GenomeNet

Database: UniProt/SWISS-PROT
Entry: TRYDT_DROME TRYGT_DROME Y0031_DROME
LinkDB: TRYDT_DROME TRYGT_DROME Y0031_DROME
Original site: TRYDT_DROME TRYGT_DROME Y0031_DROME 
ID   TRYDT_DROME             Reviewed;         253 AA.
AC   C0HKA2; G7H855; P42276; P42277; Q8SXZ4; Q9V5Y4;
DT   15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2017, sequence version 1.
DT   27-SEP-2017, entry version 8.
DE   RecName: Full=Trypsin delta {ECO:0000312|FlyBase:FBgn0010358};
DE            EC=3.4.21.4 {ECO:0000255|PROSITE-ProRule:PRU00274};
DE   Flags: Precursor;
GN   Name=deltaTry {ECO:0000312|FlyBase:FBgn0010358};
GN   ORFNames=CG12351 {ECO:0000312|FlyBase:FBgn0010358};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Oregon-R;
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   [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.,
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   [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.,
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley {ECO:0000312|EMBL:AET62584.1};
RA   Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000250|UniProtKB:P04814}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; U04853; AAA17449.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAF58657.2; -; Genomic_DNA.
DR   EMBL; BT132779; AET62584.1; -; mRNA.
DR   RefSeq; NP_523694.2; NM_078970.4.
DR   RefSeq; NP_725034.1; NM_165823.3.
DR   RefSeq; NP_725035.1; NM_165824.3.
DR   UniGene; Dm.14041; -.
DR   UniGene; Dm.21711; -.
DR   UniGene; Dm.30904; -.
DR   SMR; C0HKA2; -.
DR   EnsemblMetazoa; FBtr0088123; FBpp0087224; FBgn0050031.
DR   EnsemblMetazoa; FBtr0088124; FBpp0087225; FBgn0010358.
DR   EnsemblMetazoa; FBtr0088159; FBpp0087255; FBgn0010359.
DR   GeneID; 246404; -.
DR   GeneID; 36221; -.
DR   GeneID; 48343; -.
DR   KEGG; dme:Dmel_CG12351; -.
DR   KEGG; dme:Dmel_CG30028; -.
DR   KEGG; dme:Dmel_CG30031; -.
DR   CTD; 36221; -.
DR   CTD; 48343; -.
DR   FlyBase; FBgn0010358; deltaTry.
DR   KO; K01312; -.
DR   OMA; YSNNIIV; -.
DR   PRO; PR:C0HKA2; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0010358; -.
DR   ExpressionAtlas; C0HKA2; differential.
DR   GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
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   Complete proteome; Disulfide bond; Hydrolase; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL        1     22       {ECO:0000305}.
FT   PROPEP       23     30       Activation peptide.
FT                                /FTId=PRO_0000028269.
FT   CHAIN        31    253       Trypsin delta. {ECO:0000255}.
FT                                /FTId=PRO_0000028270.
FT   DOMAIN       31    253       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE     71     71       Charge relay system.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   ACT_SITE    116    116       Charge relay system.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   ACT_SITE    210    210       Charge relay system.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID     56     72       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    180    197       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    206    230       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   CONFLICT    118    118       A -> V (in Ref. 1; AAA17449).
FT                                {ECO:0000305}.
FT   CONFLICT    148    148       A -> G (in Ref. 1; AAA17449).
FT                                {ECO:0000305}.
FT   CONFLICT    240    240       A -> S (in Ref. 1; AAA17449).
FT                                {ECO:0000305}.
SQ   SEQUENCE   253 AA;  25680 MW;  F77D47E0CCC78F92 CRC64;
     MLKFVILLSA VACALGGTVP EGLLPQLDGR IVGGSATTIS SFPWQISLQR SGSHSCGGSI
     YSSNVIVTAA HCLQSVSASV LQIRAGSSYW SSGGVTFSVS SFKNHEGYNA NTMVNDIAII
     KINGALTFSS TIKAIGLASS NPANGAAASV SGWGTLSYGS SSIPSQLQYV NVNIVSQSQC
     ASSTYGYGSQ IRSTMICAAA SGKDACQGDS GGPLVSGGVL VGVVSWGYGC AYSNYPGVYA
     DVAALRSWVI SNA
//
  All links  
Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (11)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (3)   
   NCBI-Gene (3)   
   UniGene (3)   
   FLYBASE (1)   
Protein sequence (3)   
   RefSeq(pep) (3)   
DNA sequence (3)   
   EMBL (3)   
Protein domain (10)   
   InterPro (5)   
   Pfam (1)   
   PROSITE (3)   
   SMART (1)   
Literature (3)   
   PubMed (3)   
All databases (34)   

Download RDF
ID   TRYGT_DROME             Reviewed;         253 AA.
AC   C0HKA3; P42276; P42277; Q8SXZ4; Q9V5Y4;
DT   15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2017, sequence version 1.
DT   27-SEP-2017, entry version 6.
DE   RecName: Full=Trypsin gamma {ECO:0000312|FlyBase:FBgn0010359};
DE            EC=3.4.21.4 {ECO:0000255|PROSITE-ProRule:PRU00274};
DE   Flags: Precursor;
GN   Name=gammaTry {ECO:0000312|FlyBase:FBgn0010359};
GN   ORFNames=CG30028 {ECO:0000312|FlyBase:FBgn0010359};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Oregon-R;
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   [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.,
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   [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.,
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W.,
RA   Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
RA   George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
RA   Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
RA   Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
RA   Celniker S.E.;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000250|UniProtKB:P04814}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; U04853; AAA17450.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAM68730.1; -; Genomic_DNA.
DR   EMBL; AY075487; AAL68297.1; -; mRNA.
DR   RefSeq; NP_523694.2; NM_078970.4.
DR   RefSeq; NP_725034.1; NM_165823.3.
DR   RefSeq; NP_725035.1; NM_165824.3.
DR   UniGene; Dm.14041; -.
DR   UniGene; Dm.21711; -.
DR   UniGene; Dm.30904; -.
DR   SMR; C0HKA3; -.
DR   EnsemblMetazoa; FBtr0088123; FBpp0087224; FBgn0050031.
DR   EnsemblMetazoa; FBtr0088124; FBpp0087225; FBgn0010358.
DR   EnsemblMetazoa; FBtr0088159; FBpp0087255; FBgn0010359.
DR   GeneID; 246404; -.
DR   GeneID; 36221; -.
DR   GeneID; 48343; -.
DR   KEGG; dme:Dmel_CG12351; -.
DR   KEGG; dme:Dmel_CG30028; -.
DR   KEGG; dme:Dmel_CG30031; -.
DR   CTD; 36221; -.
DR   CTD; 48343; -.
DR   FlyBase; FBgn0010359; gammaTry.
DR   KO; K01312; -.
DR   PRO; PR:C0HKA3; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   ExpressionAtlas; C0HKA3; differential.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
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   Complete proteome; Disulfide bond; Hydrolase; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL        1     22       {ECO:0000305}.
FT   PROPEP       23     30       Activation peptide.
FT                                /FTId=PRO_0000438899.
FT   CHAIN        31    253       Trypsin gamma. {ECO:0000255}.
FT                                /FTId=PRO_0000438900.
FT   DOMAIN       31    253       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE     71     71       Charge relay system.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   ACT_SITE    116    116       Charge relay system.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   ACT_SITE    210    210       Charge relay system.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID     56     72       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    180    197       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    206    230       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   CONFLICT    118    118       A -> V (in Ref. 1; AAA17450).
FT                                {ECO:0000305}.
FT   CONFLICT    148    148       A -> G (in Ref. 1; AAA17450).
FT                                {ECO:0000305}.
SQ   SEQUENCE   253 AA;  25680 MW;  F77D47E0CCC78F92 CRC64;
     MLKFVILLSA VACALGGTVP EGLLPQLDGR IVGGSATTIS SFPWQISLQR SGSHSCGGSI
     YSSNVIVTAA HCLQSVSASV LQIRAGSSYW SSGGVTFSVS SFKNHEGYNA NTMVNDIAII
     KINGALTFSS TIKAIGLASS NPANGAAASV SGWGTLSYGS SSIPSQLQYV NVNIVSQSQC
     ASSTYGYGSQ IRSTMICAAA SGKDACQGDS GGPLVSGGVL VGVVSWGYGC AYSNYPGVYA
     DVAALRSWVI SNA
//
  All links  
Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (11)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (3)   
   NCBI-Gene (3)   
   UniGene (3)   
   FLYBASE (1)   
Protein sequence (3)   
   RefSeq(pep) (3)   
DNA sequence (3)   
   EMBL (3)   
Protein domain (10)   
   InterPro (5)   
   Pfam (1)   
   PROSITE (3)   
   SMART (1)   
Literature (3)   
   PubMed (3)   
All databases (33)   

Download RDF
ID   Y0031_DROME             Reviewed;         253 AA.
AC   C0HKA4; P42276; P42277; Q8SXZ4; Q9V5Y4;
DT   15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2017, sequence version 1.
DT   25-OCT-2017, entry version 8.
DE   RecName: Full=Trypsin delta/gamma-like protein CG30031 {ECO:0000305};
DE            EC=3.4.21.4 {ECO:0000255|PROSITE-ProRule:PRU00274};
DE   Flags: Precursor;
GN   ORFNames=CG30031 {ECO:0000312|FlyBase:FBgn0050031};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; 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   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.
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.,
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).
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000250|UniProtKB:P04814}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; AE013599; AAM68731.1; -; Genomic_DNA.
DR   RefSeq; NP_523694.2; NM_078970.4.
DR   RefSeq; NP_725034.1; NM_165823.3.
DR   RefSeq; NP_725035.1; NM_165824.3.
DR   UniGene; Dm.14041; -.
DR   UniGene; Dm.21711; -.
DR   UniGene; Dm.30904; -.
DR   SMR; C0HKA4; -.
DR   EnsemblMetazoa; FBtr0088123; FBpp0087224; FBgn0050031.
DR   EnsemblMetazoa; FBtr0088124; FBpp0087225; FBgn0010358.
DR   EnsemblMetazoa; FBtr0088159; FBpp0087255; FBgn0010359.
DR   GeneID; 246404; -.
DR   GeneID; 36221; -.
DR   GeneID; 48343; -.
DR   KEGG; dme:Dmel_CG12351; -.
DR   KEGG; dme:Dmel_CG30028; -.
DR   KEGG; dme:Dmel_CG30031; -.
DR   CTD; 36221; -.
DR   CTD; 48343; -.
DR   FlyBase; FBgn0050031; CG30031.
DR   GeneTree; ENSGT00900000141205; -.
DR   KO; K01312; -.
DR   PRO; PR:C0HKA4; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   ExpressionAtlas; C0HKA4; differential.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
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   InterPro; IPR009003; Peptidase_S1_PA.
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   3: Inferred from homology;
KW   Complete proteome; Disulfide bond; Hydrolase; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL        1     22       {ECO:0000305}.
FT   PROPEP       23     30       Activation peptide.
FT                                /FTId=PRO_0000438901.
FT   CHAIN        31    253       Trypsin delta/gamma-like protein CG30031.
FT                                /FTId=PRO_0000438902.
FT   DOMAIN       31    253       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE     71     71       Charge relay system.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   ACT_SITE    116    116       Charge relay system.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   ACT_SITE    210    210       Charge relay system.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID     56     72       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    180    197       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    206    230       {ECO:0000255|PROSITE-ProRule:PRU00274}.
SQ   SEQUENCE   253 AA;  25680 MW;  F77D47E0CCC78F92 CRC64;
     MLKFVILLSA VACALGGTVP EGLLPQLDGR IVGGSATTIS SFPWQISLQR SGSHSCGGSI
     YSSNVIVTAA HCLQSVSASV LQIRAGSSYW SSGGVTFSVS SFKNHEGYNA NTMVNDIAII
     KINGALTFSS TIKAIGLASS NPANGAAASV SGWGTLSYGS SSIPSQLQYV NVNIVSQSQC
     ASSTYGYGSQ IRSTMICAAA SGKDACQGDS GGPLVSGGVL VGVVSWGYGC AYSNYPGVYA
     DVAALRSWVI SNA
//
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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (11)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (3)   
   NCBI-Gene (3)   
   UniGene (3)   
   FLYBASE (1)   
Protein sequence (3)   
   RefSeq(pep) (3)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (5)   
   Pfam (1)   
   PROSITE (3)   
   SMART (1)   
Literature (2)   
   PubMed (2)   
All databases (31)   

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