ID   LEA2_PHAVU              Reviewed;         240 AA.
AC   Q41114; Q43627;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Alpha-amylase inhibitor 2;
DE            Short=Alpha-AI-2;
DE            Short=Alpha-AI2;
DE   AltName: Full=Lectin;
DE   Contains:
DE     RecName: Full=Alpha-amylase inhibitor 2 chain 1;
DE   Contains:
DE     RecName: Full=Alpha-amylase inhibitor 2 chain 2;
DE   Flags: Precursor;
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 [MRNA].
RC   STRAIN=cv. OAR4; TISSUE=Cotyledon;
RX   PubMed=8003534; DOI=10.1016/0167-4838(94)90221-6;
RA   Suzuki K., Ishimoto M., Kitamura K.;
RT   "cDNA sequence and deduced primary structure of an alpha-amylase inhibitor
RT   from a bruchid-resistant wild common bean.";
RL   Biochim. Biophys. Acta 1206:289-291(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Arcelin 4; TISSUE=Seed;
RX   PubMed=7811969; DOI=10.1007/bf00040692;
RA   Mirkov T.E., Wahlstrom J.M., Hagiwara K., Finardi-Filho F., Kjemtrup S.,
RA   Chrispeels M.J.;
RT   "Evolutionary relationships among proteins in the phytohemagglutinin-
RT   arcelin-alpha-amylase inhibitor family of the common bean and its
RT   relatives.";
RL   Plant Mol. Biol. 26:1103-1113(1994).
RN   [3]
RP   PROTEOLYTIC PROCESSING OF C-TERMINAL, AND GLYCOSYLATION AT ASN-84 AND
RP   ASN-88.
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).
CC   -!- FUNCTION: Lectin and alpha-amylase inhibitor. Acts as a defensive
CC       protein against insects.
CC   -!- SUBUNIT: Heterodimer of chain 1 and chain 2. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR   EMBL; D26109; BAA05105.1; -; mRNA.
DR   EMBL; U10348; AAA67352.1; -; Genomic_DNA.
DR   PIR; S45276; S45276.
DR   AlphaFoldDB; Q41114; -.
DR   SMR; Q41114; -.
DR   iPTMnet; Q41114; -.
DR   PRIDE; Q41114; -.
DR   GO; GO:0015066; F:alpha-amylase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0030246; F:carbohydrate binding; 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   Alpha-amylase inhibitor; Glycoprotein; Lectin; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..96
FT                   /note="Alpha-amylase inhibitor 2 chain 1"
FT                   /id="PRO_0000017630"
FT   CHAIN           97..233
FT                   /note="Alpha-amylase inhibitor 2 chain 2"
FT                   /id="PRO_0000017631"
FT   PROPEP          234..240
FT                   /id="PRO_0000017632"
FT   CARBOHYD        33
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:10100643"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305|PubMed:10100643"
FT   CONFLICT        238
FT                   /note="N -> Q (in Ref. 2; AAA67352)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   240 AA;  26597 MW;  F0A97734241EDB3A CRC64;
     MASSNLLTLA LFLVLLTHAN SASDTSFNFY SFNETNLILQ GDATVSSKGY LQLHTVDSMC
     SAFYSAPIQI RDSTTGNVAS FDTNFTMNIT TQREANSVIG LDFALVPVQP KSKGHTVTVQ
     FDTFRSRISI DVNNNDIKSV PWDEQDYDGQ NAKVRITYNS STKVLAVSLS NPSTGKSNEV
     SARMEVEKEL DDWVRVGFSA ISGVHEYSFE TRDVLSWSFS SKFSQHTTSE RSNILLNNIL