TRXH1_ORYSJ
ID TRXH1_ORYSJ Reviewed; 122 AA.
AC Q0D840; A0A0P0X3K2; B7E3H0; O04743; Q42443; Q7EZX7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Thioredoxin H1;
DE Short=OsTrxh1;
DE AltName: Full=Phloem sap 13 kDa protein 1;
GN Name=TRXH; Synonyms=RPP13-1;
GN OrderedLocusNames=Os07g0186000, LOC_Os07g08840;
GN ORFNames=OJ1339_B08.1, OsJ_022432, P0506C07.2;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Nipponbare;
RX PubMed=7766047; DOI=10.1007/bf00202605;
RA Ishiwatari Y., Honda C., Kawashima I., Nakamura S., Hirano H., Mori S.,
RA Fujiwara T., Hayashi H., Chino M.;
RT "Thioredoxin h is one of the major proteins in rice phloem sap.";
RL Planta 195:456-463(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF 1-MET--GLU-5; 4-GLU-GLU-5;
RP 14-LYS--GLU-16; 25-LYS-GLU-26; 55-LYS-LYS-56; 71-LYS-GLU-72; 95-ASP-LYS-96;
RP 101-ARG--ASP-104 AND 116-THR--ALA-122.
RX PubMed=9599802; DOI=10.1007/s004250050291;
RA Ishiwatari Y., Fujiwara T., McFarland K.C., Nemoto K., Hayashi H.,
RA Chino M., Lucas W.J.;
RT "Rice phloem thioredoxin h has the capacity to mediate its own cell-to-cell
RT transport through plasmodesmata.";
RL Planta 205:12-22(1998).
RN [8]
RP INDUCTION.
RX PubMed=15618434; DOI=10.1104/pp.104.045658;
RA Tsukamoto S., Morita S., Hirano E., Yokoi H., Masumura T., Tanaka K.;
RT "A novel cis-element that is responsive to oxidative stress regulates three
RT antioxidant defense genes in rice.";
RL Plant Physiol. 137:317-327(2005).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=19665023; DOI=10.1016/j.febslet.2009.07.057;
RA Xie G., Kato H., Sasaki K., Imai R.;
RT "A cold-induced thioredoxin h of rice, OsTrx23, negatively regulates kinase
RT activities of OsMPK3 and OsMPK6 in vitro.";
RL FEBS Lett. 583:2734-2738(2009).
RN [10]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19825616; DOI=10.1093/mp/ssn076;
RA Chibani K., Wingsle G., Jacquot J.P., Gelhaye E., Rouhier N.;
RT "Comparative genomic study of the thioredoxin family in photosynthetic
RT organisms with emphasis on Populus trichocarpa.";
RL Mol. Plant 2:308-322(2009).
RN [11]
RP STRUCTURE BY NMR.
RA Kumeta H., Ogura H., Akagi K., Katoh E., Inagaki F.;
RT "Solution structure of thioredoxin type h from Oryza sativa.";
RL Submitted (JUL-2004) to the PDB data bank.
CC -!- FUNCTION: Thiol-disulfide oxidoreductase involved in the redox
CC regulation of MAP kinases. Under reducing conditions, inhibits MPK1 and
CC MPK5 kinase activities. Mediates its own transport from cell-to-cell
CC through plasmodesmata. Possesses insulin disulfide bonds reducing
CC activity. {ECO:0000269|PubMed:19665023, ECO:0000269|PubMed:7766047,
CC ECO:0000269|PubMed:9599802}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the phloem companion cells of leaf
CC sheaths and stems. {ECO:0000269|PubMed:7766047,
CC ECO:0000269|PubMed:9599802}.
CC -!- INDUCTION: By methyl viologen and chilling in roots and shoots.
CC {ECO:0000269|PubMed:15618434, ECO:0000269|PubMed:19665023}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. Plant H-type subfamily.
CC {ECO:0000305}.
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DR EMBL; D26547; BAA05546.1; -; Genomic_DNA.
DR EMBL; D21836; BAA04864.1; -; mRNA.
DR EMBL; AP003753; BAD30186.1; -; Genomic_DNA.
DR EMBL; AP004384; BAC79928.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF20983.1; -; Genomic_DNA.
DR EMBL; AP014963; BAT00373.1; -; Genomic_DNA.
DR EMBL; CM000144; EAZ38949.1; -; Genomic_DNA.
DR EMBL; AK059196; BAG86917.1; -; mRNA.
DR EMBL; AK121423; BAH00481.1; -; mRNA.
DR PIR; T04090; T04090.
DR RefSeq; XP_015647572.1; XM_015792086.1.
DR PDB; 1WMJ; NMR; -; A=1-122.
DR PDBsum; 1WMJ; -.
DR AlphaFoldDB; Q0D840; -.
DR SMR; Q0D840; -.
DR STRING; 4530.OS07T0186000-02; -.
DR CarbonylDB; Q0D840; -.
DR PaxDb; Q0D840; -.
DR PRIDE; Q0D840; -.
DR EnsemblPlants; Os07t0186000-02; Os07t0186000-02; Os07g0186000.
DR GeneID; 4342593; -.
DR Gramene; Os07t0186000-02; Os07t0186000-02; Os07g0186000.
DR KEGG; osa:4342593; -.
DR eggNOG; KOG0907; Eukaryota.
DR HOGENOM; CLU_090389_14_1_1; -.
DR InParanoid; Q0D840; -.
DR OMA; MKEWIKQ; -.
DR OrthoDB; 1482186at2759; -.
DR EvolutionaryTrace; Q0D840; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR Genevisible; Q0D840; OS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:UniProtKB.
DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IDA:UniProtKB.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR GO; GO:0043086; P:negative regulation of catalytic activity; IDA:UniProtKB.
DR GO; GO:0010497; P:plasmodesmata-mediated intercellular transport; IDA:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IEP:UniProtKB.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR PIRSF; PIRSF000077; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disulfide bond; Electron transport;
KW Redox-active center; Reference proteome; Transport.
FT CHAIN 1..122
FT /note="Thioredoxin H1"
FT /id="PRO_0000120057"
FT DOMAIN 2..118
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 40
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 43
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 34
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000250"
FT SITE 41
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 42
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT DISULFID 40..43
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MUTAGEN 1..5
FT /note="Missing: Loss of cell-to-cell movement."
FT /evidence="ECO:0000269|PubMed:9599802"
FT MUTAGEN 4..5
FT /note="EE->AA: Reduces the efficiency of cell-to-cell
FT movement."
FT /evidence="ECO:0000269|PubMed:9599802"
FT MUTAGEN 14..16
FT /note="KDE->AAA: Reduces the efficiency of cell-to-cell
FT movement."
FT /evidence="ECO:0000269|PubMed:9599802"
FT MUTAGEN 25..26
FT /note="KE->AA: Reduces the efficiency of cell-to-cell
FT movement."
FT /evidence="ECO:0000269|PubMed:9599802"
FT MUTAGEN 55..56
FT /note="KK->AA: Reduces the efficiency of cell-to-cell
FT movement."
FT /evidence="ECO:0000269|PubMed:9599802"
FT MUTAGEN 71..72
FT /note="KE->AA: Reduces the efficiency of cell-to-cell
FT movement."
FT /evidence="ECO:0000269|PubMed:9599802"
FT MUTAGEN 95..96
FT /note="DK->AA: Reduces the efficiency of cell-to-cell
FT movement."
FT /evidence="ECO:0000269|PubMed:9599802"
FT MUTAGEN 101..104
FT /note="RKDD->AAAA: Almost loss of cell-to-cell movement."
FT /evidence="ECO:0000269|PubMed:9599802"
FT MUTAGEN 116..122
FT /note="Missing: Reduces the efficiency of cell-to-cell
FT movement."
FT /evidence="ECO:0000269|PubMed:9599802"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:1WMJ"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:1WMJ"
FT HELIX 15..25
FT /evidence="ECO:0007829|PDB:1WMJ"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:1WMJ"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1WMJ"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:1WMJ"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:1WMJ"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:1WMJ"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:1WMJ"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:1WMJ"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:1WMJ"
FT TURN 89..92
FT /evidence="ECO:0007829|PDB:1WMJ"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:1WMJ"
FT HELIX 105..112
FT /evidence="ECO:0007829|PDB:1WMJ"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1WMJ"
SQ SEQUENCE 122 AA; 13156 MW; E595C3FDC0EE229E CRC64;
MAAEEGVVIA CHNKDEFDAQ MTKAKEAGKV VIIDFTASWC GPCRFIAPVF AEYAKKFPGA
VFLKVDVDEL KEVAEKYNVE AMPTFLFIKD GAEADKVVGA RKDDLQNTIV KHVGATAASA
SA
