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SER1_DROME
ID   SER1_DROME              Reviewed;         265 AA.
AC   C0HKF7; P17205; Q23988; Q9VAD9; Q9VAE0;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2017, sequence version 1.
DT   03-AUG-2022, entry version 21.
DE   RecName: Full=Serine protease 1 {ECO:0000303|PubMed:2469005};
DE            EC=3.4.21.-;
DE   AltName: Full=Protein Jonah 99Cii {ECO:0000305};
DE   Flags: Precursor;
GN   Name=Jon99Cii {ECO:0000312|FlyBase:FBgn0003356};
GN   Synonyms=SER1 {ECO:0000303|PubMed:2469005},
GN   Ser99Da {ECO:0000312|FlyBase:FBgn0003356};
GN   ORFNames=CG7877 {ECO:0000312|FlyBase:FBgn0003356};
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=Canton-S;
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).
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 72-219.
RA   Elvin C.M., Bunch R., Vuocolo T., Hemingway J., Smith W.J., Riddles P.W.;
RT   "Serine protease genes expressed in haematophagous insects.";
RL   Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Major function may be to aid in digestion.
CC       {ECO:0000303|PubMed:2469005}.
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in the larval gut.
CC       {ECO:0000269|PubMed:2469005}.
CC   -!- DEVELOPMENTAL STAGE: Expression appears at the late embryo stage and
CC       continues to increase in abundance throughout the larval stage. No
CC       expression in pupae but is expressed 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; M24379; AAB02552.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAF56972.1; -; Genomic_DNA.
DR   EMBL; U09800; AAA18625.1; -; mRNA.
DR   PIR; JS0260; JS0260.
DR   RefSeq; NP_001287598.1; NM_001300669.1.
DR   RefSeq; NP_524554.1; NM_079830.4.
DR   RefSeq; NP_733330.1; NM_170451.3.
DR   AlphaFoldDB; C0HKF7; -.
DR   SMR; C0HKF7; -.
DR   STRING; 7227.FBpp0084868; -.
DR   PRIDE; C0HKF7; -.
DR   DNASU; 43544; -.
DR   EnsemblMetazoa; FBtr0085502; FBpp0084868; FBgn0003357.
DR   EnsemblMetazoa; FBtr0085512; FBpp0084878; FBgn0003356.
DR   EnsemblMetazoa; FBtr0346340; FBpp0312057; FBgn0003357.
DR   GeneID; 43543; -.
DR   GeneID; 43544; -.
DR   KEGG; dme:Dmel_CG31034; -.
DR   KEGG; dme:Dmel_CG31362; -.
DR   CTD; 43543; -.
DR   CTD; 43544; -.
DR   FlyBase; FBgn0003356; Jon99Cii.
DR   VEuPathDB; VectorBase:FBgn0003356; -.
DR   VEuPathDB; VectorBase:FBgn0003357; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   OMA; MICINTE; -.
DR   OrthoDB; 1522379at2759; -.
DR   ChiTaRS; Spn43Aa; fly.
DR   PRO; PR:C0HKF7; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0003356; Expressed in midgut and 13 other tissues.
DR   ExpressionAtlas; C0HKF7; baseline and differential.
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..21
FT                   /evidence="ECO:0000305"
FT   PROPEP          22..35
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000440557"
FT   CHAIN           36..265
FT                   /note="Serine protease 1"
FT                   /id="PRO_0000440558"
FT   DOMAIN          36..262
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        78
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        123
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        215
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        63..79
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        189..201
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        211..239
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CONFLICT        74
FT                   /note="L -> V (in Ref. 4; AAA18625)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        181
FT                   /note="V -> A (in Ref. 4; AAA18625)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        187
FT                   /note="S -> R (in Ref. 4; AAA18625)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        215
FT                   /note="S -> T (in Ref. 4; AAA18625)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   265 AA;  28469 MW;  44848C523F03384B CRC64;
     MKLFVFLALA VAAATAVPAP AQKLTPTPIK DIQGRITNGY PAYEGKVPYI VGLLFSGNGN
     WWCGGSIIGN TWVLTAAHCT NGASGVTINY GASIRTQPQY THWVGSGDII QHHHYNSGNL
     HNDISLIRTP HVDFWSLVNK VELPSYNDRY QDYAGWWAVA SGWGGTYDGS PLPDWLQSVD
     VQIISQSDCS RTWSLHDNMI CINTDGGKST CGGDSGGPLV THDGNRLVGV TSFGSAAGCQ
     SGAPAVFSRV TGYLDWIRDN TGISY
 
 
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