NRX1_ARATH
ID NRX1_ARATH Reviewed; 578 AA.
AC O80763; Q8LB68;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 148.
DE RecName: Full=Probable nucleoredoxin 1;
DE Short=AtNrx1;
DE EC=1.8.1.8;
GN OrderedLocusNames=At1g60420; ORFNames=T13D8.29;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19714218; DOI=10.1371/journal.pgen.1000621;
RA Qin Y., Leydon A.R., Manziello A., Pandey R., Mount D., Denic S., Vasic B.,
RA Johnson M.A., Palanivelu R.;
RT "Penetration of the stigma and style elicits a novel transcriptome in
RT pollen tubes, pointing to genes critical for growth in a pistil.";
RL PLoS Genet. 5:E1000621-E1000621(2009).
RN [7]
RP STRUCTURE BY NMR OF 476-551.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of DC1 domain of PDI-like hypothetical protein from
RT Arabidopsis thaliana.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Probable thiol-disulfide oxidoreductase required for pollen
CC tube growth and pollen function in the pistil. Seems not to be required
CC for in vitro pollen tube growth. May be involved in the generation of
CC lipid signaling molecules in pistil. {ECO:0000269|PubMed:19714218}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) +
CC NADH; Xref=Rhea:RHEA:18749, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.8.1.8;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-dithiol + NADP(+) = [protein]-disulfide + H(+) +
CC NADPH; Xref=Rhea:RHEA:18753, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.8;
CC -!- DISRUPTION PHENOTYPE: Disruption of pollen tube growth in the pistil
CC and reduction in the ability to target ovules.
CC {ECO:0000269|PubMed:19714218}.
CC -!- SIMILARITY: Belongs to the nucleoredoxin family. {ECO:0000305}.
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DR EMBL; AC004473; AAC24068.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33684.1; -; Genomic_DNA.
DR EMBL; AY065433; AAL38874.1; -; mRNA.
DR EMBL; AY117231; AAM51306.1; -; mRNA.
DR EMBL; AY087396; AAM64945.1; -; mRNA.
DR PIR; T02292; T02292.
DR RefSeq; NP_564756.1; NM_104729.4.
DR PDB; 1V5N; NMR; -; A=476-551.
DR PDBsum; 1V5N; -.
DR AlphaFoldDB; O80763; -.
DR SMR; O80763; -.
DR BioGRID; 27561; 9.
DR IntAct; O80763; 1.
DR STRING; 3702.AT1G60420.1; -.
DR PaxDb; O80763; -.
DR PRIDE; O80763; -.
DR ProteomicsDB; 250609; -.
DR EnsemblPlants; AT1G60420.1; AT1G60420.1; AT1G60420.
DR GeneID; 842337; -.
DR Gramene; AT1G60420.1; AT1G60420.1; AT1G60420.
DR KEGG; ath:AT1G60420; -.
DR Araport; AT1G60420; -.
DR TAIR; locus:2195623; AT1G60420.
DR eggNOG; KOG2501; Eukaryota.
DR HOGENOM; CLU_019626_1_0_1; -.
DR InParanoid; O80763; -.
DR OMA; HNDFEIV; -.
DR OrthoDB; 1350271at2759; -.
DR PhylomeDB; O80763; -.
DR EvolutionaryTrace; O80763; -.
DR PRO; PR:O80763; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O80763; baseline and differential.
DR Genevisible; O80763; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:InterPro.
DR GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
DR GO; GO:0010183; P:pollen tube guidance; IMP:TAIR.
DR GO; GO:0080092; P:regulation of pollen tube growth; IMP:UniProtKB.
DR CDD; cd03009; TryX_like_TryX_NRX; 2.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR004146; DC1.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR InterPro; IPR045870; TryX_NRX_thioredoxin_dom.
DR Pfam; PF03107; C1_2; 1.
DR Pfam; PF13905; Thioredoxin_8; 3.
DR SUPFAM; SSF52833; SSF52833; 3.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; NAD; Oxidoreductase; Reference proteome; Repeat.
FT CHAIN 1..578
FT /note="Probable nucleoredoxin 1"
FT /id="PRO_0000394550"
FT DOMAIN 18..172
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 178..321
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 325..485
FT /note="Thioredoxin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT CONFLICT 97
FT /note="R -> S (in Ref. 4; AAM64945)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="G -> E (in Ref. 4; AAM64945)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="T -> I (in Ref. 4; AAM64945)"
FT /evidence="ECO:0000305"
FT CONFLICT 529
FT /note="S -> C (in Ref. 4; AAM64945)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="D -> Y (in Ref. 4; AAM64945)"
FT /evidence="ECO:0000305"
FT HELIX 482..490
FT /evidence="ECO:0007829|PDB:1V5N"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:1V5N"
FT STRAND 496..498
FT /evidence="ECO:0007829|PDB:1V5N"
FT TURN 502..505
FT /evidence="ECO:0007829|PDB:1V5N"
FT STRAND 508..511
FT /evidence="ECO:0007829|PDB:1V5N"
FT TURN 519..521
FT /evidence="ECO:0007829|PDB:1V5N"
FT STRAND 529..531
FT /evidence="ECO:0007829|PDB:1V5N"
FT TURN 533..535
FT /evidence="ECO:0007829|PDB:1V5N"
FT HELIX 541..545
FT /evidence="ECO:0007829|PDB:1V5N"
SQ SEQUENCE 578 AA; 65170 MW; 814C7EE33DAD7B5D CRC64;
MAETSKQVNG DDAQDLHSLL SSPARDFLVR NDGEQVKVDS LLGKKIGLYF SAAWCGPCQR
FTPQLVEVYN ELSSKVGFEI VFVSGDEDEE SFGDYFRKMP WLAVPFTDSE TRDRLDELFK
VRGIPNLVMV DDHGKLVNEN GVGVIRSYGA DAYPFTPEKM KEIKEDEDRA RRGQTLRSVL
VTPSRDFVIS PDGNKVPVSE LEGKTIGLLF SVASYRKCTE LTPKLVEFYT KLKENKEDFE
IVLISLEDDE ESFNQDFKTK PWLALPFNDK SGSKLARHFM LSTLPTLVIL GPDGKTRHSN
VAEAIDDYGV LAYPFTPEKF QELKELEKAK VEAQTLESLL VSGDLNYVLG KDGAKVLVSD
LVGKTILMYF SAHWCPPCRA FTPKLVEVYK QIKERNEAFE LIFISSDRDQ ESFDEYYSQM
PWLALPFGDP RKASLAKTFK VGGIPMLAAL GPTGQTVTKE ARDLVVAHGA DAYPFTEERL
KEIEAKYDEI AKDWPKKVKH VLHEEHELEL TRVQVYTCDK CEEEGTIWSY HCDECDFDLH
AKCALNEDTK ENGDEAVKVG GDESKDGWVC EGNVCTKA
