ID RABC1_ARATH Reviewed; 212 AA. AC O23657; Q9LP15; DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 157. DE RecName: Full=Ras-related protein RABC1; DE Short=AtRABC1; DE AltName: Full=Ras-related protein Rab18; DE Short=AtRab18; GN Name=RABC1; Synonyms=RAB18, RAB18-1; OrderedLocusNames=At1g43890; GN ORFNames=F28H19.15, F9C16.3; 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; RA Bischoff F., Palme K.; RT "A member of the Rab18-family from Arabidopsis thaliana."; RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases. 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 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 ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-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 -!- 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}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF79660.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U75603; AAB61997.1; -; mRNA. DR EMBL; AC006423; AAF63103.1; -; Genomic_DNA. DR EMBL; AC022314; AAF79660.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002684; AEE32003.1; -; Genomic_DNA. DR EMBL; CP002684; AEE32004.1; -; Genomic_DNA. DR EMBL; CP002684; AEE32005.1; -; Genomic_DNA. DR EMBL; AF370263; AAK44078.1; -; mRNA. DR EMBL; AY063080; AAL34254.1; -; mRNA. DR EMBL; AK227664; BAE99651.1; -; mRNA. DR EMBL; AY086878; AAM63924.1; -; mRNA. DR PIR; A96503; A96503. DR RefSeq; NP_001077675.1; NM_001084206.1. DR RefSeq; NP_001117435.1; NM_001123963.1. DR RefSeq; NP_175056.1; NM_103516.4. DR AlphaFoldDB; O23657; -. DR SMR; O23657; -. DR BioGRID; 26212; 1. DR IntAct; O23657; 2. DR MINT; O23657; -. DR STRING; 3702.O23657; -. DR iPTMnet; O23657; -. DR PaxDb; 3702-AT1G43890-1; -. DR ProteomicsDB; 236498; -. DR EnsemblPlants; AT1G43890.1; AT1G43890.1; AT1G43890. DR EnsemblPlants; AT1G43890.2; AT1G43890.2; AT1G43890. DR EnsemblPlants; AT1G43890.3; AT1G43890.3; AT1G43890. DR GeneID; 840987; -. DR Gramene; AT1G43890.1; AT1G43890.1; AT1G43890. DR Gramene; AT1G43890.2; AT1G43890.2; AT1G43890. DR Gramene; AT1G43890.3; AT1G43890.3; AT1G43890. DR KEGG; ath:AT1G43890; -. DR Araport; AT1G43890; -. DR TAIR; AT1G43890; RAB18. DR eggNOG; KOG0080; Eukaryota. DR HOGENOM; CLU_041217_10_1_1; -. DR InParanoid; O23657; -. DR OMA; RVHKMDV; -. DR OrthoDB; 3487147at2759; -. DR PhylomeDB; O23657; -. DR PRO; PR:O23657; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; O23657; baseline and differential. DR GO; GO:0005634; C:nucleus; HDA:TAIR. DR GO; GO:0005886; C:plasma membrane; HDA:TAIR. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR CDD; cd01863; Rab18; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR001806; Small_GTPase. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR47977; RAS-RELATED PROTEIN RAB; 1. DR PANTHER; PTHR47977:SF96; RAS-RELATED PROTEIN RABC1-LIKE; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00177; ARF; 1. DR SMART; SM00175; RAB; 1. DR SMART; SM00176; RAN; 1. DR SMART; SM00173; RAS; 1. DR SMART; SM00174; RHO; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51419; RAB; 1. DR Genevisible; O23657; AT. 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..212 FT /note="Ras-related protein RABC1" FT /id="PRO_0000407357" FT REGION 182..212 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 41..49 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 67..71 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 127..130 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 157..158 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT MOD_RES 2 FT /note="N-acetylglycine" FT /evidence="ECO:0007744|PubMed:22223895" FT LIPID 209 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000250" FT LIPID 210 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000250" SQ SEQUENCE 212 AA; 23531 MW; 042AFFE8C133612C CRC64; MGSSSGQPEF DYLFKVLLIG DSGVGKSSLL LSFTSNTFDD LSPTIGVDFK VKYLTIGEKK LKLAIWDTAG QERFRTLTSS YYRGAQGIIM VYDVTRRDTF TNLSDIWAKE IDLYSTNQDC IKMLVGNKVD KESERAVSKK EGIDFAREYG CLFLECSAKT RVNVEQCFEE LVLKILETPS LTAEGSSGGK KNIFKQNPAQ TTSTSSSYCC SS //