RAG3B_ARATH
ID RAG3B_ARATH Reviewed; 203 AA.
AC O04157; Q2HIJ2;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Ras-related protein RABG3b;
DE Short=AtRABG3b;
DE AltName: Full=Ras-related protein Rab75;
DE Short=AtRab75;
GN Name=RABG3B; Synonyms=RAB7, RAB75; OrderedLocusNames=At1g22740;
GN ORFNames=T22J18.9;
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].
RA Ueda T., Wada Y., Nakano A.;
RT "Rab7 homologs in Arabidopsis thaliana.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=9369203; DOI=10.1016/s0014-5793(97)01190-3;
RA Terryn N., Neyt P., de Clercq R., de Keyser A., van den Daele H.,
RA Ardiles W., Dehais P., Rouze P., Gielen J., Villarroel R., van Montagu M.;
RT "Sequence analysis of a 24-kb contiguous genomic region at the Arabidopsis
RT thaliana PFL locus on chromosome 1.";
RL FEBS Lett. 416:156-160(1997).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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, TISSUE SPECIFICITY, AND MUTAGENESIS OF THR-22 AND GLN-67.
RX PubMed=20659276; DOI=10.1111/j.1365-313x.2010.04315.x;
RA Kwon S.I., Cho H.J., Jung J.H., Yoshimoto K., Shirasu K., Park O.K.;
RT "The Rab GTPase RabG3b functions in autophagy and contributes to tracheary
RT element differentiation in Arabidopsis.";
RL Plant J. 64:151-164(2010).
RN [8]
RP INTERACTION WITH VPS39.
RX PubMed=29463724; DOI=10.1073/pnas.1717839115;
RA Takemoto K., Ebine K., Askani J.C., Krueger F., Gonzalez Z.A., Ito E.,
RA Goh T., Schumacher K., Nakano A., Ueda T.;
RT "Distinct sets of tethering complexes, SNARE complexes, and Rab GTPases
RT mediate membrane fusion at the vacuole in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E2457-E2466(2018).
CC -!- FUNCTION: Intracellular vesicle trafficking and protein transport.
CC Functions in autophagy. Involved in xylem and tracheary element
CC differentiation. {ECO:0000269|PubMed:20659276}.
CC -!- SUBUNIT: Interacts with VPS39. {ECO:0000269|PubMed:29463724}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in xylem cells of inflorescence stems.
CC {ECO:0000269|PubMed:20659276}.
CC -!- MISCELLANEOUS: Plants silencing RABG3B display a significant decrease
CC in the number of both protoxylem and metaxylem cells in the basal
CC region of inflorescence stems. {ECO:0000305|PubMed:20659276}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AB071850; BAB68375.1; -; mRNA.
DR EMBL; Y09821; CAA70951.1; -; mRNA.
DR EMBL; Y12227; CAA72904.1; -; Genomic_DNA.
DR EMBL; AC003979; AAC25512.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30279.1; -; Genomic_DNA.
DR EMBL; BT024589; ABD42987.1; -; mRNA.
DR PIR; T00770; T00770.
DR RefSeq; NP_173688.1; NM_102121.3.
DR AlphaFoldDB; O04157; -.
DR SMR; O04157; -.
DR STRING; 3702.AT1G22740.1; -.
DR PaxDb; O04157; -.
DR PRIDE; O04157; -.
DR ProteomicsDB; 236341; -.
DR EnsemblPlants; AT1G22740.1; AT1G22740.1; AT1G22740.
DR GeneID; 838880; -.
DR Gramene; AT1G22740.1; AT1G22740.1; AT1G22740.
DR KEGG; ath:AT1G22740; -.
DR Araport; AT1G22740; -.
DR TAIR; locus:2199716; AT1G22740.
DR eggNOG; KOG0394; Eukaryota.
DR HOGENOM; CLU_041217_10_6_1; -.
DR InParanoid; O04157; -.
DR OMA; CENNGNI; -.
DR OrthoDB; 1172019at2759; -.
DR PhylomeDB; O04157; -.
DR PRO; PR:O04157; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O04157; baseline and differential.
DR Genevisible; O04157; AT.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; ISS:TAIR.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:UniProtKB.
DR GO; GO:0010623; P:programmed cell death involved in cell development; IMP:TAIR.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:1905177; P:tracheary element differentiation; IMP:TAIR.
DR GO; GO:0010089; P:xylem development; IMP:UniProtKB.
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; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..203
FT /note="Ras-related protein RABG3b"
FT /id="PRO_0000121280"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 15..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 63..67
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 158..159
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 203
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 201
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 203
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 22
FT /note="T->N: Dominant negative (GDP-bound form); inhibits
FT autophagy and tracheary element formation."
FT /evidence="ECO:0000269|PubMed:20659276"
FT MUTAGEN 67
FT /note="Q->L: Constitutively active (GTP bound form);
FT stimulates autophagy and tracheary element formation."
FT /evidence="ECO:0000269|PubMed:20659276"
SQ SEQUENCE 203 AA; 22945 MW; 18FAA93B2709C14A CRC64;
MSTRRRTLLK VIILGDSGVG KTSLMNQYVN NKFSQQYKAT IGADFVTKEL QIDDRLVTLQ
IWDTAGQERF QSLGVAFYRG ADCCVLVYDV NHLKSFESLD NWHNEFLTRA SPRDPMAFPF
ILLGNKVDID GGNSRVVSEK KAREWCAEKG NIVYFETSAK EDYNVDDSFL CITKLALANE
RDQDIYFQPD TGSVPEQRGG CAC
