PHAL_PHAVU
ID PHAL_PHAVU Reviewed; 272 AA.
AC P05087;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Leucoagglutinating phytohemagglutinin;
DE Short=PHA-L;
DE Flags: Precursor;
GN Name=DLEC2;
OS Phaseolus vulgaris (Kidney bean) (French bean).
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; Phaseolus.
OX NCBI_TaxID=3885;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2990911; DOI=10.1002/j.1460-2075.1985.tb03714.x;
RA Hoffman L.M., Donaldson D.D.;
RT "Characterization of two Phaseolus vulgaris phytohemagglutinin genes
RT closely linked on the chromosome.";
RL EMBO J. 4:883-889(1985).
RN [2]
RP GLYCOSYLATION AT ASN-32 AND ASN-80.
RC STRAIN=cv. Greensleeves;
RA Sturm A., Chrispeels M.J.;
RT "The high mannose oligosaccharide of phytohemagglutinin is attached to
RT asparagine 12 and the modified oligosaccharide to asparagine 60.";
RL Plant Physiol. 80:320-322(1986).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=8702788; DOI=10.1074/jbc.271.34.20479;
RA Hamelryck T.W., Dao-Thi M.H., Poortmans F., Chrispeels M.J., Wyns L.,
RA Loris R.;
RT "The crystallographic structure of phytohemagglutinin-L.";
RL J. Biol. Chem. 271:20479-20485(1996).
CC -!- FUNCTION: This insecticidal carbohydrate-binding lectin is toxic for
CC the cowpea weevil.
CC -!- SUBUNIT: Homotetramer.
CC -!- PTM: N-glycosylated on Asn-80; contains xylose. {ECO:0000269|Ref.2}.
CC -!- MISCELLANEOUS: Antibiosis properties of legume lectins are proposed to
CC be due to the lysis of epithelial cells of the intestine by binding to
CC the carbohydrate moieties of these proteins.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=PHA-L;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_pla_other_418";
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; X02409; CAA26257.1; -; Genomic_DNA.
DR EMBL; K03289; AAA33760.1; -; Genomic_DNA.
DR PIR; B22826; B22826.
DR RefSeq; XP_007152772.1; XM_007152710.1.
DR PDB; 1FAT; X-ray; 2.80 A; A/B/C/D=21-272.
DR PDB; 1G8W; X-ray; 2.80 A; A/B/C/D=21-253.
DR PDBsum; 1FAT; -.
DR PDBsum; 1G8W; -.
DR AlphaFoldDB; P05087; -.
DR SMR; P05087; -.
DR IntAct; P05087; 1.
DR STRING; 3885.XP_007152772.1; -.
DR Allergome; 6155; Pha v PHA.
DR UniLectin; P05087; -.
DR GlyConnect; 497; 2 N-Linked glycans (4 sites).
DR EnsemblPlants; ESW24766; ESW24766; PHAVU_004G158300g.
DR GeneID; 18633199; -.
DR Gramene; ESW24766; ESW24766; PHAVU_004G158300g.
DR KEGG; pvu:PHAVU_004G158300g; -.
DR eggNOG; ENOG502QTX3; Eukaryota.
DR OMA; DHPSFQP; -.
DR OrthoDB; 1732410at2759; -.
DR EvolutionaryTrace; P05087; -.
DR PRO; PR:P05087; -.
DR GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; 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; Glycoprotein; Lectin; Mannose-binding; Plant defense; Signal;
KW Toxin.
FT SIGNAL 1..20
FT CHAIN 21..272
FT /note="Leucoagglutinating phytohemagglutinin"
FT /id="PRO_0000017634"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|Ref.2"
FT /id="CAR_000121"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|Ref.2"
FT /id="CAR_000122"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:1FAT"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:1FAT"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:1FAT"
FT STRAND 66..76
FT /evidence="ECO:0007829|PDB:1FAT"
FT TURN 80..83
FT /evidence="ECO:0007829|PDB:1FAT"
FT STRAND 84..95
FT /evidence="ECO:0007829|PDB:1FAT"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:1FAT"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:1FAT"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:1FAT"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:1FAT"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:1FAT"
FT STRAND 157..166
FT /evidence="ECO:0007829|PDB:1FAT"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:1FAT"
FT STRAND 180..188
FT /evidence="ECO:0007829|PDB:1FAT"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:1FAT"
FT STRAND 193..200
FT /evidence="ECO:0007829|PDB:1FAT"
FT TURN 201..204
FT /evidence="ECO:0007829|PDB:1FAT"
FT STRAND 205..212
FT /evidence="ECO:0007829|PDB:1FAT"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:1FAT"
FT STRAND 221..231
FT /evidence="ECO:0007829|PDB:1FAT"
FT STRAND 242..252
FT /evidence="ECO:0007829|PDB:1FAT"
SQ SEQUENCE 272 AA; 29556 MW; 9DBF7D3077A067D7 CRC64;
MASSKFFTVL FLVLLTHANS SNDIYFNFQR FNETNLILQR DASVSSSGQL RLTNLNGNGE
PRVGSLGRAF YSAPIQIWDN TTGTVASFAT SFTFNIQVPN NAGPADGLAF ALVPVGSQPK
DKGGFLGLFD GSNSNFHTVA VEFDTLYNKD WDPTERHIGI DVNSIRSIKT TRWDFVNGEN
AEVLITYDSS TNLLVASLVY PSQKTSFIVS DTVDLKSVLP EWVSVGFSAT TGINKGNVET
NDVLSWSFAS KLSDGTTSEG LNLANLVLNK IL
