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 15-JUN-2010, entry version 92. 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; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; 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., 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.L., 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.J., 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.C., Zhu X., RA Smith H.O., 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 GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; 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., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., 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 RP SPECIFICITY, AND DEVELOPMENTAL STAGE. 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 the peptidase S1 family. CC -!- SIMILARITY: Contains 1 peptidase S1 domain. 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; -. DR UniGene; Dm.5661; -. DR SMR; P17207; 41-272. DR STRING; P17207; -. DR MEROPS; S01.168; -. DR EnsemblMetazoa; FBtr0085511; FBpp0084877; FBgn0003358. DR GeneID; 43545; -. DR KEGG; dme:Dmel_CG31039; -. DR NMPDR; fig|7227.3.peg.15335; -. DR CTD; 43545; -. DR FlyBase; FBgn0003358; Jon99Ci. DR eggNOG; meNOG25599; -. DR InParanoid; P17207; -. DR OMA; ASENTIC; -. DR OrthoDB; EOG9CZBNM; -. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-014064-MONOMER; -. DR NextBio; 834472; -. DR Bgee; P17207; -. DR GermOnline; CG31039; Drosophila melanogaster. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; NAS:FlyBase. DR InterPro; IPR018114; Peptidase_S1/S6_AS. DR InterPro; IPR001254; Peptidase_S1_S6. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR009003; Ser/Cys_Pept_Trypsin-like. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF50494; Pept_Ser_Cys; 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 Complete proteome; Disulfide bond; Hydrolase; Protease; KW Serine protease; Signal; Zymogen. FT SIGNAL 1 17 Potential. FT PROPEP 18 40 By similarity. FT /FTId=PRO_0000028139. FT CHAIN 41 272 Serine protease 3. FT /FTId=PRO_0000028140. FT DOMAIN 41 269 Peptidase S1. 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. 4; AAB02551). 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 //