PSH_DROME
ID PSH_DROME Reviewed; 394 AA.
AC Q9VWU1; A4V9U0; A4V9U1; A4V9U4; A4V9U7;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Serine protease persephone;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=psh {ECO:0000312|EMBL:AAF48846.1, ECO:0000312|FlyBase:FBgn0030926};
GN ORFNames=CG6367;
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP HIS-187 AND GLY-341, AND DISRUPTION PHENOTYPE.
RX PubMed=12098703; DOI=10.1126/science.1072391;
RA Ligoxygakis P., Pelte N., Hoffmann J.A., Reichhart J.-M.;
RT "Activation of Drosophila Toll during fungal infection by a blood serine
RT protease.";
RL Science 297:114-116(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-11; HIS-14 AND PHE-18.
RC STRAIN=G124, G136, G145, G173, G179, G185, G186, G187, G191, and G193;
RX PubMed=17465907; DOI=10.1111/j.1420-9101.2007.01305.x;
RA Jiggins F.M., Kim K.W.;
RT "A screen for immunity genes evolving under positive selection in
RT Drosophila.";
RL J. Evol. Biol. 20:965-970(2007).
RN [3] {ECO:0000312|EMBL:AAF48846.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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] {ECO:0000305, ECO:0000312|EMBL:AAF48846.1}
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 [5] {ECO:0000305, ECO:0000312|EMBL:AAM27491.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM27491.1};
RC TISSUE=Head {ECO:0000269|PubMed:12537569};
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 FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-187.
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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-187.
RX PubMed=18724373; DOI=10.1038/ni.1643;
RA El Chamy L., Leclerc V., Caldelari I., Reichhart J.M.;
RT "Sensing of 'danger signals' and pathogen-associated molecular patterns
RT defines binary signaling pathways 'upstream' of Toll.";
RL Nat. Immunol. 9:1165-1170(2008).
RN [8]
RP MUTAGENESIS OF HIS-187.
RX PubMed=21576362; DOI=10.1128/mcb.01397-10;
RA Fullaondo A., Garcia-Sanchez S., Sanz-Parra A., Recio E., Lee S.Y.,
RA Gubb D.;
RT "Spn1 regulates the GNBP3-dependent Toll signaling pathway in Drosophila
RT melanogaster.";
RL Mol. Cell. Biol. 31:2960-2972(2011).
CC -!- FUNCTION: Serine protease that plays a key role in innate immunity in
CC response to Gram-positive bacterial and fungal proteases
CC (PubMed:12098703, PubMed:18724373, PubMed:16399077). Acts as a
CC component of the Toll pathway upstream of protease spz processing
CC enzyme SPE and Tl ligand spz (PubMed:12098703, PubMed:18724373,
CC PubMed:16399077). Nec regulates the cascade by inhibiting psh
CC (PubMed:12098703). {ECO:0000269|PubMed:12098703,
CC ECO:0000269|PubMed:16399077, ECO:0000269|PubMed:18724373}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12098703}.
CC -!- DOMAIN: The clip domain consists of 35-55 residues which are 'knitted'
CC together usually by 3 conserved disulfide bonds forming a clip-like
CC compact structure. {ECO:0000255|PROSITE-ProRule:PRU01236}.
CC -!- DISRUPTION PHENOTYPE: Increased susceptibility to fungal infection and
CC failure to induce the expression of antifungal peptide Drs in response
CC to fungal infection but not in response to E.coli or M.luteus bacterial
CC infection. {ECO:0000269|PubMed:12098703, ECO:0000269|PubMed:16399077,
CC ECO:0000269|PubMed:18724373}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01236}.
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DR EMBL; AM412840; CAL85463.1; -; Genomic_DNA.
DR EMBL; AM412841; CAL85464.1; -; Genomic_DNA.
DR EMBL; AM412842; CAL85465.1; -; Genomic_DNA.
DR EMBL; AM412843; CAL85466.1; -; Genomic_DNA.
DR EMBL; AM412844; CAL85467.1; -; Genomic_DNA.
DR EMBL; AM412845; CAL85468.1; -; Genomic_DNA.
DR EMBL; AM412846; CAL85469.1; -; Genomic_DNA.
DR EMBL; AM412847; CAL85470.1; -; Genomic_DNA.
DR EMBL; AM412848; CAL85471.1; -; Genomic_DNA.
DR EMBL; AM412849; CAL85472.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF48846.1; -; Genomic_DNA.
DR EMBL; AY102662; AAM27491.1; -; mRNA.
DR RefSeq; NP_573297.1; NM_133069.2.
DR AlphaFoldDB; Q9VWU1; -.
DR SMR; Q9VWU1; -.
DR BioGRID; 59145; 3.
DR STRING; 7227.FBpp0074400; -.
DR MEROPS; S01.421; -.
DR GlyGen; Q9VWU1; 3 sites.
DR PaxDb; Q9VWU1; -.
DR PRIDE; Q9VWU1; -.
DR DNASU; 32832; -.
DR EnsemblMetazoa; FBtr0074629; FBpp0074400; FBgn0030926.
DR GeneID; 32832; -.
DR KEGG; dme:Dmel_CG6367; -.
DR UCSC; CG6367-RA; d. melanogaster.
DR CTD; 32832; -.
DR FlyBase; FBgn0030926; psh.
DR VEuPathDB; VectorBase:FBgn0030926; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000168826; -.
DR HOGENOM; CLU_006842_0_3_1; -.
DR InParanoid; Q9VWU1; -.
DR OMA; LICAMAM; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q9VWU1; -.
DR BioGRID-ORCS; 32832; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 32832; -.
DR PRO; PR:Q9VWU1; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030926; Expressed in capitellum (Drosophila) and 13 other tissues.
DR ExpressionAtlas; Q9VWU1; baseline and differential.
DR Genevisible; Q9VWU1; DM.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; IMP:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IMP:FlyBase.
DR GO; GO:0061760; P:antifungal innate immune response; IMP:FlyBase.
DR GO; GO:0071219; P:cellular response to molecule of bacterial origin; IMP:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR GO; GO:0006963; P:positive regulation of antibacterial peptide biosynthetic process; IMP:FlyBase.
DR GO; GO:0002804; P:positive regulation of antifungal peptide production; IMP:UniProtKB.
DR GO; GO:0035008; P:positive regulation of melanization defense response; IGI:FlyBase.
DR GO; GO:0045752; P:positive regulation of Toll signaling pathway; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IMP:UniProtKB.
DR GO; GO:0008592; P:regulation of Toll signaling pathway; IMP:UniProtKB.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR InterPro; IPR022700; CLIP.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00680; CLIP; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS51888; CLIP; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Immunity; Innate immunity;
KW Protease; Reference proteome; Secreted; Serine protease; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..394
FT /note="Serine protease persephone"
FT /evidence="ECO:0000255"
FT /id="PRO_0000271766"
FT DOMAIN 29..78
FT /note="Clip"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DOMAIN 144..389
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 187
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 234
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 339
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..77
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DISULFID 40..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DISULFID 46..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DISULFID 125..254
FT /evidence="ECO:0000250|UniProtKB:Q9VB68"
FT DISULFID 172..188
FT /evidence="ECO:0000250|UniProtKB:Q9VB68"
FT DISULFID 300..324
FT /evidence="ECO:0000250|UniProtKB:Q9VB68"
FT DISULFID 335..366
FT /evidence="ECO:0000250|UniProtKB:Q9VB68"
FT VARIANT 11
FT /note="T -> I (in strain: G187)"
FT /evidence="ECO:0000269|PubMed:17465907"
FT VARIANT 14
FT /note="L -> H (in strain: G136)"
FT /evidence="ECO:0000269|PubMed:17465907"
FT VARIANT 18
FT /note="S -> F (in strain: G179)"
FT /evidence="ECO:0000269|PubMed:17465907"
FT MUTAGEN 187
FT /note="H->Y: In psh1 and psh4; immune response defective.
FT Reduced levels of Drs following immune challenge with
FT fungal or bacterial proteases."
FT /evidence="ECO:0000269|PubMed:12098703,
FT ECO:0000269|PubMed:16399077, ECO:0000269|PubMed:18724373,
FT ECO:0000269|PubMed:21576362"
FT MUTAGEN 341
FT /note="G->E: In psh5; immune response defective."
FT /evidence="ECO:0000269|PubMed:12098703"
SQ 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
