PHAE_PHAVU
ID PHAE_PHAVU Reviewed; 275 AA.
AC P05088;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Erythroagglutinating phytohemagglutinin;
DE AltName: Full=PHA-E;
DE Flags: Precursor;
GN Name=DLEC1;
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-33 AND ASN-81.
RC STRAIN=cv. Greensleeves;
RA Strum 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 GLYCOSYLATION AT ASN-33 AND ASN-81.
RX PubMed=3089787; DOI=10.1111/j.1432-1033.1986.tb09803.x;
RA Faye L., Sturm A., Bollini R., Vitale A., Chrispeels M.J.;
RT "The position of the oligosaccharide side-chains of phytohemagglutinin and
RT their accessibility to glycosidases determines their subsequent processing
RT in the Golgi.";
RL Eur. J. Biochem. 158:655-661(1986).
CC -!- FUNCTION: This insecticidal carbohydrate-binding lectin is toxic for
CC the cowpea weevil.
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}.
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DR EMBL; X02408; CAA26256.1; -; Genomic_DNA.
DR EMBL; K03288; AAA33759.1; -; Genomic_DNA.
DR PIR; A22826; A22826.
DR PDB; 3WCR; X-ray; 2.45 A; A/B=22-275.
DR PDB; 3WCS; X-ray; 1.75 A; A/B=22-275.
DR PDB; 3WOG; X-ray; 2.00 A; A/B=22-275.
DR PDB; 5AVA; X-ray; 3.00 A; A/B/C/D/E/F/G/H=1-275.
DR PDBsum; 3WCR; -.
DR PDBsum; 3WCS; -.
DR PDBsum; 3WOG; -.
DR PDBsum; 5AVA; -.
DR AlphaFoldDB; P05088; -.
DR SMR; P05088; -.
DR Allergome; 6155; Pha v PHA.
DR UniLectin; P05088; -.
DR GlyConnect; 497; 2 N-Linked glycans (4 sites).
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..21
FT CHAIN 22..275
FT /note="Erythroagglutinating phytohemagglutinin"
FT /id="PRO_0000017633"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:3089787, ECO:0000269|Ref.2"
FT /id="CAR_000119"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3089787, ECO:0000269|Ref.2"
FT /id="CAR_000120"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT STRAND 23..31
FT /evidence="ECO:0007829|PDB:3WCS"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:3WCS"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:3WCS"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:3WCS"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:3WCS"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:3WCS"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:3WCS"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:3WCS"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:3WCS"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:3WCS"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:3WCR"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:3WCS"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:3WCS"
FT STRAND 160..169
FT /evidence="ECO:0007829|PDB:3WCS"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:3WCS"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:3WCS"
FT TURN 192..195
FT /evidence="ECO:0007829|PDB:3WCS"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:3WCS"
FT TURN 204..207
FT /evidence="ECO:0007829|PDB:3WCS"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:3WCS"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:3WCS"
FT STRAND 224..234
FT /evidence="ECO:0007829|PDB:3WCS"
FT STRAND 245..255
FT /evidence="ECO:0007829|PDB:3WCS"
FT HELIX 266..270
FT /evidence="ECO:0007829|PDB:3WCS"
SQ SEQUENCE 275 AA; 29746 MW; D1BBA1B0E4B2702E CRC64;
MASSNLLSLA LFLVLLTHAN SASQTSFSFQ RFNETNLILQ RDATVSSKGQ LRLTNVNDNG
EPTLSSLGRA FYSAPIQIWD NTTGAVAASP TSFTFNIDVP NNSGPADGLA FVLLPVGSQP
KDKGGLLGLF NNYKYDSNAH TVAVEFDTLY NVHWDPKPRH IGIDVNSIKS IKTTTWDFVK
GENAEVLITY DSSTKLLVAS LVYPSLKTSF IVSDTVDLKS VLPEWVIVGF TATTGITKGN
VETNDILSWS FASKLSDGTT SEALNLANFA LNQIL
