ID   LEG_CICAR               Reviewed;         496 AA.
AC   Q9SMJ4;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Legumin {ECO:0000312|EMBL:CAB60140.1};
DE   AltName: Full=Alpha-amylase inhibitor {ECO:0000303|PubMed:19420683};
DE            Short=CLAI {ECO:0000303|PubMed:19420683};
DE   Contains:
DE     RecName: Full=Legumin alpha chain {ECO:0000250|UniProtKB:P04776};
DE   Contains:
DE     RecName: Full=Legumin beta chain {ECO:0000250|UniProtKB:P04776};
DE   Flags: Precursor;
GN   Name=leg3 {ECO:0000312|EMBL:CAB60140.1};
OS   Cicer arietinum (Chickpea) (Garbanzo).
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; Hologalegina; IRL clade; Cicereae; Cicer.
OX   NCBI_TaxID=3827;
RN   [1] {ECO:0000312|EMBL:CAB60140.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Seedling {ECO:0000312|EMBL:CAB60140.1};
RA   Mandaokar A.D., Koundal K.R.;
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 322-341, AND FUNCTION.
RC   TISSUE=Seed {ECO:0000269|PubMed:19420683};
RX   PubMed=19420683; DOI=10.1271/bbb.80776;
RA   Hao X., Li J., Shi Q., Zhang J., He X., Ma H.;
RT   "Characterization of a novel legumin alpha-amylase inhibitor from chickpea
RT   (Cicer arietinum L.) seeds.";
RL   Biosci. Biotechnol. Biochem. 73:1200-1202(2009).
CC   -!- FUNCTION: Seed storage protein (By similarity). Alpha-amylase
CC       inhibitor. {ECO:0000250|UniProtKB:P04776, ECO:0000269|PubMed:19420683}.
CC   -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a basic
CC       chain derived from a single precursor and linked by a disulfide bond.
CC       {ECO:0000250|UniProtKB:P04776}.
CC   -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) family.
CC       {ECO:0000255}.
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DR   EMBL; Y15527; CAB60140.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9SMJ4; -.
DR   SMR; Q9SMJ4; -.
DR   STRING; 3827.XP_004493779.1; -.
DR   Allergome; 10703; Cic a 6.
DR   PRIDE; Q9SMJ4; -.
DR   eggNOG; ENOG502QU1J; Eukaryota.
DR   Proteomes; UP000087171; Genome assembly.
DR   GO; GO:0015066; F:alpha-amylase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.10; -; 3.
DR   InterPro; IPR022379; 11S_seedstore_CS.
DR   InterPro; IPR006044; 11S_seedstore_pln.
DR   InterPro; IPR006045; Cupin_1.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   Pfam; PF00190; Cupin_1; 2.
DR   PRINTS; PR00439; 11SGLOBULIN.
DR   SMART; SM00835; Cupin_1; 2.
DR   SUPFAM; SSF51182; SSF51182; 2.
DR   PROSITE; PS00305; 11S_SEED_STORAGE; 1.
PE   1: Evidence at protein level;
KW   Alpha-amylase inhibitor; Direct protein sequencing; Disulfide bond;
KW   Reference proteome; Seed storage protein; Signal; Storage protein.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..311
FT                   /note="Legumin alpha chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000382239"
FT   CHAIN           312..496
FT                   /note="Legumin beta chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000382240"
FT   DOMAIN          36..230
FT                   /note="Cupin type-1 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          324..453
FT                   /note="Cupin type-1 2"
FT                   /evidence="ECO:0000255"
FT   REGION          240..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..309
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        31..64
FT                   /evidence="ECO:0000250|UniProtKB:P04776"
FT   DISULFID        107..318
FT                   /note="Interchain (between alpha and beta chains)"
FT                   /evidence="ECO:0000250|UniProtKB:P04776"
SQ   SEQUENCE   496 AA;  56251 MW;  2971F67FD1308132 CRC64;
     MAKLLALSLS FCFLLFGTCF ALRDQPQQNE CQLEHLNALK PDNRIKSEGG LIETWNPSNK
     QFACAGVALS RATLQPNSLL QTFLHQRSPE IFIQQGNGYF GMVFPGCVET FEEPRESEQG
     EGSKFSDSHQ KVNRFREGDI IAVPTGVVFW MFNDQDTPVI AVSLIDTSSF QNQLDQMPRR
     FYLAGNHEQE FLRYQQEGSE EEENEGGNIF SGFKRDFLED ALNVNRRIVN KLQGRNEDEE
     KGAIVKVKGG LSITTPPEKE PRQKRGSRQE EDEDEDEKRQ PHRHSRQDED EDEKRQPHHH
     SRGGSKSQRD NGFEETICTA RLHQNIGSSS SPDIYNPQAG RIKTVTSFDL QALRFLKLSA
     EFGSLHKNAM FVPHYNLNAN SILYALKGRA RLLYALNCKG NSVFDGELEA GRALIVPQNF
     AIAAKSLSDR FSYVAFKTND RALINVCQKK LLQLLSIWKE MRPGSSSSTA PFHFLFHPAV
     TQTTKQQLDL VPNQYE