ID X5MFH0_LOCMI Unreviewed; 253 AA.
AC X5MFH0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Trypsin 2A {ECO:0000313|EMBL:DAA64573.1};
OS Locusta migratoria (Migratory locust).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Orthoptera; Caelifera; Acrididea; Acridomorpha;
OC Acridoidea; Acrididae; Oedipodinae; Locusta.
OX NCBI_TaxID=7004 {ECO:0000313|EMBL:DAA64573.1};
RN [1] {ECO:0000313|EMBL:DAA64573.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24650544;
RA Spit J., Zels S., Dillen S., Holtof M., Wynant N., Vanden Broeck J.;
RT "Effects of different dietary conditions on the expression of trypsin- and
RT chymotrypsin-like protease genes in the digestive system of the migratory
RT locust, Locusta migratoria.";
RL Insect Biochem. Mol. Biol. 48C:100-109(2014).
RN [2] {ECO:0000313|EMBL:DAA64573.1}
RP NUCLEOTIDE SEQUENCE.
RA Spit J.R.M., Vanden Broeck J.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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DR EMBL; BK008822; DAA64573.1; -; mRNA.
DR AlphaFoldDB; X5MFH0; -.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 InterPro; IPR033116; TRYPSIN_SER.
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.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..253
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004958872"
FT DOMAIN 33..252
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 253 AA; 26335 MW; 099A241537C8EB30 CRC64;
MLKAALVCLL VVACSAAPSV QRPKPRPRLD GRIVGGQAVD ISEYPWQLSM QEFGSHLCGA
SIISSEWALT AAHCLEGSYI NYVTLRAGSS TRGSGGTVYD VELAYYHGYY DSYTTDYDIG
VMQISGSFSF DTNVQAVTLA TSEPSAGTSV TITGWGALSS GGSSPTQLQA VTTSVVARST
CNSAYGGEIT DRMICAGETG KDSCQGDSGG PLVSGSTQYG IVSWGYGCAE EGYPGVYSNV
AALRDWVTEA AGV
//
