RAH1B_ARATH
ID RAH1B_ARATH Reviewed; 208 AA.
AC O80501;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Ras-related protein RABH1b;
DE Short=AtRABH1b;
DE AltName: Full=Ras-related protein Rab6A;
DE Short=AtRab6A;
GN Name=RABH1B; Synonyms=RAB6A; OrderedLocusNames=At2g44610;
GN ORFNames=F16B22.10;
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], MUTAGENESIS OF ASN-122 AND 206-CYS--CYS-208,
RP AND TISSUE SPECIFICITY.
RX PubMed=8159788; DOI=10.1104/pp.104.2.591;
RA Bednarek S.Y., Reynolds T.L., Schroeder M., Grabowski R., Hengst L.,
RA Gallwitz D., Raikhel N.V.;
RT "A small GTP-binding protein from Arabidopsis thaliana functionally
RT complements the yeast YPT6 null mutant.";
RL Plant Physiol. 104:591-596(1994).
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;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [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 INTERACTION WITH GC5.
RX PubMed=18182439; DOI=10.1093/jxb/erm304;
RA Latijnhouwers M., Gillespie T., Boevink P., Kriechbaumer V., Hawes C.,
RA Carvalho C.M.;
RT "Localization and domain characterization of Arabidopsis golgin
RT candidates.";
RL J. Exp. Bot. 58:4373-4386(2007).
RN [9]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-23; GLN-68; ASN-122; CYS-206
RP AND CYS-208.
RX PubMed=19454595; DOI=10.1093/jxb/erp153;
RA Johansen J.N., Chow C.M., Moore I., Hawes C.;
RT "AtRAB-H1b and AtRAB-H1c GTPases, homologues of the yeast Ypt6, target
RT reporter proteins to the Golgi when expressed in Nicotiana tabacum and
RT Arabidopsis thaliana.";
RL J. Exp. Bot. 60:3179-3193(2009).
CC -!- FUNCTION: Protein transport. Regulator of membrane traffic from the
CC Golgi apparatus towards the endoplasmic reticulum (ER). Binds GTP and
CC GDP and possesses intrinsic GTPase activity (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the C-terminus of GC5, but not with GC3.
CC {ECO:0000269|PubMed:18182439}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000305|PubMed:19454595}; Lipid-anchor
CC {ECO:0000305|PubMed:19454595}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:19454595}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves and flowers.
CC {ECO:0000269|PubMed:8159788}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AC003672; AAC27463.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10447.1; -; Genomic_DNA.
DR EMBL; BT025780; ABF83670.1; -; mRNA.
DR EMBL; AK226988; BAE99055.1; -; mRNA.
DR EMBL; AY087904; AAM65455.1; -; mRNA.
DR PIR; T01588; T01588.
DR RefSeq; NP_181989.1; NM_130025.5.
DR AlphaFoldDB; O80501; -.
DR SMR; O80501; -.
DR BioGRID; 4405; 4.
DR STRING; 3702.AT2G44610.1; -.
DR iPTMnet; O80501; -.
DR PaxDb; O80501; -.
DR PRIDE; O80501; -.
DR ProteomicsDB; 234994; -.
DR EnsemblPlants; AT2G44610.1; AT2G44610.1; AT2G44610.
DR GeneID; 819069; -.
DR Gramene; AT2G44610.1; AT2G44610.1; AT2G44610.
DR KEGG; ath:AT2G44610; -.
DR Araport; AT2G44610; -.
DR TAIR; locus:2042321; AT2G44610.
DR eggNOG; KOG0094; Eukaryota.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; O80501; -.
DR OMA; PVSNDGC; -.
DR OrthoDB; 1277051at2759; -.
DR PhylomeDB; O80501; -.
DR PRO; PR:O80501; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80501; baseline and differential.
DR Genevisible; O80501; AT.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0006887; P:exocytosis; IMP:TAIR.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0052324; P:plant-type cell wall cellulose biosynthetic process; IMP:TAIR.
DR GO; GO:0001558; P:regulation of cell growth; IMP:TAIR.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; 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 Cytoplasm; ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein;
KW Membrane; Methylation; Nucleotide-binding; Prenylation; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..208
FT /note="Ras-related protein RABH1b"
FT /id="PRO_0000348542"
FT MOTIF 38..46
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 16..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 64..68
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 122..125
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 152..153
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 208
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 206
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 208
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 23
FT /note="T->N: Loss of GTP-binding activity. No effect on
FT targeting to Golgi."
FT /evidence="ECO:0000269|PubMed:19454595"
FT MUTAGEN 68
FT /note="Q->L: No effect on GTP-binding activity and
FT targeting to Golgi."
FT /evidence="ECO:0000269|PubMed:19454595"
FT MUTAGEN 122
FT /note="N->I: Loss of GTP-binding activity and targeting to
FT Golgi. Loss of GTP-binding activity; when associated with
FT 206-C--C-208 Del."
FT /evidence="ECO:0000269|PubMed:19454595,
FT ECO:0000269|PubMed:8159788"
FT MUTAGEN 206..208
FT /note="Missing: No effect on GTP-binding activity. Loss of
FT GTP-binding activity; when associated with I-122."
FT /evidence="ECO:0000269|PubMed:8159788"
FT MUTAGEN 206
FT /note="C->S: Loss of targeting to Golgi; when associated
FT with S-208."
FT /evidence="ECO:0000269|PubMed:19454595"
FT MUTAGEN 208
FT /note="C->S: Loss of targeting to Golgi; when associated
FT with S-206."
FT /evidence="ECO:0000269|PubMed:19454595"
SQ SEQUENCE 208 AA; 23130 MW; CD0EC2862AC7D0B7 CRC64;
MAPVSALAKY KLVFLGDQSV GKTSIITRFM YDKFDNTYQA TIGIDFLSKT MYLEDRTVRL
QLWDTAGQER FRSLIPSYIR DSSVAVIVYD VASRQSFLNT TKWIDEVRTE RGSDVIVVLV
GNKTDLVDKR QVSIEEAEAK ARELNVMFIE TSAKAGFNIK ALFRKIAAAL PGMETLSSTK
QEDMVDVNLK SSNANASLAQ QQSGGCSC
