RHD32_ORYSJ
ID RHD32_ORYSJ Reviewed; 823 AA.
AC Q2R224; A0A0N7KT47;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=Os11g0582300, LOC_Os11g37260; ORFNames=OsJ_34384;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(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 -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. GB1/RHD3 GTPase family. RHD3 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01052}.
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; DP000010; ABA94555.1; -; Genomic_DNA.
DR EMBL; AP008217; BAF28519.1; -; Genomic_DNA.
DR EMBL; AP014967; BAT14610.1; -; Genomic_DNA.
DR EMBL; CM000148; EEE52345.1; -; Genomic_DNA.
DR EMBL; AK100485; BAG94632.1; -; mRNA.
DR RefSeq; XP_015615176.1; XM_015759690.1.
DR AlphaFoldDB; Q2R224; -.
DR SMR; Q2R224; -.
DR STRING; 4530.OS11T0582300-02; -.
DR PaxDb; Q2R224; -.
DR PRIDE; Q2R224; -.
DR EnsemblPlants; Os11t0582300-02; Os11t0582300-02; Os11g0582300.
DR GeneID; 4350788; -.
DR Gramene; Os11t0582300-02; Os11t0582300-02; Os11g0582300.
DR KEGG; osa:4350788; -.
DR eggNOG; KOG2203; Eukaryota.
DR HOGENOM; CLU_011270_1_0_1; -.
DR InParanoid; Q2R224; -.
DR OMA; QYDITAY; -.
DR OrthoDB; 418635at2759; -.
DR Proteomes; UP000000763; Chromosome 11.
DR Proteomes; UP000007752; Chromosome 11.
DR Proteomes; UP000059680; Chromosome 11.
DR ExpressionAtlas; Q2R224; baseline and differential.
DR Genevisible; Q2R224; OS.
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..823
FT /note="Protein ROOT HAIR DEFECTIVE 3 homolog 2"
FT /id="PRO_0000407759"
FT TOPO_DOM 1..688
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 689..709
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 710..712
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 713..733
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 734..823
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 45..260
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 770..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 226..246
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COMPBIAS 787..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 55..62
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 823 AA; 92010 MW; 9B13F5F646426866 CRC64;
MEVPISGGGG GERFCHAAQV VGADGEMDGE AMARFAAGAG LLGRGLSYAV VSIVGPQGSG
KSTLLNQLFG TSFTEMDALK GRSQTTKGIW IAKAVGIEPF TVVMDLEGTD GRERGEDDTA
FEKQSALFAL AVSDIVMINL WCHDIGREHA ANRPLLKTIF EVLMRLFSPR KTTLLLVIRD
KTKTPLEYLT QALKEDIQKI WNAVRKPEVY KEAALSEFFN VEVTALSSYE EKENLFKEQV
GQLRQRFIHS IAPGGLAADR RGVIPASGFC LSALQIWKVI RENKDLNLPA HKIMVATVRC
EEIADEKLRS FISDKGWLEL ETAANSGLVP GFGKKLNAIL DFYLSEYDTE AMYFDEDVRT
AKRQQLESEI LKHTYDAFKK MLEHLHHVVL NKFKSDLEQS LRSGEGFAAS ARYCVQSSMA
EFDAGLRDAL VKHAEWDTTK VRSKLEQHIE AHATSVRGTK LAELKANYEK KLLDTLAGPV
QSILETGEKD SWACIRRLYR HATESAILAF SASLSEFELD QTTIRKMVME LREHARSIVE
EKAREEAGNV LMRMKERFST VLSRDKDSMP RTWKGNEDIR AITREARLAA LRLMSVMAAV
RLDDKPDKID RALTTALLDG GPLSQKRSIE FTSDPLASST WEEVSEKNTL ITPVQCKSIW
RQFNAETEYA VAQAISMQEA HRRSNNWLPP AWTVLLLAIL GYNEFIFLLR NPLYLLGLFV
AFVVSYAAWL QYDITAYFRH GTLSGLLTIT SGFLPTIMDI ITAVINMSHN QKSSSHPPRH
RPPLHPQSFR NQAQQQSQAQ VQYQAPSSLS SSSSVGSNSD DES
