DB3S_DIOPO
ID DB3S_DIOPO Reviewed; 268 AA.
AC Q75N34;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Dioscorin DB3S {ECO:0000303|PubMed:15047697, ECO:0000303|PubMed:18303202, ECO:0000303|PubMed:29423371};
DE EC=1.6.5.4 {ECO:0000269|Ref.5};
DE EC=4.2.1.1 {ECO:0000269|PubMed:10552514};
DE AltName: Full=Tuber storage protein DB3S {ECO:0000303|PubMed:18303202};
DE AltName: Allergen=Dio p TSP {ECO:0000305};
DE Flags: Precursor;
GN Name=DB3S {ECO:0000312|EMBL:BAD18021.1};
OS Dioscorea polystachya (Chinese yam).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Dioscoreales; Dioscoreaceae;
OC Dioscorea.
OX NCBI_TaxID=55575;
RN [1] {ECO:0000312|EMBL:BAD18021.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-263, FUNCTION, SUBUNIT,
RP TISSUE SPECIFICITY, PTM, IDENTIFICATION BY MASS SPECTROMETRY, AND DISULFIDE
RP BOND.
RC TISSUE=Tuber {ECO:0000303|PubMed:15047697, ECO:0000312|EMBL:BAD18021.1};
RX PubMed=15047697; DOI=10.1074/jbc.m402139200;
RA Gaidamashvili M., Ohizum Y., Iijima S., Takayama T., Ogawa T., Muramoto K.;
RT "Characterization of the yam tuber storage proteins from Dioscorea batatas
RT exhibiting unique lectin activities.";
RL J. Biol. Chem. 279:26028-26035(2004).
RN [2]
RP PROTEIN SEQUENCE OF 22-41, TISSUE SPECIFICITY, AND ALLERGEN.
RC TISSUE=Tuber {ECO:0000303|PubMed:18303202};
RX PubMed=18303202; DOI=10.3346/jkms.2008.23.1.72;
RA Hur G.Y., Park H.J., Kim H.A., Ye Y.M., Park H.S.;
RT "Identification of Dioscorea batatas (sanyak) allergen as an inhalant and
RT oral allergen.";
RL J. Korean Med. Sci. 23:72-76(2008).
RN [3]
RP PROTEIN SEQUENCE OF 23-43, FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=10552514; DOI=10.1021/jf980738o;
RA Hou W.C., Liu J.S., Chen H.J., Chen T.E., Chang C.F., Lin Y.H.;
RT "Dioscorin, the major tuber storage protein of yam (Dioscorea batatas
RT decne) with carbonic anhydrase and trypsin inhibitor activities.";
RL J. Agric. Food Chem. 47:2168-2172(1999).
RN [4]
RP PROTEIN SEQUENCE OF 23-35, AND ALLERGEN.
RX PubMed=29423371; DOI=10.5415/apallergy.2018.8.e4;
RA Xu Y.Y., Yin J.;
RT "Identification of a thermal stable allergen in yam (Dioscorea opposita) to
RT cause anaphylaxis.";
RL Asia Pac. Allergy 8:e4-e4(2018).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX DOI=10.1016/S0168-9452(99)00152-1;
RA Hou W.C., Chen H.J., Lin Y.H.;
RT "Dioscorins, the major tuber storage proteins of yam (Dioscorea batatas
RT Decne), with dehydroascorbate reductase and monodehydroascorbate reductase
RT activities.";
RL Plant Sci. 149:151-156(1999).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11600050; DOI=10.1021/jf010606m;
RA Hou W.C., Lee M.H., Chen H.J., Liang W.L., Han C.H., Liu Y.W., Lin Y.H.;
RT "Antioxidant activities of dioscorin, the storage protein of yam (Dioscorea
RT batatas Decne) tuber.";
RL J. Agric. Food Chem. 49:4956-4960(2001).
CC -!- FUNCTION: Storage protein of tuber. Involved in protection against
CC oxidative stress (Probable). Has carbonate dehydratase and weak trypsin
CC inhibitor activity detected by measuring the dehydration of sodium
CC bicarbonate and the inhibition of trypsin-catalyzed hydrolysis of N-
CC benzoyl-L-arginine-4-nitro anilide, respectively (PubMed:10552514).
CC Contrarily, no carbonate dehydratase or trypsin inhibitor activity
CC detected by measuring the hydrolysis of 4-nitrophenyl acetate or the
CC inhibition of bovine trypsin-catalyzed hydrolysis of N-benzoyl-L-
CC arginine ethyl ester, respectively (PubMed:15047697). Has
CC dehydroascorbate (DHA) reductase and monodehydroascorbate (MDA)
CC reductase activities (Ref.5). Catalyzes the reactions of carbonate
CC dehydratase and DHA reductase independently of zinc and glutathione
CC (GSH). The coupled reaction is capable of recycling a plant antioxidant
CC ascorbate using ubiquitous compounds H(2)O and CO(2) (By similarity).
CC Exhibits antioxidant activity. Able to scavenge 1,1-diphenyl-2-
CC picrylhydrazyl (DPPH) radical and hydroxyl radicals (PubMed:11600050).
CC Exhibits immunomodulatory activity. Activates Toll-like receptor 4
CC signaling pathways by up-regulating the gene expression of pro-
CC inflammatory cytokines, such as tumor necrosis factor alpha,
CC interleukin-1 beta and interleukin-6, and chemokines RANTES and MCP-1,
CC in mouse RAW 264.7 macrophages. Stimulates the phagocytosis of E.coli
CC by the LPS-treated mouse macrophages (By similarity).
CC {ECO:0000250|UniProtKB:A7MAQ2, ECO:0000269|PubMed:10552514,
CC ECO:0000269|PubMed:11600050, ECO:0000269|PubMed:15047697,
CC ECO:0000269|Ref.5, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17544; EC=4.2.1.1;
CC Evidence={ECO:0000269|PubMed:10552514};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + 2 monodehydro-L-ascorbate radical + NADH = 2 L-
CC ascorbate + NAD(+); Xref=Rhea:RHEA:14581, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:59513; EC=1.6.5.4; Evidence={ECO:0000269|Ref.5};
CC -!- SUBUNIT: Monomer (By similarity). Homodimer (PubMed:15047697).
CC {ECO:0000250|UniProtKB:A7MAQ2, ECO:0000269|PubMed:15047697}.
CC -!- TISSUE SPECIFICITY: Expressed in tuber (at protein level).
CC {ECO:0000269|PubMed:10552514, ECO:0000269|PubMed:11600050,
CC ECO:0000269|PubMed:15047697, ECO:0000269|PubMed:18303202,
CC ECO:0000269|Ref.5}.
CC -!- PTM: Not glycosylated. {ECO:0000269|PubMed:15047697}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE of
CC patients allergic to Chinese yam (PubMed:18303202, PubMed:29423371).
CC Patients can be sensitized to this protein via an oral or inhalant
CC route (PubMed:18303202). Thermal stable oral allergen, which can to
CC trigger anaphylactic reaction and oral allergy syndrome even when
CC consumed as cooked. Activates human basophils (PubMed:29423371).
CC {ECO:0000269|PubMed:18303202, ECO:0000269|PubMed:29423371}.
CC -!- SIMILARITY: Belongs to the alpha-class carbonic anhydrase family.
CC {ECO:0000305}.
CC -!- CAUTION: Despite overall sequence similarity to the typical alpha class
CC carbonic anhydrases, lacks one of the three conserved catalytic zinc-
CC ligand histidines. The carbonate dehydratase activity of this protein
CC is zinc-independent. {ECO:0000250|UniProtKB:A7MAQ2}.
CC -!- CAUTION: It is uncertain whether the mature protein starts at position
CC 22 or 23. The first residue of the N-terminus obtained by direct
CC protein sequencing is 'Asn-22' according to PubMed:18303202, but it is
CC 'Val-23' according to PubMed:15047697, PubMed:10552514 and
CC PubMed:29423371. {ECO:0000305}.
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DR EMBL; AB178473; BAD18021.1; -; mRNA.
DR AlphaFoldDB; Q75N34; -.
DR SMR; Q75N34; -.
DR Allergome; 4051; Dio p TSP.
DR GO; GO:0016209; F:antioxidant activity; IDA:UniProtKB.
DR GO; GO:0004089; F:carbonate dehydratase activity; IDA:UniProtKB.
DR GO; GO:0031418; F:L-ascorbic acid binding; ISS:UniProtKB.
DR GO; GO:0016656; F:monodehydroascorbate reductase (NADH) activity; IDA:UniProtKB.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015976; P:carbon utilization; IC:UniProtKB.
DR GO; GO:0098869; P:cellular oxidant detoxification; IDA:UniProtKB.
DR GO; GO:0071244; P:cellular response to carbon dioxide; IC:UniProtKB.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:0000305; P:response to oxygen radical; IC:UniProtKB.
DR CDD; cd03124; alpha_CA_prokaryotic_like; 1.
DR Gene3D; 3.10.200.10; -; 1.
DR InterPro; IPR041891; Alpha_CA_prokaryot-like.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
DR InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR PANTHER; PTHR18952; PTHR18952; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; SSF51069; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
PE 1: Evidence at protein level;
KW Allergen; Antioxidant; Direct protein sequencing; Disulfide bond; Lyase;
KW Oxidoreductase; Signal; Storage protein.
FT SIGNAL 1..?
FT /evidence="ECO:0000305"
FT CHAIN ?..268
FT /note="Dioscorin DB3S"
FT /evidence="ECO:0000305"
FT /id="PRO_5004286658"
FT DOMAIN 25..259
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT ACT_SITE 91
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 92
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:A7MAQ2"
FT BINDING 117..119
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:A7MAQ2"
FT BINDING 136
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:A7MAQ2"
FT BINDING 205..206
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:A7MAQ2"
FT DISULFID 50..209
FT /evidence="ECO:0000305|PubMed:15047697"
FT CONFLICT 35
FT /note="N -> H (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 268 AA; 30460 MW; 30F2BC9D273FCB30 CRC64;
MSSSTLLHLL LLSSLLFSCL ANVEDEFSYI EGNPNGPENW GNLKPEWETC GKGMEQSPIQ
LRDNRVIFDQ TLGRLRRNYR AVDARLRNSG HDVLVEFKGN AGSLSINRVA YQLKRIHFHS
PSEHEMNGER FDLEAQLVHE SQDQKRAVVS ILFIFGRADP FLSDLEDFIK QFSSSQKNEI
NAGVVDPNQL QIDDSAYYRY MGSFTAPPCT EGISWTVMRK VATVSPRQVL LLKQAVNENA
INNARPLQPT NFRSVFYFEQ LKSKVCAI
