RAF2A_ARATH
ID RAF2A_ARATH Reviewed; 200 AA.
AC P31582;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Ras-related protein RABF2a;
DE Short=AtRABF2a;
DE AltName: Full=Ras-related protein Rab5A;
DE Short=AtRab5A;
DE AltName: Full=Ras-related protein Rha1;
GN Name=RABF2A; Synonyms=RAB5A, RHA1; OrderedLocusNames=At5g45130;
GN ORFNames=K17O22.15;
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 TISSUE=Flower;
RX PubMed=1844882; DOI=10.1111/j.1365-313x.1991.00167.x;
RA Anuntalabhochai S., Terryn N., van Montagu M., Inze D.;
RT "Molecular characterization of an Arabidopsis thaliana cDNA encoding a
RT small GTP-binding protein, Rha1.";
RL Plant J. 1:167-174(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. C24;
RX PubMed=8305870; DOI=10.2307/3869692;
RA Terryn N., Arias M.B., Engler G., Tire C., Villarroel R., van Montagu M.,
RA Inze D.;
RT "rha1, a gene encoding a small GTP binding protein from Arabidopsis, is
RT expressed primarily in developing guard cells.";
RL Plant Cell 5:1761-1769(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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;
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-24; THR-42 AND
RP 198-CYS-CYS-199.
RX PubMed=12724533; DOI=10.1105/tpc.009779;
RA Sohn E.J., Kim E.S., Zhao M., Kim S.J., Kim H., Kim Y.W., Lee Y.J.,
RA Hillmer S., Sohn U., Jiang L., Hwang I.;
RT "Rha1, an Arabidopsis Rab5 homolog, plays a critical role in the vacuolar
RT trafficking of soluble cargo proteins.";
RL Plant Cell 15:1057-1070(2003).
RN [7]
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 [8]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-24; THR-42; GLN-69 AND
RP 198-CYS-CYS-199.
RX PubMed=15509844; DOI=10.1093/pcp/pch142;
RA Lee G.J., Sohn E.J., Lee M.H., Hwang I.;
RT "The Arabidopsis rab5 homologs rha1 and ara7 localize to the prevacuolar
RT compartment.";
RL Plant Cell Physiol. 45:1211-1220(2004).
RN [9]
RP INTERACTION WITH VPS9A, INDUCTION, AND MUTAGENESIS OF SER-24; GLN-69 AND
RP ASN-123.
RX PubMed=18055610; DOI=10.1105/tpc.107.053876;
RA Goh T., Uchida W., Arakawa S., Ito E., Dainobu T., Ebine K., Takeuchi M.,
RA Sato K., Ueda T., Nakano A.;
RT "VPS9a, the common activator for two distinct types of Rab5 GTPases, is
RT essential for the development of Arabidopsis thaliana.";
RL Plant Cell 19:3504-3515(2007).
RN [10]
RP DEVELOPMENTAL STAGE.
RX PubMed=18775970; DOI=10.1104/pp.108.126375;
RA Wang Y., Zhang W.Z., Song L.F., Zou J.J., Su Z., Wu W.H.;
RT "Transcriptome analyses show changes in gene expression to accompany pollen
RT germination and tube growth in Arabidopsis.";
RL Plant Physiol. 148:1201-1211(2008).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF SER-24.
RX PubMed=21899678; DOI=10.1111/j.1600-0854.2011.01276.x;
RA Jung C., Lee G.J., Jang M., Lee M., Lee J., Kang H., Sohn E.J., Hwang I.;
RT "Identification of sorting motifs of AtbetaFruct4 for trafficking from the
RT ER to the vacuole through the Golgi and PVC.";
RL Traffic 12:1774-1792(2011).
RN [12]
RP FUNCTION, INTERACTION WITH EREX, AND MUTAGENESIS OF SER-24.
RX PubMed=27288222; DOI=10.1105/tpc.16.00326;
RA Sakurai H.T., Inoue T., Nakano A., Ueda T.;
RT "ENDOSOMAL RAB EFFECTOR WITH PX-DOMAIN, an interacting partner of RAB5
RT GTPases, regulates membrane trafficking to protein storage vacuoles in
RT Arabidopsis.";
RL Plant Cell 28:1490-1503(2016).
RN [13]
RP INTERACTION WITH VPS3.
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: Involved in the trafficking of soluble cargo proteins from
CC the prevacuolar compartment to the central vacuole (PubMed:12724533,
CC PubMed:21899678). Involved in vacuolar transport of storage proteins
CC with EREX as effector. Regulates membrane trafficking to protein
CC storage vacuoles (PSVs). {ECO:0000269|PubMed:12724533,
CC ECO:0000269|PubMed:21899678}.
CC -!- SUBUNIT: Interacts with VPS9A (PubMed:18055610). Interacts with EREX
CC (via PX domain) (PubMed:27288222). Binds to VPS3 (PubMed:29463724).
CC {ECO:0000269|PubMed:18055610, ECO:0000269|PubMed:27288222,
CC ECO:0000269|PubMed:29463724}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:12724533,
CC ECO:0000269|PubMed:15509844}; Lipid-anchor
CC {ECO:0000305|PubMed:12724533, ECO:0000305|PubMed:15509844}. Prevacuolar
CC compartment membrane {ECO:0000269|PubMed:12724533,
CC ECO:0000269|PubMed:15509844}; Lipid-anchor {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: High in stem, root, and inflorescence.
CC -!- DEVELOPMENTAL STAGE: Expressed during pollen germination and pollen
CC tube growth. {ECO:0000269|PubMed:18775970}.
CC -!- INDUCTION: Activated by VPS9A. {ECO:0000269|PubMed:18055610}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; X59152; CAA41863.1; -; mRNA.
DR EMBL; Z22958; CAA80534.1; -; Genomic_DNA.
DR EMBL; AB019224; BAB09498.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95208.1; -; Genomic_DNA.
DR EMBL; AF389298; AAK63870.1; -; mRNA.
DR EMBL; AY097362; AAM19878.1; -; mRNA.
DR PIR; S23727; S23727.
DR RefSeq; NP_199326.1; NM_123881.4.
DR AlphaFoldDB; P31582; -.
DR SMR; P31582; -.
DR BioGRID; 19798; 9.
DR IntAct; P31582; 12.
DR STRING; 3702.AT5G45130.1; -.
DR PaxDb; P31582; -.
DR PRIDE; P31582; -.
DR ProteomicsDB; 236628; -.
DR EnsemblPlants; AT5G45130.1; AT5G45130.1; AT5G45130.
DR GeneID; 834549; -.
DR Gramene; AT5G45130.1; AT5G45130.1; AT5G45130.
DR KEGG; ath:AT5G45130; -.
DR Araport; AT5G45130; -.
DR TAIR; locus:2153202; AT5G45130.
DR eggNOG; KOG0092; Eukaryota.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; P31582; -.
DR OMA; AVHFDIW; -.
DR PhylomeDB; P31582; -.
DR PRO; PR:P31582; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P31582; baseline and differential.
DR Genevisible; P31582; AT.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005774; C:vacuolar membrane; IMP:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:TAIR.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0007034; P:vacuolar transport; 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 Endosome; GTP-binding; Lipoprotein; Membrane; Nucleotide-binding;
KW Prenylation; Protein transport; Reference proteome; Transport.
FT CHAIN 1..200
FT /note="Ras-related protein RABF2a"
FT /id="PRO_0000121277"
FT MOTIF 39..47
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 17..25
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9SN68"
FT BINDING 65..69
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9SN68"
FT BINDING 123..126
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9SN68"
FT BINDING 153..154
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9SN68"
FT LIPID 198
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 199
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 24
FT /note="S->N: Dominant negative (GDP-bound form); loss of
FT targeting to the prevacuolar compartment. Inhibits vacuolar
FT trafficking. No effect on the interaction with VPS9A. Loss
FT of interaction with EREX."
FT /evidence="ECO:0000269|PubMed:12724533,
FT ECO:0000269|PubMed:15509844, ECO:0000269|PubMed:18055610,
FT ECO:0000269|PubMed:21899678, ECO:0000269|PubMed:27288222"
FT MUTAGEN 42
FT /note="T->A: Loss of targeting to the prevacuolar
FT compartment, but no effect on the vacuolar trafficking."
FT /evidence="ECO:0000269|PubMed:12724533,
FT ECO:0000269|PubMed:15509844"
FT MUTAGEN 69
FT /note="Q->L: Constitutively active (GTP-bound form); no
FT effect on the targeting to the prevacuolar compartment.
FT Loss of interaction with VPS9A."
FT /evidence="ECO:0000269|PubMed:15509844,
FT ECO:0000269|PubMed:18055610"
FT MUTAGEN 123
FT /note="N->I: Blocks nucleotide binding; no effect on the
FT interaction with VPS9A."
FT /evidence="ECO:0000269|PubMed:18055610"
FT MUTAGEN 198..199
FT /note="CC->SS: Loss of targeting to the prevacuolar
FT compartment, but no effect on the vacuolar trafficking."
FT /evidence="ECO:0000269|PubMed:12724533,
FT ECO:0000269|PubMed:15509844"
SQ SEQUENCE 200 AA; 21654 MW; 98E2ED559A59DE35 CRC64;
MASSGNKNIN AKLVLLGDVG AGKSSLVLRF VKDQFVEFQE STIGAAFFSQ TLAVNDATVK
FEIWDTAGQE RYHSLAPMYY RGAAAAIIVF DITNQASFER AKKWVQELQA QGNPNMVMAL
AGNKADLLDA RKVSAEEAEI YAQENSLFFM ETSAKTATNV KDIFYEIAKR LPRVQPAENP
TGMVLPNGPG ATAVSSSCCA
