ID   2SS2_CAPMA              Reviewed;         155 AA.
AC   P30233; O04774;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2001, sequence version 3.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Sweet protein mabinlin-2;
DE   AltName: Full=Mabinlin II;
DE            Short=MAB II;
DE   Contains:
DE     RecName: Full=Sweet protein mabinlin-2 chain A;
DE   Contains:
DE     RecName: Full=Sweet protein mabinlin-2 chain B;
DE   Flags: Precursor;
OS   Capparis masaikai (Mabinlang).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Capparaceae; Capparis.
OX   NCBI_TaxID=13395;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Seed;
RX   PubMed=8973336; DOI=10.1016/s0378-1119(96)00465-9;
RA   Nirasawa S., Masuda Y., Nakaya K., Kurihara Y.;
RT   "Cloning and sequencing of a cDNA encoding a heat-stable sweet protein,
RT   mabinlin II.";
RL   Gene 181:225-227(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 36-68 AND 83-154, AND PYROGLUTAMATE FORMATION AT GLN-36
RP   AND GLN-83.
RC   TISSUE=Seed;
RX   PubMed=8425538; DOI=10.1111/j.1432-1033.1993.tb19896.x;
RA   Liu X., Maeda S., Hu Z., Aiuchi T., Nakaya K., Kurihara Y.;
RT   "Purification, complete amino acid sequence and structural characterization
RT   of the heat-stable sweet protein, mabinlin II.";
RL   Eur. J. Biochem. 211:281-287(1993).
RN   [3]
RP   PARTIAL PROTEIN SEQUENCE, AND DISULFIDE BONDS.
RX   PubMed=8399391; DOI=10.1016/0167-4838(93)90016-k;
RA   Nirasawa S., Liu X., Nishino T., Kurihara Y.;
RT   "Disulfide bridge structure of the heat-stable sweet protein mabinlin II.";
RL   Biochim. Biophys. Acta 1202:277-280(1993).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 36-68 AND 83-154, AND DISULFIDE
RP   BONDS.
RX   PubMed=18308584; DOI=10.1016/j.jsb.2007.12.007;
RA   Li D.F., Jiang P., Zhu D.Y., Hu Y., Max M., Wang D.C.;
RT   "Crystal structure of Mabinlin II: a novel structural type of sweet
RT   proteins and the main structural basis for its sweetness.";
RL   J. Struct. Biol. 162:50-62(2008).
CC   -!- FUNCTION: Heat stable 2S seed storage protein having sweetness-inducing
CC       activity.
CC   -!- SUBUNIT: Heterodimer of a small A and a large B chain linked by
CC       disulfide bonds.
CC   -!- SIMILARITY: Belongs to the 2S seed storage albumins family.
CC       {ECO:0000305}.
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DR   EMBL; D83997; BAA12204.1; -; mRNA.
DR   PIR; JC5379; JC5379.
DR   PIR; S28842; S28842.
DR   PIR; S28843; S28843.
DR   PDB; 2DS2; X-ray; 1.70 A; A/C=36-68, B/D=83-154.
DR   PDBsum; 2DS2; -.
DR   AlphaFoldDB; P30233; -.
DR   SMR; P30233; -.
DR   EvolutionaryTrace; P30233; -.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR   CDD; cd00261; AAI_SS; 1.
DR   Gene3D; 1.10.110.10; -; 1.
DR   InterPro; IPR044723; AAI_SS_dom.
DR   InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR   InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR   InterPro; IPR000617; Napin/2SS/CON.
DR   PANTHER; PTHR35496; PTHR35496; 1.
DR   Pfam; PF00234; Tryp_alpha_amyl; 1.
DR   PRINTS; PR00496; NAPIN.
DR   SMART; SM00499; AAI; 1.
DR   SUPFAM; SSF47699; SSF47699; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Pyrrolidone carboxylic acid; Seed storage protein; Signal; Storage protein;
KW   Taste-modifying protein.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..35
FT                   /evidence="ECO:0000269|PubMed:8425538"
FT                   /id="PRO_0000032137"
FT   CHAIN           36..68
FT                   /note="Sweet protein mabinlin-2 chain A"
FT                   /id="PRO_0000032138"
FT   PROPEP          69..82
FT                   /evidence="ECO:0000269|PubMed:8425538"
FT                   /id="PRO_0000032139"
FT   CHAIN           83..154
FT                   /note="Sweet protein mabinlin-2 chain B"
FT                   /id="PRO_0000032140"
FT   PROPEP          155
FT                   /id="PRO_0000032141"
FT   REGION          64..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         36
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:8425538"
FT   MOD_RES         83
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:8425538"
FT   DISULFID        40..103
FT                   /note="Interchain (between A and B chains)"
FT   DISULFID        53..92
FT                   /note="Interchain (between A and B chains)"
FT   DISULFID        93..141
FT   DISULFID        105..149
FT   CONFLICT        148
FT                   /note="A -> T (in Ref. 1; BAA12204)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        153
FT                   /note="A -> T (in Ref. 1; BAA12204)"
FT                   /evidence="ECO:0000305"
FT   HELIX           40..46
FT                   /evidence="ECO:0007829|PDB:2DS2"
FT   HELIX           47..50
FT                   /evidence="ECO:0007829|PDB:2DS2"
FT   HELIX           51..62
FT                   /evidence="ECO:0007829|PDB:2DS2"
FT   HELIX           88..96
FT                   /evidence="ECO:0007829|PDB:2DS2"
FT   HELIX           101..103
FT                   /evidence="ECO:0007829|PDB:2DS2"
FT   HELIX           104..118
FT                   /evidence="ECO:0007829|PDB:2DS2"
FT   HELIX           124..140
FT                   /evidence="ECO:0007829|PDB:2DS2"
SQ   SEQUENCE   155 AA;  18089 MW;  72E885DEDCC2D46A CRC64;
     MAKLIFLFAT LALFVLLANA SIQTTVIEVD EEEDNQLWRC QRQFLQHQRL RACQRFIHRR
     AQFGGQPDEL EDEVEDDNDD ENQPRRPALR QCCNQLRQVD RPCVCPVLRQ AAQQVLQRQI
     IQGPQQLRRL FDAARNLPNI CNIPNIGACP FRAWP