RAA4A_ARATH
ID RAA4A_ARATH Reviewed; 226 AA.
AC Q9FJN8;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Ras-related protein RABA4a {ECO:0000303|PubMed:12644670};
DE Short=AtRABA4a {ECO:0000303|PubMed:12644670};
GN Name=RABA4A {ECO:0000303|PubMed:12644670};
GN OrderedLocusNames=At5g65270 {ECO:0000312|Araport:AT5G65270};
GN ORFNames=MQN23.22 {ECO:0000312|EMBL:BAB11663.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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).
RN [6]
RP INTERACTION WITH TCTP1.
RX PubMed=20736351; DOI=10.1073/pnas.1007926107;
RA Brioudes F., Thierry A.M., Chambrier P., Mollereau B., Bendahmane M.;
RT "Translationally controlled tumor protein is a conserved mitotic growth
RT integrator in animals and plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:16384-16389(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Intracellular vesicle trafficking and protein transport.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TCTP1. {ECO:0000269|PubMed:20736351}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AB013395; BAB11663.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98031.1; -; Genomic_DNA.
DR EMBL; AY045947; AAK76621.1; -; mRNA.
DR EMBL; AY079309; AAL85040.1; -; mRNA.
DR EMBL; AY087004; AAM64565.1; -; mRNA.
DR RefSeq; NP_201330.1; NM_125925.4.
DR AlphaFoldDB; Q9FJN8; -.
DR SMR; Q9FJN8; -.
DR BioGRID; 21894; 1.
DR STRING; 3702.AT5G65270.1; -.
DR iPTMnet; Q9FJN8; -.
DR PaxDb; Q9FJN8; -.
DR PRIDE; Q9FJN8; -.
DR ProteomicsDB; 225902; -.
DR EnsemblPlants; AT5G65270.1; AT5G65270.1; AT5G65270.
DR GeneID; 836652; -.
DR Gramene; AT5G65270.1; AT5G65270.1; AT5G65270.
DR KEGG; ath:AT5G65270; -.
DR Araport; AT5G65270; -.
DR TAIR; locus:2171790; AT5G65270.
DR eggNOG; KOG0087; Eukaryota.
DR HOGENOM; CLU_041217_23_0_1; -.
DR InParanoid; Q9FJN8; -.
DR OMA; KRACCIN; -.
DR OrthoDB; 1133775at2759; -.
DR PhylomeDB; Q9FJN8; -.
DR PRO; PR:Q9FJN8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJN8; baseline and differential.
DR Genevisible; Q9FJN8; AT.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0042546; P:cell wall biogenesis; IMP:TAIR.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 Acetylation; Cell membrane; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..226
FT /note="Ras-related protein RABA4a"
FT /id="PRO_0000407344"
FT REGION 189..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 46..54
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 24..31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 72..76
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 130..133
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 160..161
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT LIPID 223
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 224
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 226 AA; 24842 MW; 28975BD201CE2226 CRC64;
MTSGGGYGDP SQKIDYVFKV VLIGDSAVGK SQILARYARD EFSLDSKATI GVEFQTRTLV
IDHKSVKAQI WDTAGQERYR AVTSAYYRGA VGAMLVYDIT RRQTFDHIPR WLEELRAHAD
KNIVIILIGN KSDLVDQRAI PTEDAKEFAE KEGLFFLETS AFNATNVESA FSTVLTEIFN
IVNKKSLAAS EDQENGNPGS LAGKKIDIVP GPGQVIPNKS NMCCNS
