GenomeNet

Database: UniProt
Entry: P54624
LinkDB: P54624
Original site: P54624 
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   01-OCT-2014, entry version 73.
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; 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).
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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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; EOG7MKW6Q; -.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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; 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;
KW   Signal; Zymogen.
FT   SIGNAL        1     22       {ECO:0000305}.
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. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE     71     71       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    116    116       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    210    210       Charge relay system. {ECO:0000250}.
FT   SITE        204    204       Required for specificity. {ECO:0000250}.
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   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
//
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