AR5A_PHAVU
ID AR5A_PHAVU Reviewed; 261 AA.
AC Q42460;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Arcelin-5A;
DE Flags: Precursor;
GN Name=ARC5A; Synonyms=ARC5-1, ARC5-I;
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 / MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=cv. G02771; TISSUE=Seed;
RX PubMed=7957215; DOI=10.1111/j.1432-1033.1994.0787b.x;
RA Goossens A., Geremia R., Bauw G., van Montagu M., Angenon G.;
RT "Isolation and characterisation of arcelin-5 proteins and cDNAs.";
RL Eur. J. Biochem. 225:787-795(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE, AND SEQUENCE REVISION TO 125.
RC STRAIN=cv. G02771; TISSUE=Seed;
RA Goossens A., Ardiles Diaz W., de Keyser A., van Montagu M., Angenon G.;
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEOLYTIC PROCESSING OF C-TERMINAL.
RX PubMed=10100643; DOI=10.1016/s0014-5793(99)00212-4;
RA Young N.M., Thibault P., Watson D.C., Chrispeels M.J.;
RT "Post-translational processing of two alpha-amylase inhibitors and an
RT arcelin from the common bean, Phaseolus vulgaris.";
RL FEBS Lett. 446:203-206(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=8955116; DOI=10.1074/jbc.271.51.32796;
RA Hamelryck T.W., Poortmans F., Goossens A., Angenon G., van Montagu M.,
RA Wyns L., Loris R.;
RT "Crystal structure of arcelin-5, a lectin-like defense protein from
RT Phaseolus vulgaris.";
RL J. Biol. Chem. 271:32796-32802(1996).
CC -!- FUNCTION: Seed storage. This carbohydrate-binding lectin has toxic
CC effects on bean bruchid pests.
CC -!- SUBUNIT: Monomer.
CC -!- PTM: The C-terminal segment appears to be highly susceptible to
CC proteolysis.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR EMBL; Z36943; CAA85405.1; -; mRNA.
DR EMBL; Z50202; CAA90585.1; -; Genomic_DNA.
DR PIR; S51359; S51359.
DR PDB; 1IOA; X-ray; 2.70 A; A/B=22-261.
DR PDBsum; 1IOA; -.
DR AlphaFoldDB; Q42460; -.
DR SMR; Q42460; -.
DR EvolutionaryTrace; Q42460; -.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0045735; F:nutrient reservoir activity; 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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Lectin; Plant defense; Seed storage protein; Signal; Storage protein;
KW Toxin.
FT SIGNAL 1..21
FT CHAIN 22..254
FT /note="Arcelin-5A"
FT /id="PRO_0000017639"
FT PROPEP 255..261
FT /id="PRO_0000017640"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 167..203
FT VARIANT 252..261
FT /note="Missing (in C-terminal processing variant)"
FT VARIANT 253..261
FT /note="Missing (in C-terminal processing variant)"
FT VARIANT 254..261
FT /note="Missing (in C-terminal processing variant)"
FT VARIANT 255..261
FT /note="Missing (in C-terminal processing variant)"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:1IOA"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:1IOA"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1IOA"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:1IOA"
FT STRAND 87..95
FT /evidence="ECO:0007829|PDB:1IOA"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:1IOA"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:1IOA"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:1IOA"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:1IOA"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:1IOA"
FT TURN 147..150
FT /evidence="ECO:0007829|PDB:1IOA"
FT STRAND 151..160
FT /evidence="ECO:0007829|PDB:1IOA"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:1IOA"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:1IOA"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:1IOA"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:1IOA"
FT STRAND 189..196
FT /evidence="ECO:0007829|PDB:1IOA"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:1IOA"
FT STRAND 202..208
FT /evidence="ECO:0007829|PDB:1IOA"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:1IOA"
FT STRAND 217..227
FT /evidence="ECO:0007829|PDB:1IOA"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:1IOA"
FT STRAND 238..247
FT /evidence="ECO:0007829|PDB:1IOA"
SQ SEQUENCE 261 AA; 29121 MW; 07974BFA7381BD92 CRC64;
MASSKLLSLA LFLVLLTHAN SATETSFNFP NFHTDDKLIL QGNATISSKG QLQLTGVGSN
ELPRVDSLGR AFYSDPIQIK DSNNVASFNT NFTFIIRAKN QSISAYGLAF ALVPVNSPPQ
KKQEFLGIFN TNNPEPNART VAVVFNTFKN RIDFDKNFIK PYVNENCDFH KYNGEKTDVQ
ITYDSSNNDL RVFLHFTVSQ VKCSVSATVH LEKEVDEWVS VGFSATSGLT EDTTETHDVL
SWSFSSKFRN KLSNILLNNI L
