ID   LEC2_CYMRO              Reviewed;         239 AA.
AC   P86795;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   03-AUG-2022, entry version 22.
DE   RecName: Full=Lactose-binding lectin-2;
DE   AltName: Full=Lectin-II {ECO:0000303|PubMed:18712290};
DE            Short=CRLII {ECO:0000303|PubMed:18712290, ECO:0000303|Ref.1};
OS   Cymbosema roseum (Dioclea purpurea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Cymbosema.
OX   NCBI_TaxID=202239;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Seed {ECO:0000269|Ref.1};
RA   Rocha B.A.M., Nagano C.S., Delatorre P., Calvete J.J., Cavada B.S.;
RT   "Primary sequencing of CRLII by Edman's degradation and tandem mass
RT   spectrometry.";
RL   Submitted (AUG-2010) to UniProtKB.
RN   [2] {ECO:0000305}
RP   FUNCTION, SUBUNIT, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY,
RP   AND PRELIMINARY CRYSTALLIZATION.
RC   TISSUE=Seed {ECO:0000269|PubMed:18712290};
RX   PubMed=18712290; DOI=10.1007/s12010-008-8334-9;
RA   Rocha B.A., Moreno F.B., Delatorre P., Souza E.P., Marinho E.S.,
RA   Benevides R.G., Rustiguel J.K., Souza L.A., Nagano C.S., Debray H.,
RA   Sampaio A.H., de Azevedo W.F. Jr., Cavada B.S.;
RT   "Purification, characterization, and preliminary X-ray diffraction analysis
RT   of a lactose-specific lectin from Cymbosema roseum seeds.";
RL   Appl. Biochem. Biotechnol. 152:383-393(2009).
CC   -!- FUNCTION: Lactose-binding lectin. Also binds derivatives of galactose,
CC       glucose, lactose, and mannose. Binds O-glycoproteins such as mucins
CC       more strongly than N-glycoproteins. Shows agglutinating activity
CC       towards rabbit erythrocytes. {ECO:0000269|PubMed:18712290,
CC       ECO:0000269|Ref.1}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:18712290,
CC       ECO:0000269|Ref.1}.
CC   -!- SUBCELLULAR LOCATION: Vacuole, aleurone grain {ECO:0000269|Ref.1}.
CC       Vacuole {ECO:0000269|Ref.1}. Note=Cotyledonary membrane-bound vacuolar
CC       protein bodies. {ECO:0000269|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Seed. {ECO:0000269|PubMed:18712290,
CC       ECO:0000269|Ref.1}.
CC   -!- MASS SPECTROMETRY: Mass=25698; Mass_error=10; Method=MALDI;
CC       Evidence={ECO:0000269|Ref.1};
CC   -!- MASS SPECTROMETRY: Mass=25652; Mass_error=1; Method=Electrospray;
CC       Evidence={ECO:0000269|Ref.1};
CC   -!- MISCELLANEOUS: Binds one manganese (or another transition metal) ion
CC       and one calcium ion. The metal ions are essential for the saccharide-
CC       binding and cell-agglutinating activities.
CC   -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000255}.
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DR   AlphaFoldDB; P86795; -.
DR   SMR; P86795; -.
DR   GO; GO:0033095; C:aleurone grain; IEA:UniProtKB-SubCell.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR016363; L-lectin.
DR   InterPro; IPR001220; Legume_lectin_dom.
DR   Pfam; PF00139; Lectin_legB; 1.
DR   PIRSF; PIRSF002690; L-type_lectin_plant; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Lectin; Manganese; Mannose-binding;
KW   Metal-binding; Vacuole.
FT   CHAIN           1..239
FT                   /note="Lactose-binding lectin-2"
FT                   /id="PRO_0000403321"
FT   BINDING         122
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P81637"
FT   BINDING         124
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P81637"
FT   BINDING         124
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P81637"
FT   BINDING         126
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P81637"
FT   BINDING         128
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P81637"
FT   BINDING         131
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P81637"
FT   BINDING         131
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P81637"
FT   BINDING         137
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P81637"
SQ   SEQUENCE   239 AA;  25701 MW;  2EE9028450B80B2D CRC64;
     SGAVHFSFTK FSTSSSDLTL QGSALVSSKG SLKKNPSKKG KPVDHSVGRA LYRSPIHIWD
     ETTGKVASFD ATFSFVSEAP AIPMLFPSSK GELNDEDDTR IGGQLGVVND SYNVIRVTVA
     VENDGYRNRV DPSARPHISL PIKSVRSKKT AKWNMQTGKV GTAHISYNSV AKRLSAVVSY
     TGNSSSTTVS YDVLLNLAVL PSKVLVGKTA TGLYKDHVET NTILSWSFTS KLKTNSIAD