ID A0A0L0C5K5_LUCCU Unreviewed; 503 AA.
AC A0A0L0C5K5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Trypsin eta {ECO:0000313|EMBL:KNC27527.1};
GN ORFNames=FF38_12322 {ECO:0000313|EMBL:KNC27527.1};
OS Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Calliphoridae; Luciliinae; Lucilia.
OX NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC27527.1, ECO:0000313|Proteomes:UP000037069};
RN [1] {ECO:0000313|EMBL:KNC27527.1, ECO:0000313|Proteomes:UP000037069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LS {ECO:0000313|EMBL:KNC27527.1,
RC ECO:0000313|Proteomes:UP000037069};
RC TISSUE=Full body {ECO:0000313|EMBL:KNC27527.1};
RX PubMed=26108605; DOI=10.1038/ncomms8344;
RA Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT interventions.";
RL Nat. Commun. 6:7344-7344(2015).
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:KNC27527.1}.
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DR EMBL; JRES01000890; KNC27527.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0C5K5; -.
DR EnsemblMetazoa; KNC27527; KNC27527; FF38_12322.
DR OMA; PEWHSGF; -.
DR Proteomes; UP000037069; 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; 3.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR PANTHER; PTHR24276:SF91; AT26814P-RELATED; 1.
DR PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR Pfam; PF00089; Trypsin; 3.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000037069};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..503
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005535579"
FT DOMAIN 25..257
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 299..503
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 503 AA; 55257 MW; 929ABB8F75FAB831 CRC64;
MYKHFIICIL WILCAVVAAA PEGRIIGGRE VDIFKHPYLV SIRYRSQSNE SYVHKCAGAI
YSERVVVTAA QCVVDIKANE KVMVVAGANS RTGVDGLPYP ALKWFSHPSY SSWTVDYDIG
LIIIDDVFDL KHLNMNSITI KETRPIEGKV ATVAGWGYRE EFGPSSSHLE EVQVPIVSTA
ECTQSYGVGE ITERMICAGY VKTGGRDACQ GDTGGPLVMN NQLVGLVSWG RGCARPGYPS
VYTFAPALKK WIDDTIAANV YCSLKDFLTC SKTMKIFICI IALILALHFV DIEAAHVRTV
GDFKASHITQ FPFEVSIRRR FCDACMYEHY CSGTIYSKNV IITAASCVRD ATVQRTQVIA
GTSKRTTSAQ DGQVYLVDKI TLHENDDIDI ALLHLTLDIE FNGLTIAPVK LATQVPIAAV
QVPIMDLDLC KEAYFWTNVK DTEICAGYLD GGVDACVGDA GSPLLVDNEM VGIVSWGYGC
ARPNNPGVYT NVVMLRNWIQ QHA
//
