MIRA_SYNDU
ID MIRA_SYNDU Reviewed; 220 AA.
AC P13087; Q41153;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 3.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Miraculin;
DE Short=MIR;
DE Flags: Precursor;
OS Synsepalum dulcificum (Miracle fruit) (Richadella dulcifica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Ericales; Sapotaceae; Chrysophylloideae; Synsepalum.
OX NCBI_TaxID=3743;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Fruit;
RX PubMed=7665074; DOI=10.1016/0378-1119(95)00198-f;
RA Masuda Y., Nirasawa S., Nakaya K., Kurihara Y.;
RT "Cloning and sequencing of a cDNA encoding a taste-modifying protein,
RT miraculin.";
RL Gene 161:175-177(1995).
RN [2]
RP PROTEIN SEQUENCE OF 30-220.
RX PubMed=2708331; DOI=10.1016/s0021-9258(18)83477-9;
RA Theerasilp S., Hitotsuya H., Nakajo S., Nakaja K., Nakamura Y.,
RA Kurihara Y.;
RT "Complete amino acid sequence and structure characterization of the taste-
RT modifying protein, miraculin.";
RL J. Biol. Chem. 264:6655-6659(1989).
RN [3]
RP PROTEIN SEQUENCE OF 30-50.
RX PubMed=3403544; DOI=10.1016/s0021-9258(18)37991-2;
RA Theerasilp S., Kurihara Y.;
RT "Complete purification and characterization of the taste-modifying protein,
RT miraculin, from miracle fruit.";
RL J. Biol. Chem. 263:11536-11539(1988).
RN [4]
RP DISULFIDE BONDS.
RX PubMed=1911854; DOI=10.1016/0167-4838(91)90073-9;
RA Igeta H., Tamura Y., Nakaya K., Nakmura Y., Kurihara Y.;
RT "Determination of disulfide array and subunit structure of taste-modifying
RT protein, miraculin.";
RL Biochim. Biophys. Acta 1079:303-307(1991).
RN [5]
RP GLYCOSYLATION AT ASN-71 AND ASN-215.
RX PubMed=2335505; DOI=10.1016/s0021-9258(19)38998-7;
RA Takahashi N., Hitotsuya H., Hanzawa H., Arata Y., Kurihara Y.;
RT "Structural study of asparagine-linked oligosaccharide moiety of taste-
RT modifying protein, miraculin.";
RL J. Biol. Chem. 265:7793-7798(1990).
CC -!- FUNCTION: Miraculin has the property of modifying a sour taste into a
CC sweet taste. This alteration of taste perception persists for many
CC minutes.
CC -!- SUBUNIT: Homotetramer; dimer of homodimer.
CC -!- TISSUE SPECIFICITY: Expressed in fruit pulp after pollination. Not
CC expressed in seeds, stems or leaves. {ECO:0000269|PubMed:7665074}.
CC -!- PTM: Glycosylated; contains as much as 13,9% of sugars (glucosamine,
CC mannose, galactose, xylose, and fucose). {ECO:0000269|PubMed:2335505}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC type inhibitor) family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The sweet side of life
CC - Issue 17 of December 2001;
CC URL="https://web.expasy.org/spotlight/back_issues/017";
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DR EMBL; D38598; BAA07603.1; -; mRNA.
DR PIR; JC4232; A33872.
DR AlphaFoldDB; P13087; -.
DR SMR; P13087; -.
DR MEROPS; I03.030; -.
DR GlyConnect; 369; 5 N-Linked glycans (2 sites).
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR CDD; cd00178; STI; 1.
DR InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
DR InterPro; IPR002160; Prot_inh_Kunz-lg.
DR PANTHER; PTHR33107; PTHR33107; 1.
DR Pfam; PF00197; Kunitz_legume; 1.
DR PRINTS; PR00291; KUNITZINHBTR.
DR SMART; SM00452; STI; 1.
DR SUPFAM; SSF50386; SSF50386; 1.
DR PROSITE; PS00283; SOYBEAN_KUNITZ; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Signal;
KW Taste-modifying protein.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:2708331,
FT ECO:0000269|PubMed:3403544"
FT CHAIN 30..220
FT /note="Miraculin"
FT /id="PRO_0000016935"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:2335505"
FT /id="CAR_000132"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:2335505"
FT /id="CAR_000133"
FT DISULFID 76..121
FT /evidence="ECO:0000269|PubMed:1911854"
FT DISULFID 167
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:1911854"
FT DISULFID 177..188
FT /evidence="ECO:0000269|PubMed:1911854"
FT DISULFID 181..184
FT /evidence="ECO:0000269|PubMed:1911854"
FT CONFLICT 129
FT /note="W -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 220 AA; 24367 MW; BD7E70CE1AAEE520 CRC64;
MKELTMLSLS FFFVSALLAA AANPLLSAAD SAPNPVLDID GEKLRTGTNY YIVPVLRDHG
GGLTVSATTP NGTFVCPPRV VQTRKEVDHD RPLAFFPENP KEDVVRVSTD LNINFSAFMP
CRWTSSTVWR LDKYDESTGQ YFVTIGGVKG NPGPETISSW FKIEEFCGSG FYKLVFCPTV
CGSCKVKCGD VGIYIDQKGR RRLALSDKPF AFEFNKTVYF
