ID A0A212FPE2_DANPL Unreviewed; 502 AA.
AC A0A212FPE2;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Trypsin {ECO:0000313|EMBL:OWR55583.1};
GN ORFNames=KGM_202640 {ECO:0000313|EMBL:OWR55583.1};
OS Danaus plexippus plexippus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Danainae; Danaini; Danaina; Danaus; Danaus.
OX NCBI_TaxID=278856 {ECO:0000313|EMBL:OWR55583.1, ECO:0000313|Proteomes:UP000007151};
RN [1] {ECO:0000313|EMBL:OWR55583.1, ECO:0000313|Proteomes:UP000007151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F-2 {ECO:0000313|EMBL:OWR55583.1};
RX PubMed=22118469; DOI=10.1016/j.cell.2011.09.052;
RA Zhan S., Merlin C., Boore J.L., Reppert S.M.;
RT "The monarch butterfly genome yields insights into long-distance
RT migration.";
RL Cell 147:1171-1185(2011).
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWR55583.1}.
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DR EMBL; AGBW02003040; OWR55583.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A212FPE2; -.
DR STRING; 278856.A0A212FPE2; -.
DR KEGG; dpl:KGM_202640; -.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; A0A212FPE2; -.
DR Proteomes; UP000007151; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00190; Tryp_SPc; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
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:SF100; AT20289P-RELATED; 1.
DR PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR Pfam; PF00089; Trypsin; 2.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 2.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000007151}.
FT DOMAIN 48..266
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 274..501
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 502 AA; 55315 MW; 817544B7ACCD4A57 CRC64;
MSCHHKAILR AKADERDVAW FLRPSIILSE KIPLWESWKT PPKVDERIVG GEDANIEDYP
YQVSYTFNNS YFCGGFIVSE NYILTAGHCS QNVDPSTVVL RAGSSYRQNG TIIPIAEVMA
HPEYDDPAFD KDVGFMRTAE PIQFSDTIQP IQLAERDRPL VGDIQVTGWG RLKQGQNPIP
SRLMRVKVPV VNYWQCTLSY FSVLTRNMFC AGNFFLGGQG TCQGDSGGAA IQDGRAVGIV
SFGRGGYSSD IIQPGNVPLW SDTEETEYDV DERIVGGQET TIEEYPHQVN FLFQRDNGTY
FCGGFIISEY YILTAAHCAQ GIDPTTVILR AGSTYRGNGT IIPIDEIVAH PEYNDSPFDK
DVGYIRTSNP IQFTGAMKPI PLVNESEPCS NRVNVSGWGR LMEGQNPLPL RLRAVNVPVV
DYFRCKMAYP RILTRNMVCV GNFVLGGQGT CQGDSGDAGV DNGRACGIVS FARGCARPMS
PNVFTNIAAG PVRRFITDNT GV
//