WAT1_ARATH
ID WAT1_ARATH Reviewed; 389 AA.
AC Q94AP3; Q0WMC8; Q9LQZ3;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Protein WALLS ARE THIN 1;
GN Name=WAT1; OrderedLocusNames=At1g75500; ORFNames=F10A5.28, F1B16.19;
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].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17151019; DOI=10.1074/mcp.m600250-mcp200;
RA Jaquinod M., Villiers F., Kieffer-Jaquinod S., Hugouvieux V., Bruley C.,
RA Garin J., Bourguignon J.;
RT "A proteomics dissection of Arabidopsis thaliana vacuoles isolated from
RT cell culture.";
RL Mol. Cell. Proteomics 6:394-412(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=20497379; DOI=10.1111/j.1365-313x.2010.04256.x;
RA Ranocha P., Denance N., Vanholme R., Freydier A., Martinez Y., Hoffmann L.,
RA Koehler L., Pouzet C., Renou J.-P., Sundberg B., Boerjan W., Goffner D.;
RT "Walls are thin 1 (WAT1), an Arabidopsis homolog of Medicago truncatula
RT NODULIN21, is a tonoplast-localized protein required for secondary wall
RT formation in fibers.";
RL Plant J. 63:469-483(2010).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20935503; DOI=10.4161/psb.5.10.13103;
RA Denance N., Ranocha P., Martinez Y., Sundberg B., Goffner D.;
RT "Light-regulated compensation of wat1 (walls are thin1) growth and
RT secondary cell wall phenotypes is auxin-independent.";
RL Plant Signal. Behav. 5:1302-1304(2010).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22978675; DOI=10.1111/tpj.12027;
RA Denance N., Ranocha P., Oria N., Barlet X., Riviere M.-P., Yadeta K.A.,
RA Hoffmann L., Perreau F., Clement G., Maia-Grondard A., van den Berg G.C.M.,
RA Savelli B., Fournier S., Aubert Y., Pelletier S., Thomma B.P.H.J.,
RA Molina A., Jouanin L., Marco Y., Goffner D.;
RT "Arabidopsis wat1 (walls are thin1)-mediated resistance to the bacterial
RT vascular pathogen, Ralstonia solanacearum, is accompanied by cross-
RT regulation of salicylic acid and tryptophan metabolism.";
RL Plant J. 73:225-239(2013).
CC -!- FUNCTION: Required for secondary wall formation in fibers, especially
CC in short days conditions. Promotes indole metabolism and transport
CC (e.g. tryptophan, neoglucobrassicin and auxin (indole-3-acetic acid)).
CC May prevent salicylic-acid (SA) accumulation.
CC {ECO:0000269|PubMed:20497379, ECO:0000269|PubMed:20935503,
CC ECO:0000269|PubMed:22978675}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:17151019,
CC ECO:0000269|PubMed:20497379}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17151019, ECO:0000269|PubMed:20497379}. Note=Also
CC detected in transvacuolar strands.
CC -!- TISSUE SPECIFICITY: Mostly expressed in stems and hypocotyls, also
CC present in seedlings, root, leaves, flowers and siliques. Ubiquitous,
CC mostly expressed in vascular tissues and secondary wall-forming cells,
CC including developing xylem vessels and fibers.
CC {ECO:0000269|PubMed:20497379}.
CC -!- DISRUPTION PHENOTYPE: In stems, defect in cell elongation resulting in
CC dwarf and bushy plants with altered mechanical properties, as well as
CC little to no secondary cell walls in fibers, including xylary and
CC interfascicular fibers; these symptoms are partly reversed by
CC continuous light conditions. At the flowering stage, red, dry and bent
CC downwards stem apices. General repression of indole metabolism,
CC including tryptophan, neoglucobrassicin and auxin (indole-3-acetic
CC acid). Broad-spectrum resistance to vascular pathogens, including the
CC bacteria Ralstonia solanacearum and Xanthomonas campestris pv.
CC campestris, and the fungi Verticillium dahliae and Verticillium albo-
CC atrum in a salicylic-acid- (SA-) dependent manner. SA accumulation in
CC roots. {ECO:0000269|PubMed:20497379, ECO:0000269|PubMed:20935503,
CC ECO:0000269|PubMed:22978675}.
CC -!- SIMILARITY: Belongs to the drug/metabolite transporter (DMT)
CC superfamily. Plant drug/metabolite exporter (P-DME) (TC 2.A.7.4)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF87121.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC006434; AAF87121.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC023754; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE35726.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35727.1; -; Genomic_DNA.
DR EMBL; AY045896; AAK76570.1; -; mRNA.
DR EMBL; AY091450; AAM14389.1; -; mRNA.
DR EMBL; BT000668; AAN31815.1; -; mRNA.
DR EMBL; AK226453; BAE98595.1; -; mRNA.
DR EMBL; AK229900; BAF01728.1; -; mRNA.
DR PIR; E96785; E96785.
DR RefSeq; NP_001185403.1; NM_001198474.1.
DR RefSeq; NP_565111.1; NM_106203.6.
DR AlphaFoldDB; Q94AP3; -.
DR BioGRID; 29105; 24.
DR IntAct; Q94AP3; 24.
DR STRING; 3702.AT1G75500.1; -.
DR iPTMnet; Q94AP3; -.
DR PaxDb; Q94AP3; -.
DR PRIDE; Q94AP3; -.
DR ProteomicsDB; 242690; -.
DR EnsemblPlants; AT1G75500.1; AT1G75500.1; AT1G75500.
DR EnsemblPlants; AT1G75500.2; AT1G75500.2; AT1G75500.
DR GeneID; 843886; -.
DR Gramene; AT1G75500.1; AT1G75500.1; AT1G75500.
DR Gramene; AT1G75500.2; AT1G75500.2; AT1G75500.
DR KEGG; ath:AT1G75500; -.
DR Araport; AT1G75500; -.
DR TAIR; locus:2005689; AT1G75500.
DR eggNOG; ENOG502QSV3; Eukaryota.
DR HOGENOM; CLU_025359_1_2_1; -.
DR InParanoid; Q94AP3; -.
DR OMA; RIMGFAM; -.
DR OrthoDB; 883954at2759; -.
DR PhylomeDB; Q94AP3; -.
DR PRO; PR:Q94AP3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94AP3; baseline and differential.
DR Genevisible; Q94AP3; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0009851; P:auxin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0010315; P:auxin export across the plasma membrane; IMP:CACAO.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009834; P:plant-type secondary cell wall biogenesis; IMP:TAIR.
DR GO; GO:0090355; P:positive regulation of auxin metabolic process; IMP:TAIR.
DR GO; GO:0090358; P:positive regulation of tryptophan metabolic process; IMP:TAIR.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
DR InterPro; IPR000620; EamA_dom.
DR InterPro; IPR030184; WAT1-related.
DR PANTHER; PTHR31218; PTHR31218; 1.
DR Pfam; PF00892; EamA; 2.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Auxin biosynthesis; Auxin signaling pathway;
KW Cell wall biogenesis/degradation; Membrane; Phosphoprotein; Plant defense;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix;
KW Tryptophan biosynthesis; Vacuole.
FT CHAIN 1..389
FT /note="Protein WALLS ARE THIN 1"
FT /id="PRO_0000421308"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 32..161
FT /note="EamA 1"
FT DOMAIN 210..339
FT /note="EamA 2"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 389 AA; 42571 MW; 19D964BF4198A01E CRC64;
MADNTDNRRS LWGVPEKLQL HIAMLTLQFG YAGFHVVSRA ALNMGISKLV FPVYRNIIAL
LLLLPFAYFL EKKERPAITL NFLIQFFFLA LIGITANQGF YLLGLDNTSP TFASSMQNSV
PAITFLMAAL LRIEKVRINR RDGISKILGT ALCVAGASVI TLYKGPTIYT PASHLHAHLL
TTNSAVLAPL GNAAPKNWTL GCIYLIGHCL SWSGWLVFQA PVLKSYPARL SVTSYTCFFG
IIQFLIIAAF CERDSQAWVF HSGWELFTIL YAGIVASGIA FAVQIWCIDR GGPVFVAVYQ
PVQTLVVAIM ASIALGEEFY LGGIIGAVLI IAGLYFVLYG KSEERKFAAL EKAAIQSSAE
HGIERAPVSR NSIKSSITTP LLHQSTDNV
