RHD32_ARATH
ID RHD32_ARATH Reviewed; 834 AA.
AC Q9FKE9;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Protein ROOT HAIR DEFECTIVE 3 homolog 2 {ECO:0000255|HAMAP-Rule:MF_03109};
DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_03109};
DE AltName: Full=Protein SEY1 homolog 3 {ECO:0000255|HAMAP-Rule:MF_03109};
GN OrderedLocusNames=At5g45160; ORFNames=K18C1.4;
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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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 TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: Probable GTP-binding protein that may be involved in cell
CC development. {ECO:0000255|HAMAP-Rule:MF_03109}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03109}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03109}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and flowers.
CC {ECO:0000269|PubMed:12844267}.
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; AB012240; BAB11389.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95211.1; -; Genomic_DNA.
DR RefSeq; NP_199329.1; NM_123884.4.
DR AlphaFoldDB; Q9FKE9; -.
DR SMR; Q9FKE9; -.
DR STRING; 3702.AT5G45160.1; -.
DR iPTMnet; Q9FKE9; -.
DR PaxDb; Q9FKE9; -.
DR PRIDE; Q9FKE9; -.
DR ProteomicsDB; 236174; -.
DR EnsemblPlants; AT5G45160.1; AT5G45160.1; AT5G45160.
DR GeneID; 834552; -.
DR Gramene; AT5G45160.1; AT5G45160.1; AT5G45160.
DR KEGG; ath:AT5G45160; -.
DR Araport; AT5G45160; -.
DR TAIR; locus:2153343; AT5G45160.
DR eggNOG; KOG2203; Eukaryota.
DR HOGENOM; CLU_011270_1_0_1; -.
DR InParanoid; Q9FKE9; -.
DR OMA; DERPDNI; -.
DR OrthoDB; 418635at2759; -.
DR PhylomeDB; Q9FKE9; -.
DR PRO; PR:Q9FKE9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKE9; baseline and differential.
DR Genevisible; Q9FKE9; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0016320; P:endoplasmic reticulum membrane fusion; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Coiled coil; Endoplasmic reticulum; GTP-binding; Hydrolase; Membrane;
KW Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..834
FT /note="Protein ROOT HAIR DEFECTIVE 3 homolog 2"
FT /id="PRO_0000407756"
FT TOPO_DOM 1..683
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 684..704
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 705..707
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 708..728
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 729..834
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 37..252
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 767..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 214..241
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COMPBIAS 768..809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 47..54
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 834 AA; 93570 MW; FABB3AF47E3DA8AE CRC64;
MGENDDGCST QLIDGNGEFN VKGLDNFVKK TKLSDCGLSY AVVAIMGPQS SGKSTLLNHL
FKTSFREMDA FAGRSQTTKG IWMARCVGIE PFTIAMDLEG TDGRERGEDD TTFEKQSALF
AIAVADIVLI NMWCHDIGRE QAANKPLLKT VFQVMLRLFS PRKTTLLFVI RDKTKTPIEL
LERALREDIQ KIWDSVRKPE AHKNTPLNEF FNVMIVALSS YEEKEKQFEQ EVAELRQRFF
HSISPGGLAG DRRGVVPASG FSFSSQQIWK VIKENRDLDL PAHKVMVATV RCEEIANEKL
RDLATNESWL ELHEAAEGGL VPGFGKKLSS ILEKYFSEYD AEAIYFDEGV RKEKRLQLKL
NALDFVYPSY ATMLGHLRSN ALESFKIRLE QSLNQGEGFA KAVRDSQQSC LMVFDKGCED
AAVKQATWDA SKIREKLCRD IDAHTFFARS AKLSELTANY EKRLTQALSE PVESLFEAGG
KETWPSIRKL LKRETETAVT DFLDVVTGFE LDHAKIDAMV QNLKNYSQSL VEKKAREEAA
KILIRMKDRF STVFSHDKDS MPRVWTGKED IRAITKDARA EALSLLSVMT AIRLDERPDN
IESTLFSSLM DGTVSAASSH NRSVGTSTDP LASSSWEEVP PNNILLTPVQ CKSLWRQFKS
ETEYTVTQAI SAQEAHKRNN NWLPPAWAIV LMIVLGFNEF MMLLKNPLYL LGFFVAFLLS
KALWVQLDIP REFQHGAVAG VLSITSKFLP TVMNLLRKLA EEAQGKTTQE VPDLSASQTY
RQQSPSHSIS STISESVASN ISSAGDDAEY SSPSPALVRR RNTNNVQESE ISQM
