LEC_VICFA
ID LEC_VICFA Reviewed; 233 AA.
AC P02871;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Favin;
DE AltName: Full=Lectin;
DE Contains:
DE RecName: Full=Favin beta chain;
DE Contains:
DE RecName: Full=Favin alpha chain;
OS Vicia faba (Broad bean) (Faba vulgaris).
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; Hologalegina; IRL clade; Fabeae; Vicia.
OX NCBI_TaxID=3906;
RN [1]
RP PROTEIN SEQUENCE OF 1-182, AND SEQUENCE REVISION.
RX PubMed=7068646; DOI=10.1016/s0021-9258(18)34747-1;
RA Hopp T.P., Hemperly J.J., Cunningham B.A.;
RT "Amino acid sequence and variant forms of favin, a lectin from Vicia
RT faba.";
RL J. Biol. Chem. 257:4473-4483(1982).
RN [2]
RP PRELIMINARY PROTEIN SEQUENCE OF 1-182.
RX PubMed=16592676; DOI=10.1073/pnas.76.7.3218;
RA Cunningham B.A., Hemperly J.J., Hopp T.P., Edelman G.M.;
RT "Favin versus concanavalin A: circularly permuted amino acid sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 76:3218-3222(1979).
RN [3]
RP PROTEIN SEQUENCE OF 183-233.
RX PubMed=447749; DOI=10.1016/s0021-9258(18)50439-7;
RA Hemperly J.J., Hopp T.P., Becker J.W., Cunningham B.A.;
RT "The chemical characterization of favin, a lectin isolated from Vicia
RT faba.";
RL J. Biol. Chem. 254:6803-6810(1979).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH GLUCOSE.
RX PubMed=3775378; DOI=10.1126/science.3775378;
RA Reeke G.N. Jr., Becker J.W.;
RT "Three-dimensional structure of favin: saccharide binding-cyclic
RT permutation in leguminous lectins.";
RL Science 234:1108-1111(1986).
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000269|PubMed:3775378}.
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: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 PIR; A92369; FVVFBA.
DR PDB; 2B7Y; X-ray; 3.00 A; A/C=1-182, B/D=183-233.
DR PDBsum; 2B7Y; -.
DR AlphaFoldDB; P02871; -.
DR SMR; P02871; -.
DR UniLectin; P02871; -.
DR iPTMnet; P02871; -.
DR EvolutionaryTrace; P02871; -.
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 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; Glycoprotein; Lectin;
KW Manganese; Metal-binding.
FT CHAIN 1..182
FT /note="Favin beta chain"
FT /id="PRO_0000017648"
FT CHAIN 183..233
FT /note="Favin alpha chain"
FT /id="PRO_0000017649"
FT BINDING 120
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 130
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 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7068646"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:2B7Y"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:2B7Y"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:2B7Y"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:2B7Y"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:2B7Y"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:2B7Y"
FT STRAND 63..73
FT /evidence="ECO:0007829|PDB:2B7Y"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:2B7Y"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:2B7Y"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:2B7Y"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:2B7Y"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:2B7Y"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:2B7Y"
FT STRAND 137..146
FT /evidence="ECO:0007829|PDB:2B7Y"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:2B7Y"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:2B7Y"
FT TURN 169..172
FT /evidence="ECO:0007829|PDB:2B7Y"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:2B7Y"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:2B7Y"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:2B7Y"
FT STRAND 200..209
FT /evidence="ECO:0007829|PDB:2B7Y"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:2B7Y"
FT STRAND 216..227
FT /evidence="ECO:0007829|PDB:2B7Y"
SQ SEQUENCE 233 AA; 25509 MW; 341F96AF7D477B00 CRC64;
TDEITSFSIP KFRPDQPNLI FQGGGYTTKE KLTLTKAVKN TVGRALYSLP IHIWDSETGN
VADFTTTFIF VIDAPNGYNV ADGFTFFIAP VDTKPQTGGG YLGVFNGKDY DKTAQTVAVE
FDTFYNAAWD PSNGKRHIGI DVNTIKSIST KSWNLQNGEE AHVAISFNAT TNVLSVTLLY
PNLTGYTLSE VVPLKDVVPE WVRIGFSATT GAEYATHEVL SWTFLSELTG PSN
