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Spaetzle-processing enzyme (EC 3.4.21.-) (Spatzle-processing enzyme) [Cleaved into: Spaetzle-processing enzyme light chain; Spaetzle-processing enzyme heavy chain]

 SPE_DROME               Reviewed;         400 AA.
Q9VCJ8;
28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 2.
25-APR-2018, entry version 157.
RecName: Full=Spaetzle-processing enzyme {ECO:0000303|PubMed:16996061};
EC=3.4.21.- {ECO:0000269|PubMed:16399077, ECO:0000269|PubMed:26843333};
AltName: Full=Spatzle-processing enzyme {ECO:0000303|PubMed:16399077};
Contains:
RecName: Full=Spaetzle-processing enzyme light chain {ECO:0000305};
Contains:
RecName: Full=Spaetzle-processing enzyme heavy chain {ECO:0000305};
Flags: Precursor;
Name=SPE {ECO:0000312|FlyBase:FBgn0039102};
Synonyms=c-SP4 {ECO:0000312|FlyBase:FBgn0039102},
SP4 {ECO:0000312|FlyBase:FBgn0039102};
ORFNames=CG16705 {ECO:0000312|FlyBase:FBgn0039102};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
[1] {ECO:0000312|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2] {ECO:0000312|Proteomes:UP000000803}
GENOME REANNOTATION.
STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[3] {ECO:0000312|EMBL:AAK93062.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley {ECO:0000312|EMBL:AAK93062.1};
TISSUE=Head {ECO:0000312|EMBL:AAK93062.1};
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[4] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16631589; DOI=10.1016/j.cub.2006.03.020;
Kambris Z., Brun S., Jang I.H., Nam H.J., Romeo Y., Takahashi K.,
Lee W.J., Ueda R., Lemaitre B.;
"Drosophila immunity: a large-scale in vivo RNAi screen identifies
five serine proteases required for Toll activation.";
Curr. Biol. 16:808-813(2006).
[5] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, INDUCTION, DISRUPTION PHENOTYPE,
MUTAGENESIS OF ARG-134, AND PROTEOLYTIC CLEAVAGE.
PubMed=16399077; DOI=10.1016/j.devcel.2005.11.013;
Jang I.H., Chosa N., Kim S.H., Nam H.J., Lemaitre B., Ochiai M.,
Kambris Z., Brun S., Hashimoto C., Ashida M., Brey P.T., Lee W.J.;
"A Spatzle-processing enzyme required for toll signaling activation in
Drosophila innate immunity.";
Dev. Cell 10:45-55(2006).
[6] {ECO:0000305}
FUNCTION, DEVELOPMENTAL STAGE, INDUCTION, AND DISRUPTION PHENOTYPE.
PubMed=16996061; DOI=10.1016/j.febslet.2006.09.009;
Mulinari S., Haecker U., Castillejo-Lopez C.;
"Expression and regulation of Spaetzle-processing enzyme in
Drosophila.";
FEBS Lett. 580:5406-5410(2006).
[7] {ECO:0000305}
FUNCTION.
PubMed=18724373; DOI=10.1038/ni.1643;
El Chamy L., Leclerc V., Caldelari I., Reichhart J.M.;
"Sensing of 'danger signals' and pathogen-associated molecular
patterns defines binary signaling pathways 'upstream' of Toll.";
Nat. Immunol. 9:1165-1170(2008).
[8] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
PubMed=26843333; DOI=10.1247/csf.16002;
Yamamoto-Hino M., Goto S.;
"Spaetzle-processing enzyme-independent activation of the toll pathway
in Drosophila innate immunity.";
Cell Struct. Funct. 41:55-60(2016).
-!- FUNCTION: Endopeptidase which plays a key role in innate immunity
by cleaving Tl ligand spz and thereby activating the Toll pathway
in response to fungal and Gram-positive bacterial infections
(PubMed:16631589, PubMed:16399077, PubMed:18724373,
PubMed:26843333, PubMed:16996061). Acts downstream of pathogen
recognition receptors PGRP-SA and GNBP1 and protease grass in
response to Gram-positive bacterial infection (PubMed:16399077).
Acts downstream of protease psh in response to fungal infection
(PubMed:16399077). {ECO:0000269|PubMed:16399077,
ECO:0000269|PubMed:16631589, ECO:0000269|PubMed:16996061,
ECO:0000269|PubMed:18724373, ECO:0000269|PubMed:26843333}.
-!- SUBUNIT: In the active form, heterodimer of a light chain and a
heavy chain; disulfide-linked. {ECO:0000305|PubMed:16399077}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Note=Probably
secreted in the hemolymph. {ECO:0000305}.
-!- DEVELOPMENTAL STAGE: In embryogenesis, expressed from stage 11 at
the posterior tip of the germ-band; during germline retraction,
expressed both ventrally and dorsally; expressed in the developing
fat body and lymph nodes. In larvae, expressed in the fat body and
in mature hemocytes with weak expression in the lymph glands.
{ECO:0000269|PubMed:16996061}.
-!- INDUCTION: Up-regulated in response to fungal and Gram-positive
bacterial infections. {ECO:0000269|PubMed:16399077,
ECO:0000269|PubMed:16996061}.
-!- DOMAIN: The CLIP domain consists of 37-55 residues which are
"knitted" together usually by 3 conserved disulfide bonds forming
a clip-like compact structure. {ECO:0000305}.
-!- PTM: Proteolytically cleaved in response to Gram-negative
bacterial or fungal infection; processing is likely to result in
its activation (PubMed:16399077). Cleavage produces a light chain
containing the CLIP domain and a catalytic heavy chain which
remain covalently associated through an interchain disulfide bond
(Probable). {ECO:0000269|PubMed:16399077,
ECO:0000305|PubMed:16399077}.
-!- DISRUPTION PHENOTYPE: In larvae infected with Gram-positive
bacteria, fails to induce the expression of the Toll pathway-
activated anti-fungal peptide Drs (PubMed:26843333). siRNA-
mediated knockdown results in increased susceptibility to fungal
and Gram-positive bacterial infections, failure to cleave spz and
to induce the expression of the antifungal peptide Drs
(PubMed:16399077, PubMed:16996061). RNAi-mediated knockdown in the
fat body causes increased susceptibility to fungal and Gram-
positive bacterial infections and failure to induce the expression
of the antifungal peptide Drs (PubMed:16631589).
{ECO:0000269|PubMed:16399077, ECO:0000269|PubMed:16631589,
ECO:0000269|PubMed:16996061, ECO:0000269|PubMed:26843333}.
-!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
{ECO:0000305}.
-!- CAUTION: It is not clear if the light chain is degraded after
cleavage. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AE014297; AAF56160.2; -; Genomic_DNA.
EMBL; AY051638; AAK93062.1; -; mRNA.
RefSeq; NP_651168.1; NM_142911.4.
UniGene; Dm.1296; -.
SMR; Q9VCJ8; -.
STRING; 7227.FBpp0083832; -.
MEROPS; S01.462; -.
EnsemblMetazoa; FBtr0084440; FBpp0083832; FBgn0039102.
GeneID; 42791; -.
KEGG; dme:Dmel_CG16705; -.
UCSC; CG16705-RA; d. melanogaster.
CTD; 42791; -.
FlyBase; FBgn0039102; SPE.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00870000136615; -.
KO; K20672; -.
OMA; VWNLTSC; -.
OrthoDB; EOG091G0DF7; -.
Reactome; R-DME-209442; Formation of the trans-membrane 'signalling complex'.
ChiTaRS; spen; fly.
GenomeRNAi; 42791; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0039102; -.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0004175; F:endopeptidase activity; IDA:FlyBase.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; ISM:FlyBase.
GO; GO:0006952; P:defense response; IMP:FlyBase.
GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:FlyBase.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
GO; GO:0006959; P:humoral immune response; IMP:FlyBase.
GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
GO; GO:0002804; P:positive regulation of antifungal peptide production; IMP:UniProtKB.
GO; GO:0006964; P:positive regulation of biosynthetic process of antibacterial peptides active against Gram-negative bacteria; IDA:FlyBase.
GO; GO:0006965; P:positive regulation of biosynthetic process of antibacterial peptides active against Gram-positive bacteria; IMP:UniProtKB.
GO; GO:0045752; P:positive regulation of Toll signaling pathway; IDA:FlyBase.
GO; GO:0006508; P:proteolysis; IDA:FlyBase.
GO; GO:0008592; P:regulation of Toll signaling pathway; IMP:UniProtKB.
GO; GO:0009620; P:response to fungus; IEP:FlyBase.
GO; GO:0008063; P:Toll signaling pathway; IDA:FlyBase.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 2.20.20.90; -; 1.
InterPro; IPR022700; CLIP.
InterPro; IPR038565; CLIP_sf.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF12032; CLIP; 1.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00680; CLIP; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Calcium; Complete proteome; Disulfide bond; Glycoprotein; Hydrolase;
Immunity; Innate immunity; Metal-binding; Protease;
Reference proteome; Secreted; Serine protease; Signal; Zymogen.
SIGNAL 1 27 {ECO:0000255}.
CHAIN 28 134 Spaetzle-processing enzyme light chain.
{ECO:0000305|PubMed:16399077}.
/FTId=PRO_5010149006.
CHAIN 135 400 Spaetzle-processing enzyme heavy chain.
{ECO:0000305|PubMed:16399077}.
/FTId=PRO_0000443328.
DOMAIN 35 94 CLIP. {ECO:0000255}.
DOMAIN 135 399 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 181 181 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
ACT_SITE 249 249 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
ACT_SITE 346 346 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
METAL 202 202 Calcium. {ECO:0000250|UniProtKB:O97366}.
METAL 204 204 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:O97366}.
METAL 207 207 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:O97366}.
METAL 210 210 Calcium. {ECO:0000250|UniProtKB:O97366}.
SITE 134 135 Cleavage. {ECO:0000269|PubMed:16399077}.
CARBOHYD 140 140 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 311 311 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 35 93 {ECO:0000250|UniProtKB:Q9VB68}.
DISULFID 52 94 {ECO:0000250|UniProtKB:Q9VB68}.
DISULFID 127 269 Interchain (between light and heavy
chains). {ECO:0000250|UniProtKB:Q9VB68}.
DISULFID 166 182 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 211 221 {ECO:0000250|UniProtKB:Q9VB68}.
DISULFID 315 332 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 342 375 {ECO:0000255|PROSITE-ProRule:PRU00274}.
MUTAGEN 134 134 R->A: Inhibits zymogen cleavage and thus
activation and spz processing.
{ECO:0000269|PubMed:16399077}.
SEQUENCE 400 AA; 43947 MW; E4492A4BC7316582 CRC64;
MASTERNFLL LSLVVSALSG LVHRSDAAEI SFGSCTPQQS DERGQCVHIT SCPYLANLLM
VEPKTPAQRI LLSKSQCGLD NRVEGLVNRI LVCCPQSMRG NIMDSEPTPS TRDALQQGDV
LPGNDVCGFL FADRIFGGTN TTLWEFPWMV LLQYKKLFSE TYTFNCGGAL LNSRYVLTAG
HCLASRELDK SGAVLHSVRL GEWDTRTDPD CTTQMNGQRI CAPKHIDIEV EKGIIHEMYA
PNSVDQRNDI ALVRLKRIVS YTDYVRPICL PTDGLVQNNF VDYGMDVAGW GLTENMQPSA
IKLKITVNVW NLTSCQEKYS SFKVKLDDSQ MCAGGQLGVD TCGGDSGGPL MVPISTGGRD
VFYIAGVTSY GTKPCGLKGW PGVYTRTGAF IDWIKQKLEP


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