SER2_DROME
ID SER2_DROME Reviewed; 265 AA.
AC C0HKF8; 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 18.
DE RecName: Full=Serine protease 2 {ECO:0000303|PubMed:2469005};
DE EC=3.4.21.-;
DE AltName: Full=Protein Jonah 99Ciii {ECO:0000305};
DE Flags: Precursor;
GN Name=Jon99Ciii {ECO:0000312|FlyBase:FBgn0003357};
GN Synonyms=SER2 {ECO:0000303|PubMed:2469005},
GN Ser99Db {ECO:0000312|FlyBase:FBgn0003357};
GN ORFNames=CG15519 {ECO:0000312|FlyBase:FBgn0003357};
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; AAB02553.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN14201.1; -; Genomic_DNA.
DR EMBL; U09800; AAA18625.1; -; mRNA.
DR PIR; A38894; A38894.
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; C0HKF8; -.
DR SMR; C0HKF8; -.
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; FBgn0003357; Jon99Ciii.
DR VEuPathDB; VectorBase:FBgn0003356; -.
DR VEuPathDB; VectorBase:FBgn0003357; -.
DR GeneTree; ENSGT00840000130082; -.
DR OMA; MICINTE; -.
DR OrthoDB; 1522379at2759; -.
DR PRO; PR:C0HKF8; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003356; Expressed in midgut and 13 other tissues.
DR ExpressionAtlas; C0HKF8; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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_0000028137"
FT CHAIN 36..265
FT /note="Serine protease 2"
FT /id="PRO_0000028138"
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 14
FT /note="A -> T (in Ref. 1; AAB02553)"
FT /evidence="ECO:0000305"
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
