RHD3_ARATH
ID RHD3_ARATH Reviewed; 802 AA.
AC P93042; Q0WL83; Q3EB66;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Protein ROOT HAIR DEFECTIVE 3 {ECO:0000255|HAMAP-Rule:MF_03109};
DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_03109};
DE AltName: Full=Protein FRAGILE FIBER 4 {ECO:0000255|HAMAP-Rule:MF_03109};
DE AltName: Full=Protein SEY1 homolog 1 {ECO:0000255|HAMAP-Rule:MF_03109};
GN Name=RHD3; Synonyms=FRA4; OrderedLocusNames=At3g13870; ORFNames=MCP4.11;
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 [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF ILE-134; ASP-185 AND ALA-575.
RX PubMed=9087433; DOI=10.1101/gad.11.6.799;
RA Wang H., Lockwood S.K., Hoeltzel M.F., Schiefelbein J.W.;
RT "The ROOT HAIR DEFECTIVE3 gene encodes an evolutionarily conserved protein
RT with GTP-binding motifs and is required for regulated cell enlargement in
RT Arabidopsis.";
RL Genes Dev. 11:799-811(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 218-802.
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9084218; DOI=10.1007/bf01007706;
RA Galway M.E., Heckman J.W. Jr., Schiefelbein J.W.;
RT "Growth and ultrastructure of Arabidopsis root hairs: the rhd3 mutation
RT alters vacuole enlargement and tip growth.";
RL Planta 201:209-218(1997).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12068108; DOI=10.1104/pp.002675;
RA Wang H., Lee M.M., Schiefelbein J.W.;
RT "Regulation of the cell expansion gene RHD3 during Arabidopsis
RT development.";
RL Plant Physiol. 129:638-649(2002).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP ASP-185.
RX PubMed=12844267; DOI=10.1007/s00425-003-1067-7;
RA Hu Y., Zhong R., Morrison W.H. III, Ye Z.H.;
RT "The Arabidopsis RHD3 gene is required for cell wall biosynthesis and actin
RT organization.";
RL Planta 217:912-921(2003).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14731265; DOI=10.1046/j.1365-313x.2003.01969.x;
RA Zheng H., Kunst L., Hawes C., Moore I.;
RT "A GFP-based assay reveals a role for RHD3 in transport between the
RT endoplasmic reticulum and Golgi apparatus.";
RL Plant J. 37:398-414(2004).
RN [10]
RP FUNCTION.
RX PubMed=15908600; DOI=10.1104/pp.105.059774;
RA Yuen C.Y., Sedbrook J.C., Perrin R.M., Carroll K.L., Masson P.H.;
RT "Loss-of-function mutations of ROOT HAIR DEFECTIVE3 suppress root waving,
RT skewing, and epidermal cell file rotation in Arabidopsis.";
RL Plant Physiol. 138:701-714(2005).
CC -!- FUNCTION: Probable GTP-binding protein involved in cell wall expansion.
CC Required for appropriate root and root hair cells enlargement. May
CC inhibit vacuole enlargement during root hair cell expansion. Plays a
CC role in cell wall biosynthesis and actin organization. Seems to act
CC independently from auxin and ethylene pathways. May regulate membrane
CC traffic from the Golgi apparatus towards the endoplasmic reticulum
CC (ER). {ECO:0000269|PubMed:12068108, ECO:0000269|PubMed:12844267,
CC ECO:0000269|PubMed:14731265, ECO:0000269|PubMed:15908600,
CC ECO:0000269|PubMed:9084218, ECO:0000269|PubMed:9087433}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:14731265}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:14731265}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:14731265}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P93042-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P93042-2; Sequence=VSP_040970;
CC -!- TISSUE SPECIFICITY: Highly expressed in fiber and xylem cells.
CC Expressed in roots, cotyledons, seedling hypocotyls, stems, pedicel,
CC stigmatic papillae cells and anthers. {ECO:0000269|PubMed:12068108,
CC ECO:0000269|PubMed:12844267, ECO:0000269|PubMed:9087433}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the embryo throughout development.
CC {ECO:0000269|PubMed:12068108}.
CC -!- DISRUPTION PHENOTYPE: Reduced root and root hair length due to defect
CC in epidermal cell growth and enlargement. Reduced size of vacuole and
CC increase in the proportion of cytoplasm in root hair cells. Strong
CC reduction in the cell wall thickness of fibers, vessels and pith cells
CC in the inflorescence stems. Reduced cellulose content and altered
CC composition of the cell wall. Altered organization of the actin
CC cytoskeleton. {ECO:0000269|PubMed:12844267, ECO:0000269|PubMed:9084218,
CC ECO:0000269|PubMed:9087433}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. GB1/RHD3 GTPase family. RHD3 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01052}.
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DR EMBL; U86081; AAB58375.1; -; Genomic_DNA.
DR EMBL; AB028610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002686; AEE75428.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75429.1; -; Genomic_DNA.
DR EMBL; AY092988; AAM12987.1; -; mRNA.
DR EMBL; AY128801; AAM91201.1; -; mRNA.
DR EMBL; AK230324; BAF02124.1; -; mRNA.
DR RefSeq; NP_188003.1; NM_112241.4. [P93042-1]
DR RefSeq; NP_974308.1; NM_202579.1. [P93042-2]
DR AlphaFoldDB; P93042; -.
DR SMR; P93042; -.
DR BioGRID; 5934; 2.
DR STRING; 3702.AT3G13870.1; -.
DR iPTMnet; P93042; -.
DR PaxDb; P93042; -.
DR PRIDE; P93042; -.
DR ProteomicsDB; 236175; -. [P93042-1]
DR EnsemblPlants; AT3G13870.1; AT3G13870.1; AT3G13870. [P93042-1]
DR EnsemblPlants; AT3G13870.2; AT3G13870.2; AT3G13870. [P93042-2]
DR GeneID; 820600; -.
DR Gramene; AT3G13870.1; AT3G13870.1; AT3G13870. [P93042-1]
DR Gramene; AT3G13870.2; AT3G13870.2; AT3G13870. [P93042-2]
DR KEGG; ath:AT3G13870; -.
DR Araport; AT3G13870; -.
DR TAIR; locus:2087964; AT3G13870.
DR eggNOG; KOG2203; Eukaryota.
DR HOGENOM; CLU_011270_1_0_1; -.
DR InParanoid; P93042; -.
DR OMA; TNFDVMD; -.
DR OrthoDB; 418635at2759; -.
DR PhylomeDB; P93042; -.
DR PRO; PR:P93042; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P93042; baseline and differential.
DR Genevisible; P93042; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005525; F:GTP binding; ISS:TAIR.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:TAIR.
DR GO; GO:0009932; P:cell tip growth; IMP:TAIR.
DR GO; GO:0016320; P:endoplasmic reticulum membrane fusion; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:TAIR.
DR GO; GO:0009832; P:plant-type cell wall biogenesis; IMP:TAIR.
DR GO; GO:0010053; P:root epidermal cell differentiation; IMP:TAIR.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03109; Sey1; 1.
DR InterPro; IPR030386; G_GB1_RHD3_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008803; RHD3/Sey1.
DR PANTHER; PTHR45923; PTHR45923; 1.
DR Pfam; PF05879; RHD3; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51715; G_GB1_RHD3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Endoplasmic reticulum;
KW ER-Golgi transport; Golgi apparatus; GTP-binding; Hydrolase; Membrane;
KW Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..802
FT /note="Protein ROOT HAIR DEFECTIVE 3"
FT /id="PRO_0000407754"
FT TOPO_DOM 1..677
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 678..698
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 699..701
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 702..722
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 723..802
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 34..249
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 757..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 214..235
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COILED 429..449
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COMPBIAS 758..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44..51
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT VAR_SEQ 1..71
FT /note="MDAACSTQLIDGDGVFNVSGVDHFIKEVKLDECGLSYAVVSIMGPQSSGKST
FT LLNHLFGTNFREMDAFRGR -> MHLEEGM (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_040970"
FT MUTAGEN 134
FT /note="I->T: In rhd3-5; reduced root and root hair length."
FT /evidence="ECO:0000269|PubMed:9087433"
FT MUTAGEN 185
FT /note="D->N: In rhd3-2/fra4; reduced root and root hair
FT length. Strong reduction in the cell wall thickness of
FT fibers and vessels."
FT /evidence="ECO:0000269|PubMed:12844267,
FT ECO:0000269|PubMed:9087433"
FT MUTAGEN 575
FT /note="A->V: In rhd3-1; reduced root and root hair length."
FT /evidence="ECO:0000269|PubMed:9087433"
SQ SEQUENCE 802 AA; 89092 MW; CC18B67CA527EEA6 CRC64;
MDAACSTQLI DGDGVFNVSG VDHFIKEVKL DECGLSYAVV SIMGPQSSGK STLLNHLFGT
NFREMDAFRG RSQTTKGIWI ARCAGIEPCT VVMDLEGTDG RERGEDDTAF EKQSALFALA
VSDIVLINMW CHDIGREQAA NKPLLKTVFQ VMMRLFSPRK TTLMFVIRDK TRTPLENLEP
VLREDIQKIW DSVPKPQAHK ETPLSDFFNV EVVALSSYEE KEEQFKEQVY NLRQRFFQSV
APGGLAGDRR GVVPANAFAF SAKQMWQVIK DNKDLDLPAH KVMVATVRCE EIANEKFSSF
IANENWRELE EAVQSGPVSG FGRKLSSILQ ASLSEYDTEA TYFEESVRSS KRQQLQEKLL
QLVQPTFQDV LGHLRAGALE NFKNAFEKAL DAGEGFSSSA KSCAQSCISK FDKGCEEAVI
EQAKWDTSKT REKLERDIEA HISSVRTAKL AELTTLYESK LNVALSGPVE ALLDGANDET
WPAIRKLLRR EGELAVYGLS NALSGFEMDE ETRSKMLADL ENYARGIVET KAKEEAGRAM
MRMKDRFATI FSHDSDSMPR VWTGKEDIRA ITKMARSASL KLLSVMAVIR LDDELDNIEK
TLTLALFNST GNNATSKSIS TIDSLASSTW EKVAPEKTLI TPVQCKSLWR QFKNETEYTV
TQAISAQEAN RRNNNWLPPP WAILALVVLG FNEFMTLLRN PLWLLVLFVG YLVSKALWVQ
LNISGEFQNG VLPGLLSLST KFIPTVMNLL KKLAEEGQAP PTNSNQSMNS TAQSEVTTNG
ESSSSSSSGS SPAKNVPIDT SA
