ID LECS_VATMA Reviewed; 240 AA.
AC P81371;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 22-FEB-2023, entry version 97.
DE RecName: Full=Seed lectin;
DE AltName: Full=VML;
DE Contains:
DE RecName: Full=Seed lectin alpha chain;
DE Contains:
DE RecName: Full=Seed lectin gamma chain;
DE Contains:
DE RecName: Full=Seed lectin beta chain;
OS Vatairea macrocarpa.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC vataireoid clade; Vatairea.
OX NCBI_TaxID=77050;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Seed;
RX PubMed=9559667; DOI=10.1016/s0014-5793(98)00243-9;
RA Calvete J.J., Santos C.F., Mann K., Grangeiro T.B., Nimtz M., Urbanke C.,
RA Sousa-Cavada B.;
RT "Amino acid sequence, glycan structure, and proteolytic processing of the
RT lectin of Vatairea macrocarpa seeds.";
RL FEBS Lett. 425:286-292(1998).
CC -!- FUNCTION: Lectin that binds galactose.
CC -!- SUBUNIT: Homotetramer.
CC -!- TISSUE SPECIFICITY: Seed.
CC -!- PTM: Partially N-glycosylated at Asn-111 and Asn-183 with the
CC heptasaccharide [(beta-xylosyl-1,2)(alpha-mannosyl-1,6)(alpha-mannosyl-
CC 1,3)]beta-manosyl-1,4-GlcNAC-beta-1,4-GlcNAc-beta-1,4 [alpha-fucosyl-
CC 1,3]GlcNAc. A small proportion of alpha chains are proteolytically
CC cleaved at 114-115 into gamma and beta chains. This is probably
CC dependent on the deglycosylation of Asn-111.
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 (By similarity).
CC {ECO:0000250}.
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; 4U2A; X-ray; 1.74 A; A=1-240.
DR PDB; 4U36; X-ray; 1.40 A; A=1-240.
DR PDB; 4WV8; X-ray; 1.83 A; A/B/C/D=1-240.
DR PDB; 4XTM; X-ray; 2.70 A; A=1-240.
DR PDB; 4XTP; X-ray; 1.97 A; A=1-240.
DR PDB; 4XXA; X-ray; 1.90 A; A/B=1-240.
DR PDBsum; 4U2A; -.
DR PDBsum; 4U36; -.
DR PDBsum; 4WV8; -.
DR PDBsum; 4XTM; -.
DR PDBsum; 4XTP; -.
DR PDBsum; 4XXA; -.
DR AlphaFoldDB; P81371; -.
DR SASBDB; P81371; -.
DR SMR; P81371; -.
DR UniLectin; P81371; -.
DR GlyConnect; 551; 2 N-Linked glycans.
DR GO; GO:0030246; F:carbohydrate 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 Gene3D; 2.60.120.200; -; 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 PANTHER; PTHR32401; CONCANAVALIN A-LIKE LECTIN FAMILY PROTEIN; 1.
DR PANTHER; PTHR32401:SF45; LECTIN; 1.
DR Pfam; PF00139; Lectin_legB; 1.
DR PIRSF; PIRSF002690; L-type_lectin_plant; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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; Glycoprotein; Lectin;
KW Manganese; Metal-binding.
FT CHAIN 1..240
FT /note="Seed lectin alpha chain"
FT /id="PRO_0000017656"
FT CHAIN 1..114
FT /note="Seed lectin gamma chain"
FT /id="PRO_0000017657"
FT CHAIN 115..239
FT /note="Seed lectin beta chain"
FT /id="PRO_0000017658"
FT BINDING 123
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT VARIANT 117
FT /note="I -> V"
FT VARIANT 148
FT /note="M -> K"
FT VARIANT 154
FT /note="G -> A"
FT VARIANT 168
FT /note="E -> Q"
FT UNSURE 239..240
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:4U36"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:4U36"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:4U36"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:4U36"
FT STRAND 68..76
FT /evidence="ECO:0007829|PDB:4U36"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:4U36"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:4U36"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:4U36"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:4WV8"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:4U36"
FT STRAND 137..146
FT /evidence="ECO:0007829|PDB:4U36"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:4U36"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:4U36"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:4U36"
FT STRAND 173..180
FT /evidence="ECO:0007829|PDB:4U36"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:4U36"
FT STRAND 185..192
FT /evidence="ECO:0007829|PDB:4U36"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:4U36"
FT STRAND 201..211
FT /evidence="ECO:0007829|PDB:4U36"
FT STRAND 222..232
FT /evidence="ECO:0007829|PDB:4U36"
SQ SEQUENCE 240 AA; 26197 MW; C17DF6B2568C65C1 CRC64;
SEVVSFSFTK FNPNPKDIIL QGDALVTSKG KLQLTKVKDG KPVDHSLGRA LYAAPIHIWD
DSTDRVASFA TSFSFVVEAP DESKTADGIA FFLAPPDTQP QKDGGFLGLF NDSNKSIQTV
AVEFDTFSNT WDPSARHIGI NVNSIESMKY VKWGWENGKV ANVYISYEAS TKTLTASLTY
PSNATSYIVS ANVDLKSALP EWVRVGFSAT SGLSRDHVET HDVLDWSFTS TLQAPSDDSN
//
