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Serine protease persephone (EC 3.4.21.-)

 PSH_DROME               Reviewed;         394 AA.
Q9VWU1; A4V9U0; A4V9U1; A4V9U4; A4V9U7;
09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
20-DEC-2017, entry version 133.
RecName: Full=Serine protease persephone;
EC=3.4.21.-;
Flags: Precursor;
Name=psh {ECO:0000312|EMBL:AAF48846.1,
ECO:0000312|FlyBase:FBgn0030926}; ORFNames=CG6367;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION,
MUTAGENESIS OF HIS-187 AND GLY-341, AND DISRUPTION PHENOTYPE.
PubMed=12098703; DOI=10.1126/science.1072391;
Ligoxygakis P., Pelte N., Hoffmann J.A., Reichhart J.-M.;
"Activation of Drosophila Toll during fungal infection by a blood
serine protease.";
Science 297:114-116(2002).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-11; HIS-14 AND
PHE-18.
STRAIN=G124, G136, G145, G173, G179, G185, G186, G187, G191, and G193;
PubMed=17465907; DOI=10.1111/j.1420-9101.2007.01305.x;
Jiggins F.M., Kim K.W.;
"A screen for immunity genes evolving under positive selection in
Drosophila.";
J. Evol. Biol. 20:965-970(2007).
[3] {ECO:0000312|EMBL:AAF48846.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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).
[4] {ECO:0000305, ECO:0000312|EMBL:AAF48846.1}
GENOME REANNOTATION.
STRAIN=Berkeley;
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).
[5] {ECO:0000305, ECO:0000312|EMBL:AAM27491.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley {ECO:0000312|EMBL:AAM27491.1};
TISSUE=Head {ECO:0000269|PubMed:12537569};
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).
[6]
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-187.
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).
[7]
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-187.
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]
MUTAGENESIS OF HIS-187.
PubMed=21576362; DOI=10.1128/MCB.01397-10;
Fullaondo A., Garcia-Sanchez S., Sanz-Parra A., Recio E., Lee S.Y.,
Gubb D.;
"Spn1 regulates the GNBP3-dependent Toll signaling pathway in
Drosophila melanogaster.";
Mol. Cell. Biol. 31:2960-2972(2011).
-!- FUNCTION: Serine protease that plays a key role in innate immunity
in response to Gram-positive bacterial and fungal proteases
(PubMed:12098703, PubMed:18724373, PubMed:16399077). Acts as a
component of the Toll pathway upstream of protease spz processing
enzyme SPE and Tl ligand spz (PubMed:12098703, PubMed:18724373,
PubMed:16399077). Nec regulates the cascade by inhibiting psh
(PubMed:12098703). {ECO:0000269|PubMed:12098703,
ECO:0000269|PubMed:16399077, ECO:0000269|PubMed:18724373}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12098703}.
-!- 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:0000250|UniProtKB:Q9VB68}.
-!- DISRUPTION PHENOTYPE: Increased susceptibility to fungal infection
and failure to induce the expression of antifungal peptide Drs in
response to fungal infection but not in response to E.coli or
M.luteus bacterial infection. {ECO:0000269|PubMed:12098703,
ECO:0000269|PubMed:16399077, ECO:0000269|PubMed:18724373}.
-!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AM412840; CAL85463.1; -; Genomic_DNA.
EMBL; AM412841; CAL85464.1; -; Genomic_DNA.
EMBL; AM412842; CAL85465.1; -; Genomic_DNA.
EMBL; AM412843; CAL85466.1; -; Genomic_DNA.
EMBL; AM412844; CAL85467.1; -; Genomic_DNA.
EMBL; AM412845; CAL85468.1; -; Genomic_DNA.
EMBL; AM412846; CAL85469.1; -; Genomic_DNA.
EMBL; AM412847; CAL85470.1; -; Genomic_DNA.
EMBL; AM412848; CAL85471.1; -; Genomic_DNA.
EMBL; AM412849; CAL85472.1; -; Genomic_DNA.
EMBL; AE014298; AAF48846.1; -; Genomic_DNA.
EMBL; AY102662; AAM27491.1; -; mRNA.
RefSeq; NP_573297.1; NM_133069.2.
UniGene; Dm.18653; -.
ProteinModelPortal; Q9VWU1; -.
BioGrid; 59145; 3.
STRING; 7227.FBpp0074400; -.
MEROPS; S01.421; -.
PaxDb; Q9VWU1; -.
PRIDE; Q9VWU1; -.
EnsemblMetazoa; FBtr0074629; FBpp0074400; FBgn0030926.
GeneID; 32832; -.
KEGG; dme:Dmel_CG6367; -.
UCSC; CG6367-RA; d. melanogaster.
CTD; 32832; -.
FlyBase; FBgn0030926; psh.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00840000130336; -.
InParanoid; Q9VWU1; -.
KO; K20671; -.
OMA; CCPTKPC; -.
OrthoDB; EOG091G0DF7; -.
PhylomeDB; Q9VWU1; -.
GenomeRNAi; 32832; -.
PRO; PR:Q9VWU1; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0030926; -.
ExpressionAtlas; Q9VWU1; differential.
Genevisible; Q9VWU1; DM.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0008233; F:peptidase activity; IMP:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; ISM:FlyBase.
GO; GO:0071219; P:cellular response to molecule of bacterial origin; IMP:UniProtKB.
GO; GO:0006952; P:defense response; IGI:FlyBase.
GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
GO; GO:0045087; P:innate immune response; IDA:FlyBase.
GO; GO:0006967; P:positive regulation of antifungal peptide biosynthetic process; IMP:FlyBase.
GO; GO:0002804; P:positive regulation of antifungal peptide production; IMP:UniProtKB.
GO; GO:0045752; P:positive regulation of Toll signaling pathway; IMP:UniProtKB.
GO; GO:0006508; P:proteolysis; IMP:UniProtKB.
GO; GO:0008592; P:regulation of Toll signaling pathway; IMP:UniProtKB.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR022700; CLIP.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
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;
Complete proteome; Disulfide bond; Glycoprotein; Hydrolase; Immunity;
Innate immunity; Protease; Reference proteome; Secreted;
Serine protease; Signal.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 394 Serine protease persephone.
{ECO:0000255}.
/FTId=PRO_0000271766.
DOMAIN 30 79 CLIP. {ECO:0000255}.
DOMAIN 144 389 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 187 187 Charge relay system. {ECO:0000255}.
ACT_SITE 234 234 Charge relay system. {ECO:0000255}.
ACT_SITE 339 339 Charge relay system. {ECO:0000255}.
CARBOHYD 86 86 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 277 277 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 301 301 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 30 77 {ECO:0000250|UniProtKB:Q9VB68}.
DISULFID 40 67 {ECO:0000250|UniProtKB:Q9VB68}.
DISULFID 46 78 {ECO:0000250|UniProtKB:Q9VB68}.
DISULFID 125 254 {ECO:0000250|UniProtKB:Q9VB68}.
DISULFID 172 188 {ECO:0000250|UniProtKB:Q9VB68}.
DISULFID 300 324 {ECO:0000250|UniProtKB:Q9VB68}.
DISULFID 335 366 {ECO:0000250|UniProtKB:Q9VB68}.
VARIANT 11 11 T -> I (in strain: G187).
{ECO:0000269|PubMed:17465907}.
VARIANT 14 14 L -> H (in strain: G136).
{ECO:0000269|PubMed:17465907}.
VARIANT 18 18 S -> F (in strain: G179).
{ECO:0000269|PubMed:17465907}.
MUTAGEN 187 187 H->Y: In psh1 and psh4; immune response
defective. Reduced levels of Drs
following immune challenge with fungal or
bacterial proteases.
{ECO:0000269|PubMed:12098703,
ECO:0000269|PubMed:16399077,
ECO:0000269|PubMed:18724373,
ECO:0000269|PubMed:21576362}.
MUTAGEN 341 341 G->E: In psh5; immune response defective.
{ECO:0000269|PubMed:12098703}.
SEQUENCE 394 AA; 42228 MW; 92D55383E459736E CRC64;
MPLKWSLLLG TFVLISCSSV EAAVTVGRAC KVTDTMPGIC RTSSDCEPLI DGYIKSGVLT
LNDVPSCGLG AWGEIFCCPT KPCCDNSTIT SVSTSSTTST KAPMTSGRVD VPTFGSGDRP
AVAACKKIRE RKQQRSGNQL VIHIVGGYPV DPGVYPHMAA IGYITFGTDF RCGGSLIASR
FVLTAAHCVN TDANTPAFVR LGAVNIENPD HSYQDIVIRS VKIHPQYVGN KYNDIAILEL
ERDVVETDNI RPACLHTDAT DPPSNSKFFV AGWGVLNVTT RARSKILLRA GLELVPLDQC
NISYAEQPGS IRLLKQGVID SLLCAIDQKL IADACKGDSG GPLIHELNVE DGMYTIMGVI
SSGFGCATVT PGLYTRVSSY LDFIEGIVWP DNRV


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