ID   LEC_PARPU               Reviewed;         447 AA.
AC   C0HLR9;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   07-APR-2021, sequence version 1.
DT   25-MAY-2022, entry version 5.
DE   RecName: Full=Mannose/glucose-specific lectin {ECO:0000250|UniProtKB:P83304};
DE            Short=PpeL {ECO:0000303|Ref.1};
OS   Parkia pendula (Inga pendula).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Caesalpinioideae; mimosoid clade;
OC   Mimoseae; Parkia.
OX   NCBI_TaxID=1905032 {ECO:0000303|Ref.1};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Seed {ECO:0000303|Ref.1};
RX   DOI=10.1016/j.procbio.2020.11.004;
RA   Carneiro R.F., Aguiar E.S., Santos V.F., Santos A.L.E., Santos M.H.C.,
RA   Roma R.R., Silva R.R.S., Leal M.L.M., Silva L.T., Rocha B.A.M.,
RA   Silva C.G.L., Nagano C.S., Sampaio A.H., Souza R.O.S., Teixeira C.S.;
RT   "Elucidation of the primary structure and molecular modeling of Parkia
RT   pendula lectin and in vitro evaluation of the leishmanicidal activity.";
RL   Process Biochem. 101:1-10(2021).
CC   -!- FUNCTION: D-mannose/D-glucose-binding lectin that also binds
CC       derivatives N-acetyl-D-glucosamine and alpha-methyl-D-mannopyranoside
CC       (Ref.1). Does not bind D-galactose, L-Rhamnose, D-fructose, lactose or
CC       glycoproteins fetiun and mucin (Ref.1). Shows agglutinating activity
CC       towards human and rabbit erythrocytes (Ref.1). Also displays
CC       antimicrobial activity against L.infantum (Ref.1). {ECO:0000269|Ref.1}.
CC   -!- ACTIVITY REGULATION: Hemagglutinating activity is slightly inhibited by
CC       alpha-methyl-D-mannopyranoside. {ECO:0000269|Ref.1}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH for hemagglutinating activity is 5-7 with activity
CC         decreasing quickly at higher or lower pH. {ECO:0000269|Ref.1};
CC       Temperature dependence:
CC         Hemagglutinating activity stable up to 50 degrees Celsius but
CC         diminishes with higher temperatures and is absent at 60 degrees
CC         Celsius. {ECO:0000269|Ref.1};
CC   -!- TISSUE SPECIFICITY: Expressed in seeds (at protein level).
CC       {ECO:0000269|Ref.1}.
CC   -!- MASS SPECTROMETRY: Mass=47410; Mass_error=5; Method=Electrospray;
CC       Evidence={ECO:0000269|Ref.1};
CC   -!- TOXIC DOSE: LD(50) is 4.9 +-0.05 umol/ml against L.infantum.
CC       {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the jacalin lectin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01088}.
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DR   AlphaFoldDB; C0HLR9; -.
DR   SMR; C0HLR9; -.
DR   GO; GO:0005536; F:glucose binding; IDA:UniProtKB.
DR   GO; GO:0005537; F:mannose binding; IDA:UniProtKB.
DR   CDD; cd09612; Jacalin; 3.
DR   Gene3D; 2.100.10.30; -; 3.
DR   InterPro; IPR001229; Jacalin-like_lectin_dom.
DR   InterPro; IPR033734; Jacalin-like_lectin_dom_plant.
DR   InterPro; IPR036404; Jacalin-like_lectin_dom_sf.
DR   Pfam; PF01419; Jacalin; 3.
DR   SMART; SM00915; Jacalin; 3.
DR   SUPFAM; SSF51101; SSF51101; 3.
DR   PROSITE; PS51752; JACALIN_LECTIN; 3.
PE   1: Evidence at protein level;
KW   Antimicrobial; Direct protein sequencing; Lectin; Repeat.
FT   CHAIN           1..447
FT                   /note="Mannose/glucose-specific lectin"
FT                   /id="PRO_0000452499"
FT   DOMAIN          5..148
FT                   /note="Jacalin-type lectin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01088"
FT   DOMAIN          153..294
FT                   /note="Jacalin-type lectin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01088"
FT   DOMAIN          300..443
FT                   /note="Jacalin-type lectin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01088"
SQ   SEQUENCE   447 AA;  47411 MW;  CE12A3C53D36A645 CRC64;
     QLKGMISVGP WGGQGGDHWS FKANHAITEI LIHVKDNIKS ISFKDASGDI SGTFGGKDPR
     ENEKGDEKKI GIHWPTEYLK SISGSYGDYN GLLVIRSLSF ITNLTTYGSF GSTSGGESFS
     IPIADSVVVG FHGRGGYYLD ALGVFVKPVP HGTISFGPWG GPAGDDAFNF KVGSWIKDII
     IYSNGAIQSI AFKDGNGHCY GKFGGKDPND IGVEKKVEID GNLEHLTSIS GTYGNYKGFE
     VVTSLSFITN VTKHGPFGTA SGTSFSIPIE GSLVTGFHGK GGYYLDSIGI YVKPRDVEGS
     ISIGPWGGSG GDPWSYTANE GINQIIIYAG SDIKSLAFKD TSGFDSATFG GVNPKDTGEK
     NTVSINWPSE YLTSISGTYG QYKFKDVFTT ITSLSFTTNL ATYGPFGKAS GTSFSVPINN
     NTVLGFHGRA GDYLDAIGIF VKPDTAV