LECG_ARAHY
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 03-AUG-2022, entry version 127.
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}.
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 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 PRIDE; P02872; -.
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 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; 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
