ID   GPL_GLOAU               Reviewed;         274 AA.
AC   Q4TTV7;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Lectizyme;
DE            EC=3.4.21.-;
DE   AltName: Full=Proteolytic lectin;
DE   Flags: Precursor;
GN   Name=Gpl;
OS   Glossina austeni (Savannah tsetse fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC   Glossinidae; Glossina.
OX   NCBI_TaxID=7395;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND INDUCTION.
RC   TISSUE=Midgut;
RX   PubMed=16619615; DOI=10.1603/0022-2585(2006)043[0301:gpldnr]2.0.co;2;
RA   Amin D.N., Kamita S.G., Muluvi G.M., Machuka J., Hammock B.D., Osir E.O.;
RT   "Glossina proteolytic lectin does not require a carbohydrate moiety for
RT   enzymatic or trypanosome-transforming activities.";
RL   J. Med. Entomol. 43:301-308(2006).
CC   -!- FUNCTION: Protein with lectin and protease activity involved in the
CC       establishment of trypanosome infections in tsetse flies. Binds D-
CC       glucosamine and agglutinates bloodstream-form trypanosomes and rabbit
CC       red blood cells. Capable of inducing transformation of bloodstream-form
CC       trypanosomes into procyclic (midgut) forms in vitro.
CC       {ECO:0000269|PubMed:16619615}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16619615}.
CC   -!- TISSUE SPECIFICITY: Expressed in the midgut.
CC       {ECO:0000269|PubMed:16619615}.
CC   -!- INDUCTION: By blood meal. {ECO:0000269|PubMed:16619615}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; DQ060150; AAY59001.1; -; mRNA.
DR   AlphaFoldDB; Q4TTV7; -.
DR   SMR; Q4TTV7; -.
DR   STRING; 7395.Q4TTV7; -.
DR   VEuPathDB; VectorBase:GAUT018969; -.
DR   Proteomes; UP000078200; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; -; 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   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 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; Hydrolase; Protease; Secreted; Serine protease; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..274
FT                   /note="Lectizyme"
FT                   /id="PRO_0000291656"
FT   DOMAIN          32..268
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        72
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        119
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        219
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   DISULFID        57..73
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        188..204
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        215..244
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   274 AA;  29151 MW;  ADFF48DE50710349 CRC64;
     MKFFAVFALC VASVSAANLD AIAKPGFPAG RIINGHEAEK GEAPFIVSLK AGKGHFCGGS
     IIAENWVLTA GHCLIFDEFE IVAGLHSRND ESDVQIRKVT GKHQQIVHEK YGGGVGPNDI
     GLIYVDKPFN LNALTRDGTA AVAKVNLPTG KYESTGEGKL YGWGLDNSGF SPNILNTLDV
     NIIGYEECKN ALNSDAPLDP VNICSYTAGA IDGACNGDSG GPMVRITPDG TELVGIVSWG
     YQPCASTTMP SVYTWTSAFD KWIEDSIENY AQLL