SP42D_DROME
ID SP42D_DROME Reviewed; 372 AA.
AC Q7YTY6; Q7KA42;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Serine protease inhibitor 42Dd {ECO:0000303|PubMed:10692585};
DE Short=Serpin 42Dd {ECO:0000312|FlyBase:FBgn0028988};
DE Flags: Precursor;
GN Name=Spn42Dd {ECO:0000312|FlyBase:FBgn0028988};
GN Synonyms=Spn1 {ECO:0000303|PubMed:10692585};
GN ORFNames=CG9456 {ECO:0000312|FlyBase:FBgn0028988};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:CAB63096.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10692585; DOI=10.1016/s0014-5793(00)01224-2;
RA Han J.H., Zhang H., Min G.S., Hashimoto C.;
RT "A novel Drosophila serpin that inhibits serine proteases.";
RL FEBS Lett. 468:194-198(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [3] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [4] {ECO:0000312|EMBL:AAQ22579.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAQ22579.1};
RC TISSUE=Head {ECO:0000312|EMBL:AAQ22579.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, INDUCTION BY MICROORGANISMS, AND DISRUPTION PHENOTYPE.
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 inhibitor with activity toward trypsin.
CC Involved in innate immunity to fungal infection by negatively
CC regulating the Toll signaling pathway and suppressing the expression of
CC the antifungal peptide drosomycin. Acts upstream of SPE and grass, and
CC downstream of the fungal cell wall pattern recognition receptor GNBP3.
CC May function specifically in the GNBP3-dependent beta-1,3-glucan branch
CC of the Toll pathway. {ECO:0000269|PubMed:21576362}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the ovary.
CC {ECO:0000269|PubMed:10692585}.
CC -!- INDUCTION: Up-regulated by the Gram-positive bacterium M.luteus, the
CC fungus B.bassiana and the yeast C.albicans.
CC {ECO:0000269|PubMed:21576362}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in the
CC constitutive expression of Drs. {ECO:0000269|PubMed:21576362}.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR EMBL; AJ251744; CAB63096.1; -; mRNA.
DR EMBL; AE013599; ACZ94347.1; -; Genomic_DNA.
DR EMBL; BT010110; AAQ22579.1; -; mRNA.
DR RefSeq; NP_001163067.1; NM_001169596.3.
DR AlphaFoldDB; Q7YTY6; -.
DR SMR; Q7YTY6; -.
DR IntAct; Q7YTY6; 2.
DR STRING; 7227.FBpp0289586; -.
DR MEROPS; I04.038; -.
DR GlyGen; Q7YTY6; 2 sites.
DR PaxDb; Q7YTY6; -.
DR PRIDE; Q7YTY6; -.
DR DNASU; 49808; -.
DR EnsemblMetazoa; FBtr0300357; FBpp0289586; FBgn0028988.
DR GeneID; 49808; -.
DR KEGG; dme:Dmel_CG9456; -.
DR UCSC; CG9456-RA; d. melanogaster.
DR CTD; 49808; -.
DR FlyBase; FBgn0028988; Spn42Dd.
DR VEuPathDB; VectorBase:FBgn0028988; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000166714; -.
DR HOGENOM; CLU_023330_0_2_1; -.
DR InParanoid; Q7YTY6; -.
DR OMA; MGMHSAF; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; Q7YTY6; -.
DR Reactome; R-DME-114608; Platelet degranulation.
DR Reactome; R-DME-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-DME-140875; Common Pathway of Fibrin Clot Formation.
DR Reactome; R-DME-194002; Glucocorticoid biosynthesis.
DR Reactome; R-DME-204005; COPII-mediated vesicle transport.
DR Reactome; R-DME-3000178; ECM proteoglycans.
DR Reactome; R-DME-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-DME-5694530; Cargo concentration in the ER.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 49808; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 49808; -.
DR PRO; PR:Q7YTY6; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0028988; Expressed in oviduct (Drosophila) and 20 other tissues.
DR GO; GO:0005615; C:extracellular space; HDA:FlyBase.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:FlyBase.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:1905035; P:negative regulation of antifungal innate immune response; IMP:FlyBase.
DR GO; GO:0002785; P:negative regulation of antimicrobial peptide production; IMP:FlyBase.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IDA:FlyBase.
DR GO; GO:0045861; P:negative regulation of proteolysis; ISM:FlyBase.
DR GO; GO:0045751; P:negative regulation of Toll signaling pathway; IDA:FlyBase.
DR GO; GO:0019953; P:sexual reproduction; HEP:FlyBase.
DR Gene3D; 2.30.39.10; -; 1.
DR Gene3D; 3.30.497.10; -; 1.
DR InterPro; IPR015557; Serpin_B1.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR000215; Serpin_fam.
DR InterPro; IPR036186; Serpin_sf.
DR InterPro; IPR042178; Serpin_sf_1.
DR InterPro; IPR042185; Serpin_sf_2.
DR PANTHER; PTHR11461; PTHR11461; 1.
DR PANTHER; PTHR11461:SF180; PTHR11461:SF180; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Immunity; Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..372
FT /note="Serine protease inhibitor 42Dd"
FT /evidence="ECO:0000255"
FT /id="PRO_0000436914"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 26
FT /note="S -> C (in Ref. 1; CAB63096)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 372 AA; 41179 MW; FD2BB1C9D8F3DDDC CRC64;
MYYLCIFLWV TSVACQTSKE IYQLLSKSHT NQNLVVSPVS IETILSMVFM GAEGSTAKEL
QSALGLPSED KEAVAARYGA LLNDLQGQEE GPILKLANRI YVNDQYSLNQ NYNLAVREPF
KSEAESISLT NGPVAAERIN QWVLDQTSGK IKGMIDPGSM TSDVKALLVN AIYFKGQWES
KFDPAKTRAS TFQVTANKSV PVQMMAQMGT FRANYFRDLD AQVIELPYLN SNLSMTIFLP
REVEGLSALE EKIVGFARPL VAKEVYLKLP KFKIEFRDEL KETLEKLGIR ELFTDKSDLS
GLFADKSGGK VSQVSHKAFL EVNEEGAEAA GATSVAVTNR AGFSTFLMAD HPFAFVIRDA
NTIYFQGRVV SP
