ARC1_PHAVU
ID ARC1_PHAVU Reviewed; 265 AA.
AC P19329;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Arcelin-1;
DE Flags: Precursor;
GN Name=ARC1; Synonyms=ARC;
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, AND PROTEIN SEQUENCE OF 22-69.
RC STRAIN=cv. Sanilac;
RA Osborn T.C., Alexander D.C., Sun S.S.M., Cardona C., Bliss F.A.;
RT "Insecticidal activity and lectin homology of arcelin seed protein.";
RL Science 240:207-210(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16668479; DOI=10.1104/pp.97.2.839;
RA Anthony J.L., Vonder Haar R.A., Hall T.C.;
RT "Nucleotide sequence of a genomic clone encoding arcelin, a lectin-like
RT seed protein from Phaseolus vulgaris.";
RL Plant Physiol. 97:839-840(1991).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RC STRAIN=cv. RAZ-2;
RX PubMed=9582323; DOI=10.1074/jbc.273.21.12914;
RA Mourey L., Pedelacq J.-D., Birck C., Fabre C., Rouge P., Samama J.-P.;
RT "Crystal structure of the arcelin-1 dimer from Phaseolus vulgaris at 1.9-A
RT resolution.";
RL J. Biol. Chem. 273:12914-12922(1998).
CC -!- FUNCTION: Seed storage. This carbohydrate-binding lectin has toxic
CC effects on an important bean bruchid pest, Z.subfasciatus. Antibiosis
CC properties of legume lectins are proposed to be due to the lysis of
CC epithelial cells of the intestine by binding to the carbohydrate
CC moieties of these proteins.
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR EMBL; M19430; AAA33752.1; -; mRNA.
DR EMBL; M68913; AAA33753.1; -; Genomic_DNA.
DR PIR; A40111; A40111.
DR PDB; 1AVB; X-ray; 1.90 A; A/B=22-247.
DR PDBsum; 1AVB; -.
DR AlphaFoldDB; P19329; -.
DR SMR; P19329; -.
DR EvolutionaryTrace; P19329; -.
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; 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; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Lectin; Plant defense; Seed storage protein; Signal; Storage protein;
KW Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|Ref.1"
FT CHAIN 22..265
FT /note="Arcelin-1"
FT /id="PRO_0000017636"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 165..201
FT STRAND 23..31
FT /evidence="ECO:0007829|PDB:1AVB"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:1AVB"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:1AVB"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1AVB"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:1AVB"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:1AVB"
FT STRAND 82..98
FT /evidence="ECO:0007829|PDB:1AVB"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:1AVB"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:1AVB"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:1AVB"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:1AVB"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:1AVB"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:1AVB"
FT STRAND 149..158
FT /evidence="ECO:0007829|PDB:1AVB"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:1AVB"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:1AVB"
FT STRAND 174..182
FT /evidence="ECO:0007829|PDB:1AVB"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:1AVB"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:1AVB"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:1AVB"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:1AVB"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:1AVB"
FT STRAND 215..225
FT /evidence="ECO:0007829|PDB:1AVB"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:1AVB"
FT STRAND 233..246
FT /evidence="ECO:0007829|PDB:1AVB"
SQ SEQUENCE 265 AA; 29255 MW; EF8A35BE388AAECA CRC64;
MASSNLLTLA LFLVLLTHAN SSNDASFNVE TFNKTNLILQ GDATVSSEGH LLLTNVKGNE
EDSMGRAFYS APIQINDRTI DNLASFSTNF TFRINAKNIE NSAYGLAFAL VPVGSRPKLK
GRYLGLFNTT NYDRDAHTVA VVFDTVSNRI EIDVNSIRPI ATESCNFGHN NGEKAEVRIT
YDSPKNDLRV SLLYPSSEEK CHVSATVPLE KEVEDWVSVG FSATSGSKKE TTETHNVLSW
SFSSNFINFK GKKSERSNIL LNKIL
