DIOA3_DIOJA
ID DIOA3_DIOJA Reviewed; 271 AA.
AC A7MAQ2;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Dioscorin dioA3 {ECO:0000305};
DE EC=1.6.5.4 {ECO:0000269|PubMed:22195572};
DE EC=4.2.1.1 {ECO:0000269|PubMed:22195572, ECO:0000269|PubMed:25747844};
DE AltName: Full=Dj-dio5 {ECO:0000303|PubMed:22806688};
DE AltName: Full=Dj-dioA3 {ECO:0000303|PubMed:22796748, ECO:0000303|PubMed:22806688};
DE AltName: Full=Tuber storage protein dioA3 {ECO:0000305};
DE Flags: Precursor;
GN Name=dioA3 {ECO:0000303|PubMed:22806688};
GN Synonyms=dio5 {ECO:0000312|EMBL:CAO98738.1};
OS Dioscorea japonica (Japanese yam).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Dioscoreales; Dioscoreaceae;
OC Dioscorea.
OX NCBI_TaxID=4673 {ECO:0000312|EMBL:CAO98738.1};
RN [1] {ECO:0000312|EMBL:CAO98738.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lin K.C., Lin K.W., Chen K.S.;
RT "Isolation and characterization of a gene family encoding the major tuber
RT storage protein dioscorin of Japanese yam (Dioscorea japonica).";
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 56-65; 69-77; 119-133; 181-202; 203-222; 237-256 AND
RP 257-265, SUBUNIT, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND DISULFIDE BOND.
RC TISSUE=Tuber {ECO:0000303|PubMed:22806688};
RX PubMed=22806688; DOI=10.1002/jsfa.5789;
RA Tsai W.Y., Jheng Y.J., Chen K.H., Lin K.W., Ho Y.P., Yang C.C., Lin K.C.;
RT "Molecular cloning, structural analysis and mass spectrometric
RT identification of native dioscorins of various yam species.";
RL J. Sci. Food Agric. 93:761-770(2013).
RN [3]
RP CRYSTALLIZATION.
RX PubMed=22297997; DOI=10.1107/s1744309111053723;
RA Xue Y.L., Miyakawa T., Sawano Y., Tanokura M.;
RT "Crystallization and preliminary X-ray crystallographic analysis of
RT dioscorin from Dioscorea japonica.";
RL Acta Crystallogr. F 68:193-195(2012).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22195572; DOI=10.1016/j.plantsci.2011.10.021;
RA Xue Y.L., Miyakawa T., Sawano Y., Tanokura M.;
RT "Cloning of genes and enzymatic characterizations of novel dioscorin
RT isoforms from Dioscorea japonica.";
RL Plant Sci. 183:14-19(2012).
RN [5]
RP FUNCTION, AND DISULFIDE BOND.
RX PubMed=22796748; DOI=10.1016/j.pep.2012.07.001;
RA Jheng Y.J., Tsai W.Y., Chen K.H., Lin K.W., Chyan C.L., Yang C.C.,
RA Lin K.C.;
RT "Recombinant dioscorins of the yam storage protein expressed in Escherichia
RT coli exhibit antioxidant and immunomodulatory activities.";
RL Protein Expr. Purif. 85:77-85(2012).
RN [6] {ECO:0007744|PDB:4TWL, ECO:0007744|PDB:4TWM}
RP X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 26-271 AND IN COMPLEX WITH
RP ASCORBIC ACID, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, DISULFIDE BOND, MUTAGENESIS OF ASP-95; HIS-120; HIS-122 AND
RP GLN-139, AND REACTION MECHANISM.
RX PubMed=25747844; DOI=10.1016/j.molp.2015.02.015;
RA Xue Y.L., Miyakawa T., Nakamura A., Hatano K., Sawano Y., Tanokura M.;
RT "Yam Tuber Storage Protein Reduces Plant Oxidants Using the Coupled
RT Reactions as Carbonic Anhydrase and Dehydroascorbate Reductase.";
RL Mol. Plant 8:1115-1118(2015).
CC -!- FUNCTION: Storage protein of tuber. Involved in protection against
CC oxidative stress (Probable). Has carbonate dehydratase, trypsin
CC inhibitor, dehydroascorbate (DHA) reductase and monodehydroascorbate
CC (MDA) reductase activities (PubMed:22195572). Catalyzes the reactions
CC of carbonate dehydratase and DHA reductase independently of zinc and
CC glutathione (GSH). The coupled reaction is capable of recycling a plant
CC antioxidant ascorbate using ubiquitous compounds H(2)O and CO(2)
CC (PubMed:25747844). Exhibits antioxidant activity. Able to scavenge 1,1-
CC diphenyl-2-picrylhydrazyl (DPPH) radical. Exhibits immunomodulatory
CC activity. Activates Toll-like receptor 4 signaling pathways by up-
CC regulating the gene expression of pro-inflammatory cytokines, such as
CC tumor necrosis factor alpha, interleukin-1 beta and interleukin-6, and
CC chemokines RANTES and MCP-1, in mouse RAW 264.7 macrophages. Stimulates
CC the phagocytosis of E.coli by the LPS-treated mouse macrophages
CC (PubMed:22796748). {ECO:0000269|PubMed:22195572,
CC ECO:0000269|PubMed:22796748, ECO:0000269|PubMed:25747844, 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; Evidence={ECO:0000269|PubMed:22195572,
CC ECO:0000269|PubMed:25747844};
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;
CC Evidence={ECO:0000269|PubMed:22195572};
CC -!- ACTIVITY REGULATION: The carbonate dehydratase activity is not
CC substantially changed by the addition of Zn(2+).
CC {ECO:0000269|PubMed:25747844}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.49 mM for dehydroascorbate (DHA) (at ph 7.0 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:25747844};
CC KM=10.2 mM for sodium bicarbonate (at ph 7.1 and 4 degrees Celsius)
CC {ECO:0000269|PubMed:25747844};
CC Note=kcat is 0.0152 min(-1) for DHA. kcat is 30500 min(-1) for sodium
CC bicarbonate. {ECO:0000269|PubMed:25747844};
CC -!- SUBUNIT: Monomer (PubMed:22806688). Homodimer (By similarity).
CC {ECO:0000250|UniProtKB:Q75N34, ECO:0000269|PubMed:22806688}.
CC -!- TISSUE SPECIFICITY: Expressed in tuber (at protein level).
CC {ECO:0000269|PubMed:22806688}.
CC -!- PTM: Not glycosylated. {ECO:0000250|UniProtKB:Q75N34}.
CC -!- ALLERGEN: Causes an allergic reaction in human (Probable).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the alpha-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:0000305|PubMed:25747844}.
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DR EMBL; AM849820; CAO98738.1; -; mRNA.
DR PDB; 4TWL; X-ray; 2.11 A; A/B=26-271.
DR PDB; 4TWM; X-ray; 2.11 A; A/B=26-271.
DR PDBsum; 4TWL; -.
DR PDBsum; 4TWM; -.
DR AlphaFoldDB; A7MAQ2; -.
DR SMR; A7MAQ2; -.
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; IDA: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; ISS: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; IC: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; IEP:UniProtKB.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IDA: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 3D-structure; Allergen; Antioxidant; Direct protein sequencing;
KW Disulfide bond; Lyase; Oxidoreductase; Signal; Storage protein.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..271
FT /note="Dioscorin dioA3"
FT /evidence="ECO:0000255"
FT /id="PRO_5002712224"
FT DOMAIN 28..262
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT ACT_SITE 94
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 95
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000269|PubMed:25747844,
FT ECO:0007744|PDB:4TWL"
FT BINDING 120..122
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000269|PubMed:25747844,
FT ECO:0007744|PDB:4TWL"
FT BINDING 139
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000269|PubMed:25747844,
FT ECO:0007744|PDB:4TWL"
FT BINDING 208..209
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000269|PubMed:25747844,
FT ECO:0007744|PDB:4TWL"
FT DISULFID 53..212
FT /evidence="ECO:0000269|PubMed:25747844,
FT ECO:0007744|PDB:4TWL, ECO:0007744|PDB:4TWM"
FT MUTAGEN 95
FT /note="D->A: Loss of dehydroascorbate (DHA) reductase and
FT carbonate dehydratase activity."
FT /evidence="ECO:0000269|PubMed:25747844"
FT MUTAGEN 120
FT /note="H->A: Loss of dehydroascorbate (DHA) reductase
FT activity and carbonate dehydratase activity."
FT /evidence="ECO:0000269|PubMed:25747844"
FT MUTAGEN 122
FT /note="H->A: No change in dehydroascorbate (DHA) reductase
FT or carbonate dehydratase activity."
FT /evidence="ECO:0000269|PubMed:25747844"
FT MUTAGEN 139
FT /note="Q->A: Slight decrease of dehydroascorbate (DHA)
FT reductase activity."
FT /evidence="ECO:0000269|PubMed:25747844"
FT MUTAGEN 139
FT /note="Q->H: Slight decrease of dehydroascorbate (DHA)
FT reductase activity. Significant decrease of
FT dehydroascorbate (DHA) reductase activity by the addition
FT of Zn(2+). Increase of carbonate dehydratase activity by
FT the addition of Zn(2+)."
FT /evidence="ECO:0000269|PubMed:25747844"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:4TWL"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:4TWL"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:4TWL"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:4TWL"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:4TWL"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:4TWL"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:4TWL"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:4TWL"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:4TWL"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:4TWL"
FT STRAND 112..124
FT /evidence="ECO:0007829|PDB:4TWL"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:4TWL"
FT STRAND 135..143
FT /evidence="ECO:0007829|PDB:4TWL"
FT STRAND 149..160
FT /evidence="ECO:0007829|PDB:4TWL"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:4TWL"
FT HELIX 169..173
FT /evidence="ECO:0007829|PDB:4TWL"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:4TWL"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:4TWL"
FT STRAND 181..188
FT /evidence="ECO:0007829|PDB:4TWL"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:4TWL"
FT STRAND 199..206
FT /evidence="ECO:0007829|PDB:4TWL"
FT STRAND 214..223
FT /evidence="ECO:0007829|PDB:4TWL"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:4TWL"
FT HELIX 229..237
FT /evidence="ECO:0007829|PDB:4TWL"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:4TWL"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:4TWL"
SQ SEQUENCE 271 AA; 30876 MW; 50A6CD33515CB95B CRC64;
MSSSTLLHLL LLSSLLFSCL SCLTNVEDEF SYIEGNPNGP ENWGNLKPEW ETCGKGMEQS
PIQLRDNRVI FDQTLGKLRR NYRAVDARLR NSGHDVLVDF KGNAGSLSIN RVEYQLKRIH
FHSPSEHEMN GERFDLEAQL VHESQDQKRA VVSILFRFGR ADPFLSDLED FIKQFSNSQK
NEINAGVVDP NQLQIDDSAY YRYMGSFTAP PCTEGISWTV MRKVATVSPR QVLLLKQAVN
ENAINNARPL QPTNFRSVFY FEQLKSKLGV I
