CURC1_MOLLA
ID CURC1_MOLLA Reviewed; 158 AA.
AC P19667; Q39530; Q39531;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Curculin-1;
DE AltName: Full=Neoculin basic subunit;
DE Short=NBS;
DE Flags: Precursor;
GN Name=CUR09; Synonyms=CUR37;
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].
RX PubMed=1562601; DOI=10.1016/0167-4781(92)90537-a;
RA Abe K., Yamashita H., Arai S., Kurihara Y.;
RT "Molecular cloning of curculin, a novel taste-modifying protein with a
RT sweet taste.";
RL Biochim. Biophys. Acta 1130:232-234(1992).
RN [2]
RP PROTEIN SEQUENCE OF 23-136.
RC TISSUE=Fruit;
RX PubMed=2394746; DOI=10.1016/s0021-9258(18)55464-8;
RA Yamashita H., Theerasilp S., Aiuchi T., Nakaya K., Nakamura Y.,
RA Kurihara Y.;
RT "Purification and complete amino acid sequence of a new type of sweet
RT protein taste-modifying activity, curculin.";
RL J. Biol. Chem. 265:15770-15775(1990).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.76 ANGSTROMS) OF 23-136 IN COMPLEX WITH NAS,
RP SUBUNIT, AND DISULFIDE 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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 23-136, AND DISULFIDE BONDS.
RX PubMed=17895249; DOI=10.1074/jbc.c700174200;
RA Kurimoto E., Suzuki M., Amemiya E., Yamaguchi Y., Nirasawa S., Shimba N.,
RA Xu N., Kashiwagi T., Kawai M., Suzuki E., Kato K.;
RT "Curculin exhibits sweet-tasting and taste-modifying activities through its
RT distinct molecular surfaces.";
RL J. Biol. Chem. 282:33252-33256(2007).
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: Homodimer and heterodimer with curculin-2; Disulfide-linked.
CC {ECO:0000269|PubMed:16616933, ECO:0000269|PubMed:17895249}.
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DR EMBL; X64110; CAA45476.1; -; mRNA.
DR EMBL; X64111; CAA45477.1; -; mRNA.
DR PIR; S22365; S22365.
DR PDB; 2D04; X-ray; 2.76 A; B/D/F/H=23-136.
DR PDB; 2DPF; X-ray; 1.50 A; A/B/C/D=23-136.
DR PDBsum; 2D04; -.
DR PDBsum; 2DPF; -.
DR AlphaFoldDB; P19667; -.
DR SMR; P19667; -.
DR IntAct; P19667; 1.
DR EvolutionaryTrace; P19667; -.
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; Lectin; Signal;
KW Taste-modifying protein.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:2394746"
FT CHAIN 23..136
FT /note="Curculin-1"
FT /id="PRO_0000021042"
FT PROPEP 137..158
FT /id="PRO_0000021043"
FT DOMAIN 23..131
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DISULFID 51..74
FT DISULFID 99
FT /note="Interchain (with C-131)"
FT DISULFID 131
FT /note="Interchain (with C-99)"
FT CONFLICT 50
FT /note="K -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="W -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="W -> C (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="N -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:2DPF"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:2DPF"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:2DPF"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:2DPF"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:2DPF"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:2DPF"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:2DPF"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:2DPF"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:2DPF"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:2DPF"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:2DPF"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:2DPF"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:2DPF"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:2D04"
SQ SEQUENCE 158 AA; 17223 MW; 65B51E742D34706E CRC64;
MAAKFLLTIL VTFAAVASLG MADNVLLSGQ TLHADHSLQA GAYTLTIQNK CNLVKYQNGR
QIWASNTDRR GSGCRLTLLS DGNLVIYDHN NNDVWGSACW GDNGKYALVL QKDGRFVIYG
PVLWSLGPNG CRRVNGGITV AKDSTEPQHE DIKMVINN
