ID   CURC2_MOLLA             Reviewed;         158 AA.
AC   Q6F495; Q3MV17;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Curculin-2;
DE   AltName: Full=Neoculin acidic subunit;
DE            Short=NAS;
DE   Flags: Precursor;
OS   Molineria latifolia (Lumbah) (Curculigo latifolia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Hypoxidaceae;
OC   Molineria.
OX   NCBI_TaxID=4676;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-135, AND VARIANT ASN-80.
RX   PubMed=15215616; DOI=10.1271/bbb.68.1403;
RA   Shirasuka Y., Nakajima K., Asakura T., Yamashita H., Yamamoto A., Hata S.,
RA   Nagata S., Abo M., Sorimachi H., Abe K.;
RT   "Neoculin as a new taste-modifying protein occurring in the fruit of
RT   Curculigo latifolia.";
RL   Biosci. Biotechnol. Biochem. 68:1403-1407(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DISULFIDE BONDS.
RX   PubMed=15327988; DOI=10.1016/j.febslet.2004.07.073;
RA   Suzuki M., Kurimoto E., Nirasawa S., Masuda Y., Hori K., Kurihara Y.,
RA   Shimba N., Kawai M., Suzuki E., Kato K.;
RT   "Recombinant curculin heterodimer exhibits taste-modifying and sweet-
RT   tasting activities.";
RL   FEBS Lett. 573:135-138(2004).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.76 ANGSTROMS) OF 23-135, SUBUNIT, AND DISULFIDE
RP   BONDS.
RX   PubMed=16616933; DOI=10.1016/j.jmb.2006.03.030;
RA   Shimizu-Ibuka A., Morita Y., Terada T., Asakura T., Nakajima K., Iwata S.,
RA   Misaka T., Sorimachi H., Arai S., Abe K.;
RT   "Crystal structure of neoculin: insights into its sweetness and taste-
RT   modifying activity.";
RL   J. Mol. Biol. 359:148-158(2006).
CC   -!- FUNCTION: Taste-modifying protein; sweet-tasting. After curculin, water
CC       elicits a sweet taste, and sour substances induce a stronger sense of
CC       sweetness.
CC   -!- SUBUNIT: Heterodimer with curculin-1; Disulfide-linked.
CC       {ECO:0000269|PubMed:15327988, ECO:0000269|PubMed:16616933}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE45253.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB167079; BAD29946.1; -; mRNA.
DR   EMBL; AB167080; BAE45253.1; ALT_INIT; mRNA.
DR   EMBL; AB181490; BAD38841.1; -; mRNA.
DR   PDB; 2D04; X-ray; 2.76 A; A/C/E/G=23-135.
DR   PDBsum; 2D04; -.
DR   AlphaFoldDB; Q6F495; -.
DR   SMR; Q6F495; -.
DR   IntAct; Q6F495; 1.
DR   EvolutionaryTrace; Q6F495; -.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   CDD; cd00028; B_lectin; 1.
DR   Gene3D; 2.90.10.10; -; 1.
DR   InterPro; IPR001480; Bulb-type_lectin_dom.
DR   InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR   SMART; SM00108; B_lectin; 1.
DR   SUPFAM; SSF51110; SSF51110; 1.
DR   PROSITE; PS50927; BULB_LECTIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Lectin; Signal; Taste-modifying protein.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:15215616"
FT   CHAIN           23..135
FT                   /note="Curculin-2"
FT                   /id="PRO_0000366212"
FT   PROPEP          136..158
FT                   /id="PRO_0000366213"
FT   DOMAIN          23..131
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        51..74
FT   DISULFID        99
FT                   /note="Interchain (with C-131 in NBS)"
FT   DISULFID        131
FT                   /note="Interchain (with C-99 in NBS)"
FT   VARIANT         80
FT                   /note="S -> N"
FT                   /evidence="ECO:0000269|PubMed:15215616"
FT   STRAND          25..27
FT                   /evidence="ECO:0007829|PDB:2D04"
FT   STRAND          36..40
FT                   /evidence="ECO:0007829|PDB:2D04"
FT   STRAND          43..47
FT                   /evidence="ECO:0007829|PDB:2D04"
FT   STRAND          53..57
FT                   /evidence="ECO:0007829|PDB:2D04"
FT   STRAND          60..64
FT                   /evidence="ECO:0007829|PDB:2D04"
FT   STRAND          75..78
FT                   /evidence="ECO:0007829|PDB:2D04"
FT   STRAND          84..87
FT                   /evidence="ECO:0007829|PDB:2D04"
FT   STRAND          93..95
FT                   /evidence="ECO:0007829|PDB:2D04"
FT   STRAND          102..104
FT                   /evidence="ECO:0007829|PDB:2D04"
FT   STRAND          107..110
FT                   /evidence="ECO:0007829|PDB:2D04"
FT   STRAND          116..119
FT                   /evidence="ECO:0007829|PDB:2D04"
FT   STRAND          124..130
FT                   /evidence="ECO:0007829|PDB:2D04"
SQ   SEQUENCE   158 AA;  17174 MW;  CE597B53F069FFE1 CRC64;
     MAAKFLLTIL VTFAAVASLG MADSVLLSGQ TLYAGHSLTS GSYTLTIQNN CNLVKYQHGR
     QIWASDTDGQ GSQCRLTLRS DGNLIIYDDN NMVVWGSDCW GNNGTYALVL QQDGLFVIYG
     PVLWPLGLNG CRSLNGEITV AKDSTEPQHE DIKMVINN