ID TRYA_DROER Reviewed; 256 AA.
AC P54624;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-APR-2013, entry version 68.
DE RecName: Full=Trypsin alpha;
DE EC=3.4.21.4;
DE Flags: Precursor;
GN Name=alphaTry;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10486967;
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).
CC -!- CATALYTIC ACTIVITY: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC -!- SIMILARITY: Contains 1 peptidase S1 domain.
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DR EMBL; U40653; AAA83239.1; -; Genomic_DNA.
DR ProteinModelPortal; P54624; -.
DR MEROPS; S01.110; -.
DR FlyBase; FBgn0015076; Dere\alphaTry.
DR OrthoDB; EOG4M37RJ; -.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR001254; Peptidase_S1.
DR InterPro; IPR018114; Peptidase_S1_AS.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR009003; Trypsin-like_Pept_dom.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Pept_Ser_Cys; 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;
KW Signal; Zymogen.
FT SIGNAL 1 22 Probable.
FT PROPEP 23 30 Activation peptide.
FT /FTId=PRO_0000028259.
FT CHAIN 31 256 Trypsin alpha.
FT /FTId=PRO_0000028260.
FT DOMAIN 31 254 Peptidase S1.
FT ACT_SITE 71 71 Charge relay system (By similarity).
FT ACT_SITE 116 116 Charge relay system (By similarity).
FT ACT_SITE 210 210 Charge relay system (By similarity).
FT SITE 204 204 Required for specificity (By similarity).
FT DISULFID 56 72 By similarity.
FT DISULFID 180 197 By similarity.
FT DISULFID 206 230 By similarity.
SQ SEQUENCE 256 AA; 25991 MW; 32C4B5BED84BCC2D CRC64;
MLKIVILLSA VVCALGGTVP EGLLPQLDGR IVGGSATTIS SFPWQISLQR SGSHSCGGSV
YSANIIVTAA HCLQSVSASS LQVRAGSTYW SSGGVVAKVA AFRNHEGYNA NTMVNDIAVI
RLSSSLSFSS SIKAIALATY NPANGAAAAV SGWGTQSSGS NSIPSQLQYV NVNIVSQSKC
ASSAYGYGSE IRNTMICAAA SGKDACQGDS GGPLVSGGVL VGVVSWGYGC AYSNYPGVYA
DVAVLRSWVI STANSI
//