ID Q4L1L2_9NEOP Unreviewed; 215 AA.
AC Q4L1L2;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Trypsin Ia2 {ECO:0000313|EMBL:AAT95345.1};
DE EC=3.4.21.4 {ECO:0000313|EMBL:AAT95345.1};
DE Flags: Fragment;
GN Name=TrIa2 {ECO:0000313|EMBL:AAT95345.1};
OS Sesamia nonagrioides (Mediterranean corn borer).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Amphipyrinae; Sesamia.
OX NCBI_TaxID=236805 {ECO:0000313|EMBL:AAT95345.1};
RN [1] {ECO:0000313|EMBL:AAT95345.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15979001; DOI=10.1016/j.ibmb.2005.04.003;
RA Diaz-Mendoza M., Ortego F., Garcia de Lacoba M., Magana C., de la Poza M.,
RA Farinos G.P., Castanera P., Hernandez-Crespo P.;
RT "Diversity of trypsins in the Mediterranean corn borer Sesamia nonagrioides
RT (Lepidoptera: Noctuidae), revealed by nucleic acid sequences and enzyme
RT purification.";
RL Insect Biochem. Mol. Biol. 35:1005-1020(2005).
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY587153; AAT95345.1; -; mRNA.
DR AlphaFoldDB; Q4L1L2; -.
DR MEROPS; S01.112; -.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
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 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.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000313|EMBL:AAT95345.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..215
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004240457"
FT DOMAIN 22..215
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAT95345.1"
FT NON_TER 215
FT /evidence="ECO:0000313|EMBL:AAT95345.1"
SQ SEQUENCE 215 AA; 22633 MW; A8870C5E35B97D64 CRC64;
AVLALLTIAL LAGSSAALPK RIVGGDETSI DKYPSIVSLE FHDLWTGVWS HNCAANILTS
RHLVTAAHCM MASVTFRRIR AGSSYRNTGG IVILVEANFN HPSYGQNGYD GDIAVTRLAQ
PLVYSPVIQQ GRIVAANTVL PDGLPVVHAG WGAIWQGGPL SSVLRDVTIF TINNALCTAR
YLTLPRPGVV TPNMICAGIL DVGGKDACQG DCGGP
//