RAA5C_ARATH
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 03-AUG-2022, entry version 161.
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}.
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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 PRIDE; 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; SSF52540; 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
