ID   TRYA_DROME              Reviewed;         256 AA.
AC   P04814; Q541G0; Q9V5Y2;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   24-JAN-2024, entry version 185.
DE   RecName: Full=Trypsin alpha;
DE            EC=3.4.21.4;
DE   Flags: Precursor;
GN   Name=alphaTry; Synonyms=TRY-ALPHA; ORFNames=CG18444;
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], SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=2414727; DOI=10.1093/nar/13.18.6605;
RA   Davis C.A., Riddell D.C., Higgins M.J., Holden J.J.A., White B.N.;
RT   "A gene family in Drosophila melanogaster coding for trypsin-like
RT   enzymes.";
RL   Nucleic Acids Res. 13:6605-6619(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10486967; DOI=10.1093/oxfordjournals.molbev.a026202;
RA   Wang S., Magoulas C., Hickey D.A.;
RT   "Concerted evolution within a trypsin gene cluster in Drosophila.";
RL   Mol. Biol. Evol. 16:1117-1124(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Oregon-R;
RA   Wang S., Magoulas C., Hickey D.A.;
RL   Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000269|PubMed:2414727}.
CC   -!- TISSUE SPECIFICITY: Synthesized in the midgut of both larvae and
CC       adults, primarily in the ventriculus and gastric caeca.
CC       {ECO:0000269|PubMed:2414727}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; X02989; CAA26732.1; -; Genomic_DNA.
DR   EMBL; M96372; AAA28982.1; -; Genomic_DNA.
DR   EMBL; U04853; AAA17453.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAF58659.1; -; Genomic_DNA.
DR   EMBL; AY071341; AAL48963.1; -; mRNA.
DR   PIR; A23493; TRFF.
DR   RefSeq; NP_476771.1; NM_057423.4.
DR   AlphaFoldDB; P04814; -.
DR   SMR; P04814; -.
DR   BioGRID; 71314; 7.
DR   DIP; DIP-20031N; -.
DR   STRING; 7227.FBpp0087257; -.
DR   MEROPS; S01.110; -.
DR   PaxDb; 7227-FBpp0087257; -.
DR   DNASU; 48316; -.
DR   EnsemblMetazoa; FBtr0088161; FBpp0087257; FBgn0003863.
DR   GeneID; 48316; -.
DR   KEGG; dme:Dmel_CG18444; -.
DR   UCSC; CG18444-RA; d. melanogaster.
DR   AGR; FB:FBgn0003863; -.
DR   CTD; 48316; -.
DR   FlyBase; FBgn0003863; alphaTry.
DR   VEuPathDB; VectorBase:FBgn0003863; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT00940000164166; -.
DR   HOGENOM; CLU_006842_7_1_1; -.
DR   InParanoid; P04814; -.
DR   OMA; SQIRNTM; -.
DR   OrthoDB; 2910936at2759; -.
DR   PhylomeDB; P04814; -.
DR   BioGRID-ORCS; 48316; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 48316; -.
DR   PRO; PR:P04814; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0003863; Expressed in adult midgut (Drosophila) and 21 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; Trypsin-like serine proteases; 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   PANTHER; PTHR24276:SF91; AT26814P-RELATED; 1.
DR   PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
DR   Genevisible; P04814; DM.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Hydrolase; Protease; Reference proteome; Secreted;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000305"
FT   PROPEP          23..30
FT                   /note="Activation peptide"
FT                   /id="PRO_0000028261"
FT   CHAIN           31..256
FT                   /note="Trypsin alpha"
FT                   /id="PRO_0000028262"
FT   DOMAIN          31..254
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        71
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        116
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        210
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   SITE            204
FT                   /note="Required for specificity"
FT                   /evidence="ECO:0000250"
FT   DISULFID        56..72
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        180..197
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        206..230
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   256 AA;  26041 MW;  8B5634992F2E7C63 CRC64;
     MLKIVILLSA VVCALGGTVP EGLLPQLDGR IVGGSATTIS SFPWQISLQR SGSHSCGGSI
     YSANIIVTAA HCLQSVSASV LQVRAGSTYW SSGGVVAKVS SFKNHEGYNA NTMVNDIAVI
     RLSSSLSFSS SIKAISLATY NPANGASAAV SGWGTQSSGS SSIPSQLQYV NVNIVSQSQC
     ASSTYGYGSQ IRNTMICAAA SGKDACQGDS GGPLVSGGVL VGVVSWGYGC AYSNYPGVYA
     DVAVLRSWVV STANSI
//