RAA1A_ARATH
ID RAA1A_ARATH Reviewed; 216 AA.
AC P28185;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Ras-related protein RABA1a;
DE Short=AtRABA1a;
DE AltName: Full=Ras-related protein Ara-2;
DE AltName: Full=Ras-related protein Rab11E;
DE Short=AtRab11E;
GN Name=RABA1A; Synonyms=ARA-2, RAB11E; OrderedLocusNames=At1g06400;
GN ORFNames=T2D23.10, T2D23_5;
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=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 [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=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 [5]
RP FUNCTION, AND MUTAGENESIS OF GLN-72 AND ASN-126.
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 [6]
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY AUXIN, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19199049; DOI=10.1007/s11103-009-9460-7;
RA Koh E.J., Kwon Y.R., Kim K.I., Hong S.W., Lee H.;
RT "Altered ARA2 (RABA1a) expression in Arabidopsis reveals the involvement of
RT a Rab/YPT family member in auxin-mediated responses.";
RL Plant Mol. Biol. 70:113-122(2009).
CC -!- FUNCTION: Involved in auxin-mediated response. May be involved in
CC vesicle trafficking of components involved in polar auxin transport.
CC Binds GTP and GDP and possesses intrinsic GTPase activity.
CC {ECO:0000269|PubMed:19199049, ECO:0000269|PubMed:8013629}.
CC -!- INTERACTION:
CC P28185; Q8LA96: At4g17720; NbExp=3; IntAct=EBI-16944336, EBI-4425250;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:19199049};
CC Lipid-anchor {ECO:0000305|PubMed:19199049}. Note=Located in the plasma
CC membrane and endocytic vesicles derived from the plasma membrane.
CC -!- INDUCTION: By auxin. {ECO:0000269|PubMed:19199049}.
CC -!- DISRUPTION PHENOTYPE: Slight increase of primary root elongation and
CC lateral root branching and hypersensitivity of root growth in response
CC to exogenous auxin. {ECO:0000269|PubMed:19199049}.
CC -!- MISCELLANEOUS: Plants overexpressing RABA1A show reduced growth of
CC roots and shoots and smaller leaf sizes. {ECO:0000305|PubMed:19199049}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; D01024; BAA00829.1; -; mRNA.
DR EMBL; AC068143; AAF82168.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27982.1; -; Genomic_DNA.
DR EMBL; AF332428; AAG48791.1; -; mRNA.
DR EMBL; AY065306; AAL38782.1; -; mRNA.
DR EMBL; AY096439; AAM20079.1; -; mRNA.
DR PIR; JS0639; JS0639.
DR RefSeq; NP_172128.1; NM_100520.4.
DR PDB; 5XR4; X-ray; 2.80 A; A/B=10-182.
DR PDB; 5XR6; X-ray; 2.60 A; A/B=10-182.
DR PDB; 5XR7; X-ray; 2.60 A; A/B=10-182.
DR PDBsum; 5XR4; -.
DR PDBsum; 5XR6; -.
DR PDBsum; 5XR7; -.
DR AlphaFoldDB; P28185; -.
DR SMR; P28185; -.
DR BioGRID; 22392; 3.
DR IntAct; P28185; 2.
DR STRING; 3702.AT1G06400.1; -.
DR iPTMnet; P28185; -.
DR PaxDb; P28185; -.
DR PRIDE; P28185; -.
DR ProteomicsDB; 236611; -.
DR EnsemblPlants; AT1G06400.1; AT1G06400.1; AT1G06400.
DR GeneID; 837151; -.
DR Gramene; AT1G06400.1; AT1G06400.1; AT1G06400.
DR KEGG; ath:AT1G06400; -.
DR Araport; AT1G06400; -.
DR TAIR; locus:2202280; AT1G06400.
DR eggNOG; KOG0087; Eukaryota.
DR HOGENOM; CLU_041217_23_0_1; -.
DR InParanoid; P28185; -.
DR OMA; RFGCCSN; -.
DR OrthoDB; 1133775at2759; -.
DR PhylomeDB; P28185; -.
DR PRO; PR:P28185; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P28185; baseline and differential.
DR Genevisible; P28185; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005768; C:endosome; IDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0042546; P:cell wall biogenesis; IMP:TAIR.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0009733; P:response to auxin; IMP:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
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 3D-structure; Cell membrane; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..216
FT /note="Ras-related protein RABA1a"
FT /id="PRO_0000121162"
FT MOTIF 42..50
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 20..27
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 68..72
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 156..157
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 213
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 214
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 72
FT /note="Q->L: Loss of GTPase activity."
FT /evidence="ECO:0000269|PubMed:8013629"
FT MUTAGEN 126
FT /note="N->I: Decreases GTP-binding."
FT /evidence="ECO:0000269|PubMed:8013629"
FT STRAND 11..19
FT /evidence="ECO:0007829|PDB:5XR6"
FT HELIX 26..34
FT /evidence="ECO:0007829|PDB:5XR6"
FT STRAND 47..57
FT /evidence="ECO:0007829|PDB:5XR6"
FT STRAND 60..69
FT /evidence="ECO:0007829|PDB:5XR6"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:5XR4"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:5XR4"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:5XR6"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:5XR6"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:5XR6"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:5XR6"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:5XR6"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:5XR6"
FT HELIX 138..148
FT /evidence="ECO:0007829|PDB:5XR6"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:5XR6"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:5XR6"
FT HELIX 163..178
FT /evidence="ECO:0007829|PDB:5XR6"
SQ SEQUENCE 216 AA; 23927 MW; 90744490A913954C CRC64;
MAGYRADEEY DYLFKLVLIG DSGVGKSNLL SRFTKNEFNL ESKSTIGVEF ATKTTKVEGK
VVKAQIWDTA GQERYRAITS AYYRGAVGAL LIYDVTRHAT FENAARWLRE LRGHTDPNIV
VMLIGNKCDL RHLVAVKTEE AKAFAERESL YFMETSALDA TNVENAFTEV LTQIHKIVSK
RSVDGGGESA DLPGKGETIN VKEDGSVLKR MGCCSN
