RHD31_ARATH
ID RHD31_ARATH Reviewed; 795 AA.
AC Q9SSN0;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Protein ROOT HAIR DEFECTIVE 3 homolog 1 {ECO:0000255|HAMAP-Rule:MF_03109};
DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_03109};
DE AltName: Full=Protein SEY1 homolog 2 {ECO:0000255|HAMAP-Rule:MF_03109};
GN OrderedLocusNames=At1g72960; ORFNames=F3N23.16;
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 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: Specifically expressed in 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; AC008017; AAD55643.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35396.1; -; Genomic_DNA.
DR PIR; H96754; H96754.
DR RefSeq; NP_177439.2; NM_105954.3.
DR AlphaFoldDB; Q9SSN0; -.
DR SMR; Q9SSN0; -.
DR STRING; 3702.AT1G72960.1; -.
DR PaxDb; Q9SSN0; -.
DR PRIDE; Q9SSN0; -.
DR ProteomicsDB; 236915; -.
DR EnsemblPlants; AT1G72960.1; AT1G72960.1; AT1G72960.
DR GeneID; 843627; -.
DR Gramene; AT1G72960.1; AT1G72960.1; AT1G72960.
DR KEGG; ath:AT1G72960; -.
DR Araport; AT1G72960; -.
DR TAIR; locus:2032612; AT1G72960.
DR eggNOG; KOG2203; Eukaryota.
DR HOGENOM; CLU_011270_1_0_1; -.
DR InParanoid; Q9SSN0; -.
DR OMA; ICNDKSE; -.
DR OrthoDB; 418635at2759; -.
DR PRO; PR:Q9SSN0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SSN0; baseline and differential.
DR Genevisible; Q9SSN0; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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..795
FT /note="Protein ROOT HAIR DEFECTIVE 3 homolog 1"
FT /id="PRO_0000407755"
FT TOPO_DOM 1..682
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 683..703
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 704..706
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 707..727
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 728..795
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 39..254
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 761..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 218..244
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COMPBIAS 770..786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 49..56
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 795 AA; 88819 MW; E46CC2CC448139EB CRC64;
MDADKSEGCC SVQLIDGDGI YNVSRIDHFI KDVKLADCGL SYAVVSIMGP QSSGKSTLLN
HLFGTNFMEM DAFKGRSQTT KGIWLARCAG IEPCTLVMDL EGTDGRERGE DDTAFEKQSA
LFALAISDIV LINMWCHDIG REQAANKPLL KTVFQVMMRL FSPRKTTMLF VIRDKTRTPL
ENLEPVLRED IQKIWDSVPK PEAHKETPLS DFFNVEVVAL SSYEEKEEQF KEQIASLRQR
FMHSIAPGGL AGDRRGVIPA SGFAFSADQI WRVIKENKDL DLPAHKVMVA TVRCEEIANE
KFAHFITNED WRKLDEEVQA GPVSNFGKRL TTILGSCLSE YDGEATFFDE GVRSSKRQQL
EEKLLQLVNP AFQDVLGHIR WGILEKFKAS FDKALGIGEG FSSASQDWFK ACMTQFDEEC
AGAIIEQANW DTSKVRDKLV RDIEAHISSV RTSKLSELTS LYESKVHEAL SEPVEALLDG
ANDETWSTVK KLHRRETESA VSGLSSALAG FDMEEETRDR MVKSLQDYAR GVIETKAKEE
AVRVLMRMKE RFGTIFSHDS DSMPRVWTGK EDLRAITKSA RSASLKLLSV MAVIRLGDEP
DNIEKTLTVA LLDPTKNDTS KKSITTSDPL ASSTWDEVPS SRTLITPVQC KSIWRQFKTE
TEYTVTQAIS AQEANRRGNN WLPPPWAILA LIVLGFNEFM TLLRNPLYLG VMFVAFLLAK
ALWTQLDIPG EFRNGALPGL ISISAKFVPT VMNLIKNLAA QGEDPPAANP ENRRSSNNTS
SSENPPDHKS SSKED
