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SER3_DROME
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   03-AUG-2022, entry version 154.
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}.
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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; P17207; -.
DR   PRIDE; P17207; -.
DR   DNASU; 43545; -.
DR   EnsemblMetazoa; FBtr0085511; FBpp0084877; FBgn0003358.
DR   GeneID; 43545; -.
DR   KEGG; dme:Dmel_CG31039; -.
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; 1522379at2759; -.
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 tissues.
DR   Genevisible; P17207; DM.
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; -; 2.
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; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 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
 
 
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