ID SER3_DROME Reviewed; 272 AA. AC P17207; Q9VAD8; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 24-JUL-2024, entry version 161. DE RecName: Full=Serine protease 3; DE EC=3.4.21.-; DE AltName: Full=Protein Jonah 99Ci; DE Flags: Precursor; GN Name=Jon99Ci; Synonyms=SER3, Ser99Dc; ORFNames=CG17951; 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 [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 [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 212-272, FUNCTION, TISSUE SPECIFICITY, RP AND DEVELOPMENTAL STAGE. RX PubMed=2469005; DOI=10.1128/mcb.9.2.692-700.1989; RA Yun Y., Davis R.L.; RT "Levels of RNA from a family of putative serine protease genes are reduced RT in Drosophila melanogaster dunce mutants and are regulated by cyclic AMP."; RL Mol. Cell. Biol. 9:692-700(1989). CC -!- FUNCTION: Its major function may be to aid in digestion. CC {ECO:0000269|PubMed:2469005}. CC -!- TISSUE SPECIFICITY: Abundantly expressed in the larval gut. CC {ECO:0000269|PubMed:2469005}. CC -!- DEVELOPMENTAL STAGE: Began to appear at late embryo stage and continued CC to increase in abundance throughout the larval stage. They are not CC present in pupae but reappeared in the adult. CC {ECO:0000269|PubMed:2469005}. CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE- CC ProRule:PRU00274}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE014297; AAF56973.1; -; Genomic_DNA. DR EMBL; AY070605; AAL48076.1; -; mRNA. DR EMBL; M24380; AAB02551.1; -; Genomic_DNA. DR PIR; PS0049; PS0049. DR RefSeq; NP_524555.1; NM_079831.4. DR AlphaFoldDB; P17207; -. DR SMR; P17207; -. DR STRING; 7227.FBpp0084877; -. DR MEROPS; S01.B24; -. DR PaxDb; 7227-FBpp0084877; -. DR DNASU; 43545; -. DR EnsemblMetazoa; FBtr0085511; FBpp0084877; FBgn0003358. DR GeneID; 43545; -. DR KEGG; dme:Dmel_CG31039; -. DR AGR; FB:FBgn0003358; -. DR CTD; 43545; -. DR FlyBase; FBgn0003358; Jon99Ci. DR VEuPathDB; VectorBase:FBgn0003358; -. DR eggNOG; KOG3627; Eukaryota. DR GeneTree; ENSGT00840000130082; -. DR HOGENOM; CLU_006842_7_6_1; -. DR InParanoid; P17207; -. DR OMA; AFIRYPE; -. DR OrthoDB; 2917484at2759; -. DR PhylomeDB; P17207; -. DR BioGRID-ORCS; 43545; 0 hits in 1 CRISPR screen. DR GenomeRNAi; 43545; -. DR PRO; PR:P17207; -. DR Proteomes; UP000000803; Chromosome 3R. DR Bgee; FBgn0003358; Expressed in adult midgut (Drosophila) and 15 other cell types or tissues. DR GO; GO:0004175; F:endopeptidase activity; ISM:FlyBase. DR GO; GO:0017171; F:serine hydrolase activity; HDA:FlyBase. DR GO; GO:0004252; F:serine-type endopeptidase activity; ISM:FlyBase. DR GO; GO:0006508; P:proteolysis; ISM:FlyBase. DR CDD; cd00190; Tryp_SPc; 1. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2. DR InterPro; IPR051333; CLIP_Serine_Protease. 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 PANTHER; PTHR24260; -; 1. DR PANTHER; PTHR24260:SF134; AT07769P-RELATED; 1. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. PE 2: Evidence at transcript level; KW Disulfide bond; Hydrolase; Protease; Reference proteome; Serine protease; KW Signal; Zymogen. FT SIGNAL 1..17 FT /evidence="ECO:0000255" FT PROPEP 18..40 FT /evidence="ECO:0000250" FT /id="PRO_0000028139" FT CHAIN 41..272 FT /note="Serine protease 3" FT /id="PRO_0000028140" FT DOMAIN 41..269 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT ACT_SITE 84 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 127 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 222 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT DISULFID 69..85 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 193..208 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 218..246 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT CONFLICT 212 FT /note="P -> M (in Ref. 4; AAB02551)" FT /evidence="ECO:0000305" SQ SEQUENCE 272 AA; 29620 MW; A61E9DE3AFCA93AF CRC64; MRGLTLLSLA FLGVCSALTV PHSLVHPRDL EIRHGGIEGR ITNGNLASEG QVPYIVGVSL NSNGNWWWCG GSIIGHTWVL TAAHCTAGAD EASLYYGAVN YNEPAFRHTV SSENFIRYPH YVGLDHDLAL IKTPHVDFYS LVNKIELPSL DDRYNSYENN WVQAAGWGAI YDGSNVVEDL RVVDLKVISV AECQAYYGTD TASENTICVE TPDGKATCQG DSGGPLVTKE GDKLIGITSF VSAYGCQVGG PAGFTRVTKY LEWIKEETGI YY //