GPL_GLOFF
ID GPL_GLOFF Reviewed; 274 AA.
AC Q8MUG0;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Lectizyme;
DE EC=3.4.21.-;
DE AltName: Full=Proteolytic lectin;
DE Flags: Precursor;
GN Name=Gpl;
OS Glossina fuscipes fuscipes (Riverine tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=201502;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC TISSUE=Midgut;
RX PubMed=16551548; DOI=10.1016/j.ibmb.2006.01.010;
RA Abubakar L.U., Bulimo W.D., Mulaa F.J., Osir E.O.;
RT "Molecular characterization of a tsetse fly midgut proteolytic lectin that
RT mediates differentiation of African trypanosomes.";
RL Insect Biochem. Mol. Biol. 36:344-352(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:16551548}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16551548}.
CC -!- TISSUE SPECIFICITY: Expressed in the midgut.
CC {ECO:0000269|PubMed:16551548}.
CC -!- INDUCTION: By blood meal. {ECO:0000269|PubMed:16551548}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AF525314; AAM82602.1; -; mRNA.
DR AlphaFoldDB; Q8MUG0; -.
DR SMR; Q8MUG0; -.
DR STRING; 201502.Q8MUG0; -.
DR MEROPS; S01.493; -.
DR Proteomes; UP000092443; 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_0000291657"
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; 29180 MW; 1EC4A00D3DDCD5AB CRC64;
MKFFAVFALC VASVSAANLD AIAKPGFPAG RIINGHEADK GEAPFIVSLK AGKGHFCGGS
IIAENWVLTA GHCLIFDEFE IVAGLHSRND ESDVQIRKVT GKHQQIVHEK YGGGVGPNDI
GLIYVDKPFN LNALTRDGTA AVAKVNLPTG KYESTGKGKL YGWGLDNSGF SPNILNTLDV
DIIGYEECKN ALNSDDPLDP VNICSYTAGA IDGACNGDSG GPMVRITPDG TELVGIVSWG
YQPCASTTMP SVYTWTSAFD KWIEDSIKNY AQLL
