ID X5MFH7_LOCMI Unreviewed; 269 AA.
AC X5MFH7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Chymotrypsin 8 {ECO:0000313|EMBL:DAA64583.1};
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:DAA64583.1};
RN [1] {ECO:0000313|EMBL:DAA64583.1}
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:DAA64583.1}
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; BK008832; DAA64583.1; -; mRNA.
DR AlphaFoldDB; X5MFH7; -.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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:SF95; PEPTIDASE S1 DOMAIN-CONTAINING PROTEIN; 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:0000256|ARBA:ARBA00022825};
KW Protease {ECO:0000256|ARBA:ARBA00022825};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..269
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004957934"
FT DOMAIN 39..269
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 269 AA; 28456 MW; 52C6E69EE6CA386F CRC64;
MLRHALLLLA LASCVLGARL PMRRLVHSGK WLGAAGGRIV GGQDAVPGQF PYQVSLQYVT
WEFTLIECTG SLITPMRVLT AGHCCGATNT AVAGVVDLDG CEEAKQESKV LDQIYHPDFP
VGYYGIYAND IAVFTLETAF TLNEYVQTIP LATAGSIPTV NSSAVGSAWG SSPDNLQWVE
LSIIDYETCR QLVDDLGVIG ENFVVDTMVC TVPITDGVGL CSGDSGGPLV QDGALIGIAQ
WSNVESGKGG VPSGFNRVSA FIDFINAHI
//