LECA_DIOLA
ID LECA_DIOLA Reviewed; 291 AA.
AC C0HK27;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Lectin {ECO:0000303|PubMed:24008245};
DE Short=DlyL {ECO:0000303|PubMed:24008245};
DE Flags: Precursor;
OS Dioclea lasiophylla.
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; Dioclea.
OX NCBI_TaxID=1457464;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-147; 163-197 AND
RP 202-280, FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Seed {ECO:0000303|PubMed:28196677};
RX PubMed=28196677; DOI=10.1016/j.biochi.2017.02.002;
RA Pinto-Junior V.R., Osterne V.J., Santiago M.Q., Lossio C.F., Nagano C.S.,
RA Rocha C.R., Nascimento J.C., Nascimento F.L., Silva I.B., Oliveira A.S.,
RA Correia J.L., Leal R.B., Assreuy A.M., Cavada B.S., Nascimento K.S.;
RT "Molecular modeling, docking and dynamics simulations of the Dioclea
RT lasiophylla Mart. Ex Benth seed lectin: An edematogenic and
RT hypernociceptive protein.";
RL Biochimie 135:126-136(2017).
RN [2] {ECO:0000305}
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, AND TOXIC DOSE.
RC TISSUE=Seed {ECO:0000303|PubMed:24008245};
RX PubMed=24008245; DOI=10.3390/molecules180910857;
RA Pinto-Junior V.R., de Santiago M.Q., Osterne V.J., Correia J.L.,
RA Pereira-Junior F.N., Cajazeiras J.B., de Vasconcelos M.A., Teixeira E.H.,
RA do Nascimento A.S., Miguel T.B., Miguel E.C., Sampaio A.H.,
RA do Nascimento K.S., Nagano C.S., Cavada B.S.;
RT "Purification, partial characterization and immobilization of a mannose-
RT specific lectin from seeds of Dioclea lasiophylla mart.";
RL Molecules 18:10857-10869(2013).
CC -!- FUNCTION: D-mannose-binding lectin that also binds alpha-methyl-D-
CC mannoside with even higher affinity (PubMed:24008245). Has
CC hemagglutinating activity against rabbit erythrocytes
CC (PubMed:24008245). Shows toxicity against the brine shrimp A.nauplii
CC (PubMed:24008245). Induces reversible paw edema and hypernociceptivity
CC in rats (PubMed:28196677). {ECO:0000269|PubMed:24008245,
CC ECO:0000269|PubMed:28196677}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH for hemagglutinating activity is 8. Activity drops with
CC more acidic and basic pH and is lost at pH 5 and pH 8, respectively.
CC {ECO:0000269|PubMed:24008245};
CC Temperature dependence:
CC Hemagglutinating activity is stable after incubation at 70 degrees
CC Celsius for 1 hour but lost at higher temperatures.
CC {ECO:0000269|PubMed:24008245};
CC -!- PTM: The mature chain consists of residues 163-280 followed by residues
CC 29-147. Concanavalin A-like lectins of the Diocleinae subtribe undergo
CC proteolytic processing referred to as circular permutation. The
CC propeptide is split into an N-terminal and a C-terminal part, the gamma
CC and beta chain, respectively. These are then religated in beta-gamma
CC order to form the mature alpha chain. The beta and gamma chains can
CC often be detected in cell extracts. {ECO:0000269|PubMed:28196677}.
CC -!- MASS SPECTROMETRY: Mass=25569; Mass_error=2; Method=Electrospray;
CC Note=The mature chain consists of residues 163-280 followed by residues
CC 29-146. The measured range is 1-237.;
CC Evidence={ECO:0000269|PubMed:24008245};
CC -!- TOXIC DOSE: LD(50) is 45.85 ug/ml against the brine shrimp A.nauplii.
CC {ECO:0000269|PubMed:24008245}.
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 {ECO:0000250|UniProtKB:P14894}.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR PDB; 6CJ9; X-ray; 1.70 A; A=1-147.
DR PDBsum; 6CJ9; -.
DR AlphaFoldDB; C0HK27; -.
DR SMR; C0HK27; -.
DR UniLectin; C0HK27; -.
DR GO; GO:0005537; F:mannose binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; 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; IPR000985; Lectin_LegA_CS.
DR InterPro; IPR019825; Lectin_legB_Mn/Ca_BS.
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.
DR PROSITE; PS00308; LECTIN_LEGUME_ALPHA; 1.
DR PROSITE; PS00307; LECTIN_LEGUME_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Hemagglutinin; Lectin;
KW Manganese; Mannose-binding; Metal-binding; Signal; Toxin.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:28196677"
FT CHAIN 29..146
FT /note="Lectin, 2nd part"
FT /evidence="ECO:0000269|PubMed:28196677"
FT /id="PRO_0000439578"
FT PROPEP 147..162
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:28196677"
FT /id="PRO_0000439579"
FT CHAIN 163..280
FT /note="Lectin, 1st part"
FT /evidence="ECO:0000269|PubMed:28196677"
FT /id="PRO_0000439580"
FT PROPEP 281..291
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:28196677"
FT /id="PRO_0000439581"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P86624"
FT BINDING 138
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:P86624"
FT BINDING 170
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P86624"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P86624"
FT BINDING 172
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P86624"
FT BINDING 174
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:P86624"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P86624"
FT BINDING 176
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P86624"
FT BINDING 181
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P86624"
FT BINDING 181
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P86624"
FT BINDING 186
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P86624"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P86624"
FT BINDING 228
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:P86624"
FT SITE 147..148
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:28196677"
FT SITE 162..163
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:28196677"
FT SITE 280..281
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:28196677"
FT STRAND 1..6
FT /evidence="ECO:0007829|PDB:6CJ9"
FT STRAND 15..26
FT /evidence="ECO:0007829|PDB:6CJ9"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:6CJ9"
FT STRAND 33..42
FT /evidence="ECO:0007829|PDB:6CJ9"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:6CJ9"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:6CJ9"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:6CJ9"
FT STRAND 97..108
FT /evidence="ECO:0007829|PDB:6CJ9"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:6CJ9"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:6CJ9"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:6CJ9"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:6CJ9"
SQ SEQUENCE 291 AA; 31368 MW; 7620BB677147439A CRC64;
MGISKKSQLV PLLAFITMFL MVVSRVSSSI ADANSLHFSF SQFSQNPKDL ILQGDATTDS
DGNLQLTRVS SDGSPQGSSV GRALFYAPVH IWEKSAVVAS FDATFTFLIK SPDRDPADGI
TFFIANTDTS IPSGSGGRLL GLFPDANIIK NSTNLDFNAA YNADTIVAVE LDSYPNTDIG
DPSYPHIGID IKSIRSKSTA RWNMQTGKVG TAHISYNSVA KRLSAVVSYS GTSSTTVSYD
VDLNNVLPEW VRVGLSATTG LYKETNTILS WSFTSKLKTN QLQDLRIASV V
