LECA_DIORF
ID LECA_DIORF Reviewed; 237 AA.
AC C0HK81;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Lectin {ECO:0000303|PubMed:26464029};
DE Short=DrfL {ECO:0000303|PubMed:26464029};
OS Dioclea reflexa (Sea purse).
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=1048258;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY, AND X-RAY
RP CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-237 IN COMPLEX WITH CARBOHYDRATE;
RP CALCIUM AND MANGANESE.
RC TISSUE=Seed {ECO:0000303|PubMed:28130130};
RX PubMed=28130130; DOI=10.1016/j.ijbiomac.2017.01.092;
RA Pinto-Junior V.R., Osterne V.J., Santiago M.Q., Correia J.L.,
RA Pereira-Junior F.N., Leal R.B., Pereira M.G., Chicas L.S., Nagano C.S.,
RA Rocha B.A., Silva-Filho J.C., Ferreira W.P., Rocha C.R., Nascimento K.S.,
RA Assreuy A.M., Cavada B.S.;
RT "Structural studies of a vasorelaxant lectin from Dioclea reflexa Hook
RT seeds: Crystal structure, molecular docking and dynamics.";
RL Int. J. Biol. Macromol. 98:12-23(2017).
RN [2] {ECO:0000305}
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MASS SPECTROMETRY.
RX PubMed=26464029; DOI=10.1002/jmr.2512;
RA Pinto-Junior V.R., Correia J.L., Pereira R.I., Pereira-Junior F.N.,
RA Santiago M.Q., Osterne V.J., Madeira J.C., Cajazeiras J.B., Nagano C.S.,
RA Delatorre P., Assreuy A.M., Nascimento K.S., Cavada B.S.;
RT "Purification and molecular characterization of a novel mannose-specific
RT lectin from Dioclea reflexa hook seeds with inflammatory activity.";
RL J. Mol. Recognit. 29:134-141(2016).
CC -!- FUNCTION: D-mannose/D-glucose-binding lectin with hemagglutinating
CC activity towards rabbit and human erythrocytes. In rats, induces dose-
CC dependent paw edema. Has low cytotoxicity against Artemisia sp.
CC {ECO:0000269|PubMed:26464029}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH for hemagglutinating activity is between pH 5 and pH 7.
CC Activity quickly decreases outside this range.
CC {ECO:0000269|PubMed:26464029};
CC Temperature dependence:
CC Hemagglutinating activity is stable up to 50 degrees Celsius and is
CC lost after incubation for 1 hour at 80 degrees Celsius.
CC {ECO:0000269|PubMed:26464029};
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000269|PubMed:28130130}.
CC -!- PTM: 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. Residues 1-118 of the mature chain,
CC as displayed here, probably constitute the beta chain in the
CC propeptide, residues 119-237 the gamma chain.
CC {ECO:0000303|PubMed:26464029, ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=25562; Mass_error=2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:26464029};
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:0000305|PubMed:26464029}.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PDB; 5TG3; X-ray; 1.80 A; A/B/C/D=1-237.
DR PDBsum; 5TG3; -.
DR AlphaFoldDB; C0HK81; -.
DR SMR; C0HK81; -.
DR UniLectin; C0HK81; -.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0005537; F:mannose binding; IDA:UniProtKB.
DR InterPro; IPR013320; ConA-like_dom_sf.
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; 2.
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.
FT CHAIN 1..237
FT /note="Lectin"
FT /evidence="ECO:0000269|PubMed:28130130"
FT /id="PRO_0000439557"
FT BINDING 8
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:28130130,
FT ECO:0007744|PDB:5TG3"
FT BINDING 10
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:28130130,
FT ECO:0007744|PDB:5TG3"
FT BINDING 10
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:28130130,
FT ECO:0007744|PDB:5TG3"
FT BINDING 12
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:28130130,
FT ECO:0007744|PDB:5TG3"
FT BINDING 12
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:28130130,
FT ECO:0007744|PDB:5TG3"
FT BINDING 14
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:28130130,
FT ECO:0007744|PDB:5TG3"
FT BINDING 14
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:28130130,
FT ECO:0007744|PDB:5TG3"
FT BINDING 19
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:28130130,
FT ECO:0007744|PDB:5TG3"
FT BINDING 19
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:28130130,
FT ECO:0007744|PDB:5TG3"
FT BINDING 24
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:28130130,
FT ECO:0007744|PDB:5TG3"
FT BINDING 98..100
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:28130130,
FT ECO:0007744|PDB:5TG3"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:28130130,
FT ECO:0007744|PDB:5TG3"
FT BINDING 227
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:28130130,
FT ECO:0007744|PDB:5TG3"
FT BINDING 228
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:28130130,
FT ECO:0007744|PDB:5TG3"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:5TG3"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:5TG3"
FT STRAND 24..33
FT /evidence="ECO:0007829|PDB:5TG3"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:5TG3"
FT STRAND 46..55
FT /evidence="ECO:0007829|PDB:5TG3"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:5TG3"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:5TG3"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:5TG3"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:5TG3"
FT STRAND 87..96
FT /evidence="ECO:0007829|PDB:5TG3"
FT STRAND 105..116
FT /evidence="ECO:0007829|PDB:5TG3"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:5TG3"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:5TG3"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:5TG3"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:5TG3"
FT STRAND 187..198
FT /evidence="ECO:0007829|PDB:5TG3"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:5TG3"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:5TG3"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:5TG3"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:5TG3"
SQ SEQUENCE 237 AA; 25562 MW; F75DF42299DFF6FD CRC64;
ADTIVAVELD SYPNTDIGDP NYPHIGIDIK SVRSKSTARW NMQTGKVGTV HISYNSVSKR
LSAVVSYSGS SSTTVSYDVD LNNVLPEWVR VGLSATTGLY KQTNTILSWS FTSKLKTNSI
ADENSLHFSF HKFSQNPKDL ILQGDASTDS DGNLQLTKVS SSGDPQGNSV GRALFYAPVH
IWEKSAVVAS FDATFTFLIK SPDREPADGI TFFIANTDTT IPSGSGGRLL GLFPDAN
