TRYB_DROER
ID TRYB_DROER Reviewed; 253 AA.
AC P54625; B3NSH7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Trypsin beta;
DE EC=3.4.21.4;
DE Flags: Precursor;
GN Name=betaTry; ORFNames=GG20194;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1]
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.01;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; U40653; AAA83241.1; -; Genomic_DNA.
DR EMBL; CH954179; EDV56479.1; -; Genomic_DNA.
DR RefSeq; XP_001976079.1; XM_001976043.2.
DR AlphaFoldDB; P54625; -.
DR SMR; P54625; -.
DR MEROPS; S01.110; -.
DR EnsemblMetazoa; FBtr0140248; FBpp0138740; FBgn0015077.
DR GeneID; 6547181; -.
DR KEGG; der:6547181; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_7_1_1; -.
DR OMA; YSARVIV; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P54625; -.
DR Proteomes; UP000008711; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Disulfide bond; Hydrolase; Protease; Secreted; Serine protease; Signal;
KW Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000305"
FT PROPEP 23..30
FT /note="Activation peptide"
FT /id="PRO_0000028263"
FT CHAIN 31..253
FT /note="Trypsin beta"
FT /id="PRO_0000028264"
FT DOMAIN 31..253
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 253 AA; 25814 MW; 073832534B59655E CRC64;
MLKFVILLSA VACALGGTIP EGLLPQLDGR IVGGTATTIS SFPWQISLQR SGSHSCGGSI
YTDRVIVTAA HCLQSVSASS LQIRAGSSYW SSGGVTVKVS SFKNHEGYNP NTMVNDIAVI
RLSSSLGFSS TIKSISLASS NPANGAAASV SGWGTQSSGS SSIPSQLQYV NVNIVSQSKC
ASSAYGYGSE IRNTMICAAA SGKDACQGDS GGPLVSGGVL VGVVSWGYGC AYSNYPGVYA
SVADLRSWVI NNA
