ID LEA1_PHAVU Reviewed; 246 AA. AC P02873; Q8RVY2; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 02-SEP-2026, entry version 143. DE RecName: Full=Alpha-amylase inhibitor 1; DE Short=Alpha-AI-1; DE Short=Alpha-AI1; DE AltName: Full=Lectin; DE Contains: DE RecName: Full=Alpha-amylase inhibitor 1 chain 1; DE Contains: DE RecName: Full=Alpha-amylase inhibitor 1 chain 2; DE Flags: Precursor; GN Name=LLP; Synonyms=Alpha-AI1; 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]. RC STRAIN=cv. Tendergreen; RX PubMed=6090563; RA Hoffman L.M.; RT "Structure of a chromosomal Phaseolus vulgaris lectin gene and its RT transcript."; RL J. Mol. Appl. Genet. 2:447-453(1984). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Tendergreen; RX PubMed=6897567; DOI=10.1093/nar/10.23.7819; RA Hoffman L.M., Ma Y., Barker R.F.; RT "Molecular cloning of Phaseolus vulgaris lectin mRNA and use of cDNA as a RT probe to estimate lectin transcript levels in various tissues."; RL Nucleic Acids Res. 10:7819-7828(1982). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-246. RC TISSUE=Leaf; RA Lioi L., Galasso I., Lanave C., Sparvoli F., Bollini R.; RT "Arcelin and other members of lectin family in wild Phaseolus vulgaris."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP PROTEIN SEQUENCE OF 24-34 AND 101-115. RC STRAIN=cv. Greensleeves; TISSUE=Seed; RX PubMed=2682631; DOI=10.1073/pnas.86.20.7885; RA Moreno J., Chrispeels M.J.; RT "A lectin gene encodes the alpha-amylase inhibitor of the common bean."; RL Proc. Natl. Acad. Sci. U.S.A. 86:7885-7889(1989). RN [5] RP PROTEIN SEQUENCE OF 24-32 AND 101-109. RC STRAIN=cv. Tebo; TISSUE=Seed; RX PubMed=7763497; DOI=10.1271/bbb.57.297; RA Yamaguchi H.; RT "Isolation and characterization of the subunits of a heat-labile alpha- RT amylase inhibitor from Phaseolus vulgaris white kidney bean."; RL Biosci. Biotechnol. Biochem. 57:297-302(1993). RN [6] RP PROTEIN SEQUENCE OF 24-99 AND 101-231, FUNCTION, SUBUNIT, AND RP GLYCOSYLATION. RC STRAIN=cv. Magna; TISSUE=Seed; RA Kluh I., Horn M., Voburka Z.; RL Submitted (DEC-2003) to UniProtKB. RN [7] RP CHARACTERIZATION. RX PubMed=7772866; DOI=10.1093/glycob/5.1.45; RA Mirkov T.E., Evans S.V., Wahlstrom J., Gomez L., Young N.M., RA Chrispeels M.J.; RT "Location of the active site of the bean alpha-amylase inhibitor and RT involvement of a Trp, Arg, Tyr triad."; RL Glycobiology 5:45-50(1995). RN [8] RP PROTEOLYTIC PROCESSING OF C-TERMINAL, AND GLYCOSYLATION AT ASN-35; ASN-88 RP AND ASN-163. 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 [9] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF COMPLEX WITH PIG ALPHA-AMYLASE. RX PubMed=8994970; DOI=10.1016/s0969-2126(96)00151-7; RA Bompard-Gilles C., Rousseau P., Rouge P., Payan F.; RT "Substrate mimicry in the active center of a mammalian alpha-amylase: RT structural analysis of an enzyme-inhibitor complex."; RL Structure 4:1441-1452(1996). CC -!- FUNCTION: Lectin and alpha-amylase inhibitor. Acts as a defensive CC protein against insects. {ECO:0000269|Ref.6}. CC -!- SUBUNIT: Heterodimer of chain 1 and chain 2. {ECO:0000269|Ref.6}. CC -!- PTM: Proteolytic processing yields active form. CC {ECO:0000269|PubMed:10100643}. CC -!- BIOTECHNOLOGY: Sold as a diet aid under the name of 'Phaseolamin' or CC 'Phase 2'. 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; J01261; AAA33769.1; -; Genomic_DNA. DR EMBL; AJ439614; CAD28835.1; -; Genomic_DNA. DR PIR; A03365; LNFB. DR PDB; 1DHK; X-ray; 1.85 A; B=24-246. DR PDB; 1VIW; X-ray; 3.00 A; B=24-228. DR AlphaFoldDB; P02873; -. DR SMR; P02873; -. DR MINT; P02873; -. DR Allergome; 2946; Pha v aAI. DR Allergome; 8208; Pha v aAI.0101. DR GlyConnect; P02873; 8 N-Linked glycans. DR GlyCosmos; P02873; 3 sites, 14 glycans. DR iPTMnet; P02873; -. DR EvolutionaryTrace; P02873; -. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1. DR Gene3D; 2.60.120.200; -; 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 InterPro; IPR050258; Leguminous_Lectin. DR PANTHER; PTHR32401; CONCANAVALIN A-LIKE LECTIN FAMILY PROTEIN; 1. DR PANTHER; PTHR32401:SF45; LECTIN; 1. DR Pfam; PF00139; Lectin_legB; 2. DR PIRSF; PIRSF002690; L-type_lectin_plant; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR PROSITE; PS00308; LECTIN_LEGUME_ALPHA; 1. DR PROSITE; PS00307; LECTIN_LEGUME_BETA; 1. DR PDBsum; 1DHK; -. DR PDBsum; 1VIW; -. PE 1: Evidence at protein level; KW 3D-structure; Alpha-amylase inhibitor; Direct protein sequencing; KW Glycoprotein; Lectin; Signal. FT SIGNAL 1..23 FT /evidence="ECO:0000269|PubMed:2682631, FT ECO:0000269|PubMed:7763497, ECO:0000269|Ref.6" FT CHAIN 24..100 FT /note="Alpha-amylase inhibitor 1 chain 1" FT /id="PRO_0000017627" FT CHAIN 101..239 FT /note="Alpha-amylase inhibitor 1 chain 2" FT /id="PRO_0000017628" FT PROPEP 240..246 FT /id="PRO_0000017629" FT CARBOHYD 35 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:10100643" FT CARBOHYD 88 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:10100643" FT CARBOHYD 163 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:10100643" FT CONFLICT 30 FT /note="I -> N (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 73 FT /note="Q -> R (in Ref. 3; CAD28835)" FT /evidence="ECO:0000305" FT CONFLICT 142 FT /note="K -> E (in Ref. 3; CAD28835)" FT /evidence="ECO:0000305" FT CONFLICT 196 FT /note="D -> N (in Ref. 2)" FT /evidence="ECO:0000305" FT STRAND 28..33 FT /evidence="ECO:0007829|PDB:1DHK" FT HELIX 36..38 FT /evidence="ECO:0007829|PDB:1DHK" FT STRAND 39..47 FT /evidence="ECO:0007829|PDB:1DHK" FT STRAND 53..58 FT /evidence="ECO:0007829|PDB:1DHK" FT STRAND 60..70 FT /evidence="ECO:0007829|PDB:1DHK" FT STRAND 72..76 FT /evidence="ECO:0007829|PDB:1DHK" FT TURN 77..80 FT /evidence="ECO:0007829|PDB:1DHK" FT STRAND 84..94 FT /evidence="ECO:0007829|PDB:1DHK" FT STRAND 103..111 FT /evidence="ECO:0007829|PDB:1DHK" FT STRAND 121..126 FT /evidence="ECO:0007829|PDB:1DHK" FT TURN 127..130 FT /evidence="ECO:0007829|PDB:1DHK" FT STRAND 131..136 FT /evidence="ECO:0007829|PDB:1DHK" FT STRAND 139..145 FT /evidence="ECO:0007829|PDB:1DHK" FT HELIX 148..150 FT /evidence="ECO:0007829|PDB:1DHK" FT TURN 151..153 FT /evidence="ECO:0007829|PDB:1DHK" FT STRAND 156..163 FT /evidence="ECO:0007829|PDB:1DHK" FT TURN 164..167 FT /evidence="ECO:0007829|PDB:1DHK" FT STRAND 168..174 FT /evidence="ECO:0007829|PDB:1DHK" FT TURN 176..178 FT /evidence="ECO:0007829|PDB:1DHK" FT STRAND 181..187 FT /evidence="ECO:0007829|PDB:1DHK" FT HELIX 193..195 FT /evidence="ECO:0007829|PDB:1DHK" FT STRAND 196..206 FT /evidence="ECO:0007829|PDB:1DHK" FT HELIX 209..211 FT /evidence="ECO:0007829|PDB:1DHK" FT STRAND 215..226 FT /evidence="ECO:0007829|PDB:1DHK" SQ SEQUENCE 246 AA; 27207 MW; EA56F15EF1F78788 CRC64; MIMASSKLLS LALFLALLSH ANSATETSFI IDAFNKTNLI LQGDATVSSN GNLQLSYNSY DSMSRAFYSA PIQIRDSTTG NVASFDTNFT MNIRTHRQAN SAVGLDFVLV PVQPESKGDT VTVEFDTFLS RISIDVNNND IKSVPWDVHD YDGQNAEVRI TYNSSTKVFS VSLSNPSTGK SNNVSTTVEL EKEVYDWVSV GFSATSGAYQ WSYETHDVLS WSFSSKFINL KDQKSERSNI VLNKIL //