ID SER3_DROME STANDARD; PRT; 272 AA. AC P17207; Q9VAD8; DT 01-AUG-1990 (Rel. 15, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Serine protease 3 precursor (EC 3.4.21.-). GN SER99DC OR SER3 OR CG17951. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; 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., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA 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., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP SEQUENCE OF 212-272 FROM N.A. RX MEDLINE=89219063; PubMed=2469005; RA Yun Y., Davis R.L.; RT "Levels of RNA from a family of putative serine protease genes are RT reduced in Drosophila melanogaster dunce mutants and are regulated by RT cyclic AMP."; RL Mol. Cell. Biol. 9:692-700(1989). CC -!- FUNCTION: Its major function may be to aid in digestion. CC -!- TISSUE SPECIFICITY: Abundantly expressed in the larval gut. CC -!- DEVELOPMENTAL STAGE: Began to appear at late embryo stage and CC continued to increase in abundance throughout the larval stage. CC They are not present in pupae but reappeared in the adult. CC -!- SIMILARITY: Belongs to peptidase family S1. 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; AE003771; AAF56973.1; -. DR EMBL; M24380; AAB02551.1; -. DR PIR; PS0049; PS0049. DR HSSP; P08897; 2HLC. DR MEROPS; S01.UPA; -. DR FlyBase; FBgn0003358; Ser99Dc. DR GO; GO:0042708; F:elastase activity; NAS. DR GO; GO:0006508; P:proteolysis and peptidolysis; NAS. DR InterPro; IPR009003; Cys_Ser_trypsin. DR InterPro; IPR001254; Peptidase_S1. DR InterPro; IPR001314; Peptidase_S1A. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. KW Hydrolase; Serine protease; Signal; Zymogen; Multigene family. FT SIGNAL 1 17 Potential. FT PROPEP 18 40 By similarity. FT CHAIN 41 272 Serine protease 3. FT ACT_SITE 84 84 Charge relay system (By similarity). FT ACT_SITE 127 127 Charge relay system (By similarity). FT ACT_SITE 222 222 Charge relay system (By similarity). FT DISULFID 69 85 By similarity. FT DISULFID 193 208 By similarity. FT DISULFID 218 246 By similarity. FT CONFLICT 212 212 P -> M (in Ref. 2). 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 //