to
CC a spaetzle C-106 homodimer (PubMed:24733933, PubMed:24282309). However,
CC the active complex probably consists of two Tl molecules bound to a
CC spaetzle C-106 homodimer (PubMed:24282309, PubMed:24733933). This is
CC supported by in vitro experiments which also show binding of the
CC spaetzle C-106 dimer to 2 Tl receptors (PubMed:12872120). Ligand
CC binding induces conformational changes in the extracellular domain of
CC Tl (PubMed:24282309). This may enable a secondary homodimerization
CC interface at the C-terminus of the Tl extracellular domain
CC (PubMed:24282309). {ECO:0000269|PubMed:12872120,
CC ECO:0000269|PubMed:24282309, ECO:0000269|PubMed:24733933,
CC ECO:0000269|PubMed:9533958, ECO:0000303|PubMed:24282309}.
CC -!- SUBCELLULAR LOCATION: [Isoform 8.19]: Secreted. Note=Secreted in a cell
CC culture system.
CC -!- SUBCELLULAR LOCATION: [Isoform 8.29]: Secreted. Note=Secreted in a cell
CC culture system.
CC -!- SUBCELLULAR LOCATION: [Isoform 11.15]: Secreted. Note=Secreted in a
CC cell culture system.
CC -!- SUBCELLULAR LOCATION: [Isoform 11.6]: Secreted. Note=Secreted in a cell
CC culture system.
CC -!- SUBCELLULAR LOCATION: [Isoform 11.7]: Secreted. Note=Secreted in a cell
CC culture system.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Name=8.19; Synonyms=A;
CC IsoId=P48607-1; Sequence=Displayed;
CC Name=8.20; Synonyms=I;
CC IsoId=P48607-2; Sequence=VSP_004420;
CC Name=8.24;
CC IsoId=P48607-4; Sequence=VSP_004418, VSP_004425, VSP_004427,
CC VSP_004428;
CC Name=8.29; Synonyms=D;
CC IsoId=P48607-5; Sequence=VSP_004419, VSP_004424;
CC Name=11.15;
CC IsoId=P48607-10; Sequence=VSP_004422, VSP_010257;
CC Name=11.27;
CC IsoId=P48607-6; Sequence=VSP_004422, VSP_004426;
CC Name=11.32;
CC IsoId=P48607-7; Sequence=VSP_004418, VSP_004423;
CC Name=11.5;
CC IsoId=P48607-8; Sequence=VSP_004421;
CC Name=11.6; Synonyms=B, 8.23;
CC IsoId=P48607-3; Sequence=VSP_004418;
CC Name=11.7; Synonyms=C, 23 kDa;
CC IsoId=P48607-9; Sequence=VSP_004422;
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. All
CC isoforms, except isoform 8.20, are rapidly degraded on cellularisation
CC of the blastoderm embryo. {ECO:0000269|PubMed:8124709}.
CC -!- PTM: During embryonic development, easter cleaves the signal peptide
CC and also generates the C-terminal 12 kDa active fragment, C-106 (except
CC for isoform 8.24 and isoform 11.27 as they do not contain the cleavage
CC site) (PubMed:9533958). During the immune response, cleaved in the same
CC manner by SPE (PubMed:16399077). {ECO:0000269|PubMed:16399077,
CC ECO:0000269|PubMed:9533958}.
CC -!- PTM: Extracellular forms of isoform 8.19 and isoform 11.7 are
CC glycosylated.
CC -!- MISCELLANEOUS: 'Spaetzle' means 'noodles' in German.
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DR EMBL; U05850; AAA17887.1; -; Unassigned_DNA.
DR EMBL; AF237964; AAF98123.1; -; mRNA.
DR EMBL; AF237965; AAF98124.1; -; mRNA.
DR EMBL; AF237966; AAF98125.1; -; mRNA.
DR EMBL; AF237967; AAF98126.1; -; mRNA.
DR EMBL; AF237968; AAF98127.1; -; mRNA.
DR EMBL; AF237969; AAF98128.1; -; mRNA.
DR EMBL; AF237970; AAF98129.1; -; mRNA.
DR EMBL; AF237971; AAF98130.1; -; mRNA.
DR EMBL; AF237972; AAF98131.1; -; mRNA.
DR EMBL; AF237973; AAF98132.1; -; mRNA.
DR EMBL; AF237974; AAF82745.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF56658.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN14388.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN14391.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN14394.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN14395.1; -; Genomic_DNA.
DR EMBL; AY060478; AAL25517.1; -; mRNA.
DR PIR; A53190; A53190.
DR RefSeq; NP_524526.1; NM_079802.3. [P48607-1]
DR RefSeq; NP_733188.1; NM_170309.2. [P48607-2]
DR RefSeq; NP_733191.1; NM_170312.2. [P48607-3]
DR RefSeq; NP_733194.1; NM_170315.2. [P48607-9]
DR RefSeq; NP_733195.1; NM_170316.2. [P48607-5]
DR PDB; 3E07; X-ray; 2.40 A; A/B=221-326.
DR PDB; 4BV4; X-ray; 2.35 A; L/M=221-326.
DR PDB; 4LXR; X-ray; 2.20 A; J/K=221-326.
DR PDB; 4LXS; X-ray; 3.30 A; J/K=221-326.
DR PDBsum; 3E07; -.
DR PDBsum; 4BV4; -.
DR PDBsum; 4LXR; -.
DR PDBsum; 4LXS; -.
DR AlphaFoldDB; P48607; -.
DR SMR; P48607; -.
DR BioGRID; 68145; 18.
DR ComplexPortal; CPX-3140; spaetzle complex.
DR DIP; DIP-23237N; -.
DR IntAct; P48607; 2.
DR STRING; 7227.FBpp0084507; -.
DR GlyGen; P48607; 3 sites.
DR PaxDb; P48607; -.
DR PeptideAtlas; P48607; -.
DR DNASU; 43256; -.
DR EnsemblMetazoa; FBtr0085137; FBpp0084507; FBgn0003495. [P48607-1]
DR EnsemblMetazoa; FBtr0085138; FBpp0084508; FBgn0003495. [P48607-3]
DR EnsemblMetazoa; FBtr0085139; FBpp0084509; FBgn0003495. [P48607-9]
DR EnsemblMetazoa; FBtr0085140; FBpp0084510; FBgn0003495. [P48607-5]
DR EnsemblMetazoa; FBtr0085145; FBpp0084515; FBgn0003495. [P48607-2]
DR GeneID; 43256; -.
DR KEGG; dme:Dmel_CG6134; -.
DR UCSC; CG6134-RA; d. melanogaster. [P48607-1]
DR CTD; 43256; -.
DR FlyBase; FBgn0003495; spz.
DR VEuPathDB; VectorBase:FBgn0003495; -.
DR eggNOG; ENOG502S688; Eukaryota.
DR GeneTree; ENSGT00700000106225; -.
DR InParanoid; P48607; -.
DR OMA; RSFCTQV; -.
DR PhylomeDB; P48607; -.
DR Reactome; R-DME-209442; Formation of the trans-membrane 'signalling complex'.
DR Reactome; R-DME-214842; DL and DIF homodimers bind to TUB and phosphorylated PLL in the TL receptor 'signalling complex'.
DR Reactome; R-DME-214844; DL and DIF homodimers complexed with CACT are all phosphorylated in the TL receptor 'signalling complex'.
DR Reactome; R-DME-214862; Activated PLL kinase is autophosphorylated in the TL receptor 'signalling complex'.
DR Reactome; R-DME-214863; Adaptor protein complex binds to TL receptor at the plasma membrane.
DR Reactome; R-DME-214869; Phosphorylated CACT, DL and DIF homodimers dissociate from the TL receptor 'signalling complex'.
DR Reactome; R-DME-214874; PLL kinase binds to TUB in the TL receptor 'signalling complex'.
DR SignaLink; P48607; -.
DR BioGRID-ORCS; 43256; 0 hits in 1 CRISPR screen.
DR EvolutionaryTrace; P48607; -.
DR GenomeRNAi; 43256; -.
DR PRO; PR:P48607; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003495; Expressed in embryonic/larval hemocyte (Drosophila) and 30 other tissues.
DR ExpressionAtlas; P48607; baseline and differential.
DR Genevisible; P48607; DM.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0005125; F:cytokine activity; TAS:FlyBase.
DR GO; GO:0008083; F:growth factor activity; IMP:FlyBase.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
DR GO; GO:0048018; F:receptor ligand activity; IDA:FlyBase.
DR GO; GO:0005121; F:Toll binding; IDA:FlyBase.
DR GO; GO:0061760; P:antifungal innate immune response; IDA:FlyBase.
DR GO; GO:0035212; P:cell competition in a multicellular organism; IMP:FlyBase.
DR GO; GO:0021556; P:central nervous system formation; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:FlyBase.
DR GO; GO:0009950; P:dorsal/ventral axis specification; IDA:FlyBase.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IDA:FlyBase.
DR GO; GO:0045087; P:innate immune response; IDA:FlyBase.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0007526; P:larval somatic muscle development; IMP:FlyBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
DR GO; GO:0007310; P:oocyte dorsal/ventral axis specification; IEP:UniProtKB.
DR GO; GO:0006967; P:positive regulation of antifungal peptide biosynthetic process; IMP:FlyBase.
DR GO; GO:0002804; P:positive regulation of antifungal peptide production; IMP:FlyBase.
DR GO; GO:0002807; P:positive regulation of antimicrobial peptide biosynthetic process; IDA:FlyBase.
DR GO; GO:0002225; P:positive regulation of antimicrobial peptide production; IGI:UniProtKB.
DR GO; GO:0006965; P:positive regulation of biosynthetic process of antibacterial peptides active against Gram-positive bacteria; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0045752; P:positive regulation of Toll signaling pathway; IMP:UniProtKB.
DR GO; GO:0008592; P:regulation of Toll signaling pathway; IMP:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IDA:FlyBase.
DR GO; GO:0002347; P:response to tumor cell; IMP:FlyBase.
DR GO; GO:0009611; P:response to wounding; IEP:FlyBase.
DR GO; GO:0008063; P:Toll signaling pathway; IDA:FlyBase.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR032104; Spaetzle.
DR Pfam; PF16077; Spaetzle; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Antimicrobial; Cytokine;
KW Developmental protein; Direct protein sequencing; Disulfide bond;
KW Fungicide; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT CHAIN 26..326
FT /note="Protein spaetzle"
FT /id="PRO_0000022406"
FT CHAIN 221..326
FT /note="Protein spaetzle C-106"
FT /id="PRO_0000022407"
FT DOMAIN 228..322
FT /note="Spaetzle"
FT /evidence="ECO:0000255"
FT REGION 56..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 220..221
FT /note="Cleavage; by easter"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 230..288
FT /evidence="ECO:0000269|PubMed:18790733,
FT ECO:0000303|PubMed:9533958"
FT DISULFID 267..319
FT /evidence="ECO:0000269|PubMed:18790733,
FT ECO:0000303|PubMed:9533958"
FT DISULFID 274..321
FT /evidence="ECO:0000269|PubMed:18790733,
FT ECO:0000303|PubMed:9533958"
FT DISULFID 318
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:18790733,
FT ECO:0000303|PubMed:9533958"
FT VAR_SEQ 23..185
FT /note="Missing (in isoform 11.5)"
FT /evidence="ECO:0000305"
FT /id="VSP_004421"
FT VAR_SEQ 23..121
FT /note="Missing (in isoform 8.20)"
FT /evidence="ECO:0000305"
FT /id="VSP_004420"
FT VAR_SEQ 23..67
FT /note="YEAKEYERIIKELFTITNDEGVVLFNTSADSAPFMPIPTQHDDPT -> IVY
FT INIELTKRHEAEVRAEKTVADYKALLATINNGGPGKSASNHL (in isoform
FT 8.29)"
FT /evidence="ECO:0000305"
FT /id="VSP_004419"
FT VAR_SEQ 23..48
FT /note="Missing (in isoform 8.24, isoform 11.32 and isoform
FT 11.6)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_004418"
FT VAR_SEQ 49..121
FT /note="Missing (in isoform 11.15, isoform 11.27 and isoform
FT 11.7)"
FT /evidence="ECO:0000305"
FT /id="VSP_004422"
FT VAR_SEQ 65..189
FT /note="Missing (in isoform 11.32)"
FT /evidence="ECO:0000305"
FT /id="VSP_004423"
FT VAR_SEQ 68..120
FT /note="Missing (in isoform 8.29)"
FT /evidence="ECO:0000305"
FT /id="VSP_004424"
FT VAR_SEQ 101..121
FT /note="Missing (in isoform 8.24)"
FT /evidence="ECO:0000305"
FT /id="VSP_004425"
FT VAR_SEQ 142..151
FT /note="Missing (in isoform 11.15)"
FT /evidence="ECO:0000305"
FT /id="VSP_010257"
FT VAR_SEQ 189..225
FT /note="Missing (in isoform 11.27)"
FT /evidence="ECO:0000305"
FT /id="VSP_004426"
FT VAR_SEQ 197..226
FT /note="THKLKNNFAKFFSNDLQPTDVSSRVGGSDE -> RRAIPLQEHQEAGVPKKG
FT LEGGRHLAVNCQ (in isoform 8.24)"
FT /evidence="ECO:0000305"
FT /id="VSP_004427"
FT VAR_SEQ 227..326
FT /note="Missing (in isoform 8.24)"
FT /evidence="ECO:0000305"
FT /id="VSP_004428"
FT MUTAGEN 220..221
FT /note="RV->LN: Not cleaved when expressed with activated
FT SPE."
FT /evidence="ECO:0000269|PubMed:16399077"
FT MUTAGEN 234..235
FT /note="RK->AA: Abolishes signaling almost completely."
FT /evidence="ECO:0000269|PubMed:24282309"
FT MUTAGEN 275
FT /note="D->R: Strongly reduced signaling."
FT /evidence="ECO:0000269|PubMed:24282309"
FT MUTAGEN 318
FT /note="C->S,T: Reduced phenotypic rescue of a mutant."
FT /evidence="ECO:0000269|PubMed:9533958"
FT CONFLICT 50
FT /note="S -> T (in Ref. 2; AAF98130)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="S -> T (in Ref. 2; AAF98124)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="T -> P (in Ref. 5; AAL25517)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="N -> D (in Ref. 2; AAF98130/AAF98131/AAF98126)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="S -> F (in Ref. 2; AAF98132)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="R -> T (in Ref. 2; AAF98129)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="C -> S (in Ref. 2; AAF98129)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="T -> R (in Ref. 2; AAF98125)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="K -> N (in Ref. 2; AAF98129)"
FT /evidence="ECO:0000305"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:3E07"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:4LXR"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 285..293
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:3E07"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:3E07"
FT STRAND 315..325
FT /evidence="ECO:0007829|PDB:4LXR"
SQ SEQUENCE 326 AA; 37447 MW; 3252389129CFB1E0 CRC64;
MMTPMWISLF KVLLLLFAFF ATYEAKEYER IIKELFTITN DEGVVLFNTS ADSAPFMPIP
TQHDDPTQKQ KQNQNQSPIP ETNRHYHQYH SLIQPDQYFK VQRSPNGKLN LVFNDTFVSL
QRTDTEVQSE QPIPPRHPSD TFVFPDSPIA KYRPPQSPAR PLRNDTKEHN PCAKDESQHL
RNFCTNVDDY PDLSGLTHKL KNNFAKFFSN DLQPTDVSSR VGGSDERFLC RSIRKLVYPK
KGLRADDTWQ LIVNNDEYKQ AIQIEECEGA DQPCDFAANF PQSYNPICKQ HYTQQTLASI
KSDGELDVVQ NSFKIPSCCK CALKTG
