ID   LECG_ARAHY              Reviewed;         273 AA.
AC   P02872;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 3.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Galactose-binding lectin;
DE   AltName: Full=Agglutinin;
DE   AltName: Full=PNA;
DE   Flags: Precursor;
OS   Arachis hypogaea (Peanut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX   NCBI_TaxID=3818;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Seed;
RX   PubMed=1339358; DOI=10.1016/0014-5793(92)80764-8;
RA   Rodriguez-Arango E., Arango R., Adar R., Galili G., Sharon N.;
RT   "Cloning, sequence analysis and expression in Escherichia coli of the cDNA
RT   encoding a precursor of peanut agglutinin.";
RL   FEBS Lett. 307:185-189(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 24-273.
RC   TISSUE=Seed;
RX   PubMed=2013286; DOI=10.1111/j.1432-1033.1991.tb15859.x;
RA   Young N.M., Johnston R.A.Z., Watson D.C.;
RT   "The amino acid sequence of peanut agglutinin.";
RL   Eur. J. Biochem. 196:631-637(1991).
RN   [3]
RP   PRELIMINARY PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. Shulamit;
RA   Lauwereys M., Foriers A., Sharon N., Strosberg A.D.;
RT   "Sequence studies of peanut agglutinin.";
RL   FEBS Lett. 181:241-244(1985).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
RX   PubMed=8656429; DOI=10.1006/jmbi.1996.0319;
RA   Banerjee R., Das K., Ravishankar R., Suguna K., Surolia A., Vijayan M.;
RT   "Conformation, protein-carbohydrate interactions and a novel subunit
RT   association in the refined structure of peanut lectin-lactose complex.";
RL   J. Mol. Biol. 259:281-296(1996).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX   PubMed=10417405; DOI=10.1107/s0907444999006587;
RA   Ravishankar R., Suguna K., Surolia A., Vijayan M.;
RT   "Structures of the complexes of peanut lectin with methyl-beta-galactose
RT   and N-acetyllactosamine and a comparative study of carbohydrate binding in
RT   Gal/GalNAc-specific legume lectins.";
RL   Acta Crystallogr. D 55:1375-1382(1999).
CC   -!- FUNCTION: D-galactose specific lectin.
CC   -!- SUBUNIT: Homotetramer.
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}.
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DR   EMBL; S42352; AAB22817.1; -; mRNA.
DR   PIR; A03364; LNNPG.
DR   PIR; S24044; S24044.
DR   PDB; 1BZW; X-ray; 2.70 A; A/B/C/D=24-255.
DR   PDB; 1CIW; X-ray; 2.70 A; A/B/C/D=24-259.
DR   PDB; 1CQ9; X-ray; 3.50 A; A/B/C/D=24-259.
DR   PDB; 1CR7; X-ray; 2.60 A; A/B/C/D/E/F/G/H=24-259.
DR   PDB; 1QF3; X-ray; 2.80 A; A/B/C/D=24-259.
DR   PDB; 1RIR; X-ray; 2.90 A; A/B/C/D=24-259.
DR   PDB; 1RIT; X-ray; 2.85 A; A/B/C/D=24-259.
DR   PDB; 1V6I; X-ray; 2.15 A; A/B/C/D=24-255.
DR   PDB; 1V6J; X-ray; 2.90 A; A/B/C/D=24-255.
DR   PDB; 1V6K; X-ray; 2.40 A; A/B/C/D=24-255.
DR   PDB; 1V6L; X-ray; 2.50 A; A/B/C/D=24-255.
DR   PDB; 1V6M; X-ray; 2.70 A; A/B/C/D/E/F/G/H=24-255.
DR   PDB; 1V6N; X-ray; 3.50 A; A/B/C/D/E/F/G/H=24-255.
DR   PDB; 1V6O; X-ray; 3.00 A; A/B/C/D/E/F/G/H=24-255.
DR   PDB; 2DH1; X-ray; 7.65 A; A/B/C/D=24-259.
DR   PDB; 2DV9; X-ray; 2.48 A; A/B/C/D=24-259.
DR   PDB; 2DVA; X-ray; 2.20 A; A/B/C/D=24-259.
DR   PDB; 2DVB; X-ray; 2.25 A; A/B/C/D=24-259.
DR   PDB; 2DVD; X-ray; 2.25 A; A/B/C/D=24-259.
DR   PDB; 2DVF; X-ray; 2.74 A; A/B/C/D=24-259.
DR   PDB; 2DVG; X-ray; 2.78 A; A/B/C/D=24-259.
DR   PDB; 2PEL; X-ray; 2.25 A; A/B/C/D=24-259.
DR   PDB; 2TEP; X-ray; 2.50 A; A/B/C/D=24-259.
DR   PDB; 6V95; X-ray; 1.78 A; A/B/C/D=24-259.
DR   PDB; 6VAV; X-ray; 1.85 A; A/B/C/D=24-259.
DR   PDB; 6VAW; X-ray; 1.75 A; A/B/C/D=24-259.
DR   PDB; 6VC3; X-ray; 1.95 A; A/B/C/D=24-259.
DR   PDB; 6VC4; X-ray; 1.90 A; A/B/C/D=24-259.
DR   PDB; 6VGF; X-ray; 1.83 A; A/B/C/D=24-259.
DR   PDBsum; 1BZW; -.
DR   PDBsum; 1CIW; -.
DR   PDBsum; 1CQ9; -.
DR   PDBsum; 1CR7; -.
DR   PDBsum; 1QF3; -.
DR   PDBsum; 1RIR; -.
DR   PDBsum; 1RIT; -.
DR   PDBsum; 1V6I; -.
DR   PDBsum; 1V6J; -.
DR   PDBsum; 1V6K; -.
DR   PDBsum; 1V6L; -.
DR   PDBsum; 1V6M; -.
DR   PDBsum; 1V6N; -.
DR   PDBsum; 1V6O; -.
DR   PDBsum; 2DH1; -.
DR   PDBsum; 2DV9; -.
DR   PDBsum; 2DVA; -.
DR   PDBsum; 2DVB; -.
DR   PDBsum; 2DVD; -.
DR   PDBsum; 2DVF; -.
DR   PDBsum; 2DVG; -.
DR   PDBsum; 2PEL; -.
DR   PDBsum; 2TEP; -.
DR   PDBsum; 6V95; -.
DR   PDBsum; 6VAV; -.
DR   PDBsum; 6VAW; -.
DR   PDBsum; 6VC3; -.
DR   PDBsum; 6VC4; -.
DR   PDBsum; 6VGF; -.
DR   AlphaFoldDB; P02872; -.
DR   SMR; P02872; -.
DR   IntAct; P02872; 1.
DR   Allergome; 1050; Ara h Agglutinin.
DR   UniLectin; P02872; -.
DR   OrthoDB; 1131667at2759; -.
DR   EvolutionaryTrace; P02872; -.
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:SF26; LECTIN 2; 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; Lectin; Manganese;
KW   Metal-binding; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:2013286"
FT   CHAIN           24..273
FT                   /note="Galactose-binding lectin"
FT                   /id="PRO_0000017583"
FT   BINDING         144
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   BINDING         146
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT   BINDING         146
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   BINDING         148
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT   BINDING         150
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT   BINDING         155
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT   BINDING         155
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   BINDING         160
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   VARIANT         115
FT                   /note="E -> V (in minor form)"
FT   VARIANT         172
FT                   /note="K -> A (in minor form)"
FT   VARIANT         185
FT                   /note="K -> I (in minor form)"
FT   VARIANT         235..236
FT                   /note="LG -> RA (in minor form)"
FT   STRAND          25..33
FT                   /evidence="ECO:0007829|PDB:6VAW"
FT   STRAND          41..45
FT                   /evidence="ECO:0007829|PDB:6VAW"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:1V6N"
FT   STRAND          60..64
FT                   /evidence="ECO:0007829|PDB:1V6N"
FT   STRAND          66..73
FT                   /evidence="ECO:0007829|PDB:6VAW"
FT   TURN            80..82
FT                   /evidence="ECO:0007829|PDB:6VAW"
FT   STRAND          87..97
FT                   /evidence="ECO:0007829|PDB:6VAW"
FT   STRAND          100..103
FT                   /evidence="ECO:0007829|PDB:6VAW"
FT   STRAND          107..114
FT                   /evidence="ECO:0007829|PDB:6VAW"
FT   HELIX           126..128
FT                   /evidence="ECO:0007829|PDB:6VAW"
FT   TURN            129..131
FT                   /evidence="ECO:0007829|PDB:6VAW"
FT   STRAND          136..146
FT                   /evidence="ECO:0007829|PDB:6VAW"
FT   HELIX           151..153
FT                   /evidence="ECO:0007829|PDB:6VAW"
FT   STRAND          160..169
FT                   /evidence="ECO:0007829|PDB:6VAW"
FT   STRAND          171..175
FT                   /evidence="ECO:0007829|PDB:6VAW"
FT   STRAND          182..191
FT                   /evidence="ECO:0007829|PDB:6VAW"
FT   TURN            192..195
FT                   /evidence="ECO:0007829|PDB:6VAW"
FT   STRAND          196..202
FT                   /evidence="ECO:0007829|PDB:6VAW"
FT   STRAND          204..206
FT                   /evidence="ECO:0007829|PDB:1V6N"
FT   STRAND          208..214
FT                   /evidence="ECO:0007829|PDB:6VAW"
FT   HELIX           217..220
FT                   /evidence="ECO:0007829|PDB:6VAW"
FT   STRAND          223..232
FT                   /evidence="ECO:0007829|PDB:6VAW"
FT   STRAND          235..237
FT                   /evidence="ECO:0007829|PDB:6VAW"
FT   STRAND          240..252
FT                   /evidence="ECO:0007829|PDB:6VAW"
SQ   SEQUENCE   273 AA;  29325 MW;  05A0B1A8FAC7B159 CRC64;
     MKPFCVFLTF FLLLAASSKK VDSAETVSFN FNSFSEGNPA INFQGDVTVL SNGNIQLTNL
     NKVNSVGRVL YAMPVRIWSS ATGNVASFLT SFSFEMKDIK DYDPADGIIF FIAPEDTQIP
     AGSIGGGTLG VSDTKGAGHF VGVEFDTYSN SEYNDPPTDH VGIDVNSVDS VKTVPWNSVS
     GAVVKVTVIY DSSTKTLSVA VTNDNGDITT IAQVVDLKAK LPERVKFGFS ASGSLGGRQI
     HLIRSWSFTS TLITTTRRSI DNNEKKIMNM ASA
//