ID RAA5C_ARATH Reviewed; 214 AA. AC P28187; Q1ECF0; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 14-DEC-2022, entry version 163. DE RecName: Full=Ras-related protein RABA5c; DE Short=AtRABA5c; DE AltName: Full=Ras-related protein Ara-4; DE AltName: Full=Ras-related protein Rab11F; DE Short=AtRab11F; GN Name=RABA5C; Synonyms=ARA-4, RAB11F; OrderedLocusNames=At2g43130; GN ORFNames=F14B2.7; 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 [MRNA]. RC STRAIN=cv. Columbia, cv. En-1, cv. Est, cv. Landsberg erecta, and RC cv. Lapalmam; TISSUE=Leaf; RX PubMed=1748311; DOI=10.1016/0378-1119(91)90442-e; RA Anai T., Hasegawa K., Watanabe Y., Uchimiya H., Ishizaki R., Matsui M.; RT "Isolation and analysis of cDNAs encoding small GTP-binding proteins of RT Arabidopsis thaliana."; RL Gene 108:259-264(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617197; DOI=10.1038/45471; RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."; RL Nature 402:761-768(1999). 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]. RC STRAIN=cv. Columbia; RX PubMed=19423640; DOI=10.1093/dnares/dsp009; RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., RA Shinozaki K.; RT "Analysis of multiple occurrences of alternative splicing events in RT Arabidopsis thaliana using novel sequenced full-length cDNAs."; RL DNA Res. 16:155-164(2009). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RA Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.; RT "Arabidopsis ORF clones."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. RN [6] RP FUNCTION, AND MUTAGENESIS OF GLN-71 AND ASN-125. RX PubMed=8013629; DOI=10.1016/0014-5793(94)80696-9; RA Anai T., Matsui M., Nomura N., Ishizaki R., Uchimiya H.; RT "In vitro mutation analysis of Arabidopsis thaliana small GTP-binding RT proteins and detection of GAP-like activities in plant cells."; RL FEBS Lett. 346:175-180(1994). RN [7] RP SUBCELLULAR LOCATION. RX PubMed=8676856; DOI=10.1007/bf02174441; RA Ueda T., Anai T., Tsukaya H., Hirata A., Uchimiya H.; RT "Characterization and subcellular localization of a small GTP-binding RT protein (Ara-4) from Arabidopsis: conditional expression under control of RT the promoter of the gene for heat-shock protein HSP81-1."; RL Mol. Gen. Genet. 250:533-539(1996). RN [8] RP INDUCTION BY ABSCISIC ACID. RX PubMed=10341440; DOI=10.1046/j.1365-313x.1999.00423.x; RA Jeannette E., Rona J.P., Bardat F., Cornel D., Sotta B., Miginiac E.; RT "Induction of RAB18 gene expression and activation of K+ outward rectifying RT channels depend on an extracellular perception of ABA in Arabidopsis RT thaliana suspension cells."; RL Plant J. 18:13-22(1999). RN [9] RP INTERACTION WITH GDI1 AND PUX8. RX PubMed=10758485; DOI=10.1046/j.1365-313x.2000.00681.x; RA Ueda T., Matsuda N., Uchimiya H., Nakano A.; RT "Modes of interaction between the Arabidopsis Rab protein, Ara4, and its RT putative regulator molecules revealed by a yeast expression system."; RL Plant J. 21:341-349(2000). RN [10] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=11532937; DOI=10.1093/emboj/20.17.4730; RA Ueda T., Yamaguchi M., Uchimiya H., Nakano A.; RT "Ara6, a plant-unique novel type Rab GTPase, functions in the endocytic RT pathway of Arabidopsis thaliana."; RL EMBO J. 20:4730-4741(2001). RN [11] RP INDUCTION. RX PubMed=12401218; DOI=10.1016/s0167-4781(02)00502-x; RA Ciereszko I., Kleczkowski L.A.; RT "Effects of phosphate deficiency and sugars on expression of rab18 in RT Arabidopsis: hexokinase-dependent and okadaic acid-sensitive transduction RT of the sugar signal."; RL Biochim. Biophys. Acta 1579:43-49(2002). RN [12] RP GENE FAMILY, AND NOMENCLATURE. RX PubMed=12644670; DOI=10.1104/pp.013052; RA Vernoud V., Horton A.C., Yang Z., Nielsen E.; RT "Analysis of the small GTPase gene superfamily of Arabidopsis."; RL Plant Physiol. 131:1191-1208(2003). CC -!- FUNCTION: Intracellular vesicle trafficking and protein transport. CC Binds GTP and GDP and possesses intrinsic GTPase activity. CC {ECO:0000269|PubMed:8013629}. CC -!- SUBUNIT: Interacts (via C-terminus) with GDI1. Interacts with CC PUX8/SAY1. {ECO:0000269|PubMed:10758485}. CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000269|PubMed:11532937, ECO:0000269|PubMed:8676856}; Lipid-anchor CC {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane CC {ECO:0000269|PubMed:8676856}; Lipid-anchor {ECO:0000305}. Cell membrane CC {ECO:0000305}; Lipid-anchor {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Expressed in roots and actively dividing cells. CC {ECO:0000269|PubMed:11532937}. CC -!- INDUCTION: By abscisic acid (ABA), phosphate (Pi) deprivation, cold, CC sucrose, mannose, and water stress. {ECO:0000269|PubMed:10341440, CC ECO:0000269|PubMed:12401218}. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family. CC {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; D01026; BAA00831.1; -; mRNA. DR EMBL; AC004450; AAC64302.1; -; Genomic_DNA. DR EMBL; CP002685; AEC10212.1; -; Genomic_DNA. DR EMBL; BT025784; ABF83674.1; -; mRNA. DR EMBL; AK317205; BAH19889.1; -; mRNA. DR PIR; JS0641; JS0641. DR RefSeq; NP_181842.1; NM_129875.4. DR AlphaFoldDB; P28187; -. DR SMR; P28187; -. DR BioGRID; 4252; 4. DR IntAct; P28187; 3. DR STRING; 3702.AT2G43130.1; -. DR iPTMnet; P28187; -. DR PaxDb; P28187; -. DR ProteomicsDB; 236501; -. DR EnsemblPlants; AT2G43130.1; AT2G43130.1; AT2G43130. DR GeneID; 818915; -. DR Gramene; AT2G43130.1; AT2G43130.1; AT2G43130. DR KEGG; ath:AT2G43130; -. DR Araport; AT2G43130; -. DR TAIR; locus:2041036; AT2G43130. DR eggNOG; KOG0087; Eukaryota. DR HOGENOM; CLU_041217_23_0_1; -. DR InParanoid; P28187; -. DR OMA; IFTHIAN; -. DR OrthoDB; 1133775at2759; -. DR PhylomeDB; P28187; -. DR PRO; PR:P28187; -. DR Proteomes; UP000006548; Chromosome 2. DR ExpressionAtlas; P28187; baseline and differential. DR Genevisible; P28187; AT. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005795; C:Golgi stack; IDA:TAIR. DR GO; GO:0005798; C:Golgi-associated vesicle; IDA:TAIR. DR GO; GO:0005886; C:plasma membrane; HDA:TAIR. DR GO; GO:0005802; C:trans-Golgi network; IDA:TAIR. DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB. DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB. DR GO; GO:0048219; P:inter-Golgi cisterna vesicle-mediated transport; TAS:TAIR. DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central. DR GO; GO:0009408; P:response to heat; IEP:TAIR. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR001806; Small_GTPase. DR Pfam; PF00071; Ras; 1. DR SMART; SM00174; RHO; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51419; RAB; 1. PE 1: Evidence at protein level; KW Cell membrane; Golgi apparatus; GTP-binding; Lipoprotein; Membrane; KW Nucleotide-binding; Prenylation; Reference proteome. FT CHAIN 1..214 FT /note="Ras-related protein RABA5c" FT /id="PRO_0000121291" FT MOTIF 41..49 FT /note="Effector region" FT /evidence="ECO:0000250" FT BINDING 19..26 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 67..71 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 125..128 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 155..156 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT LIPID 211 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000250" FT LIPID 212 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000250" FT MUTAGEN 71 FT /note="Q->L: Loss of GTPase activity." FT /evidence="ECO:0000269|PubMed:8013629" FT MUTAGEN 125 FT /note="N->I: Decreases GTP-binding efficiency." FT /evidence="ECO:0000269|PubMed:8013629" SQ SEQUENCE 214 AA; 23981 MW; B5C11E754C14535C CRC64; MSDDDERGEE YLFKIVIIGD SAVGKSNLLT RYARNEFNPN SKATIGVEFQ TQSMLIDGKE VKAQIWDTAG QERFRAVTSA YYRGAVGALV VYDITRSSTF ENVGRWLDEL NTHSDTTVAK MLIGNKCDLE SIRAVSVEEG KSLAESEGLF FMETSALDST NVKTAFEMVI REIYSNISRK QLNSDSYKEE LTVNRVSLVK NENEGTKTFS CCSR //