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Q9SMQ6 (RAA4B_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein RABA4b

Short name=AtRABA4b
Alternative name(s):
Ras-related protein GB3
Short name=AtGB3
Ras-related protein Rab11G
Short name=AtRab11G
Gene names
Name:RABA4B
Synonyms:GB3, RAB11G
Ordered Locus Names:At4g39990
ORF Names:T5J17.160
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length224 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulator of membrane trafficking. May be required for secretion of cell wall components in cells.

Subcellular location

Early endosome membrane. Golgi apparatustrans-Golgi network membrane; Lipid-anchor Probable Ref.8.

Tissue specificity

Expressed in roots, stems, leaves and flowers. Expressed in tips of growing root hair cells. Ref.7

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 224223Ras-related protein RABA4b
PRO_0000407345

Regions

Nucleotide binding24 – 318GTP By similarity
Nucleotide binding72 – 765GTP By similarity
Nucleotide binding130 – 1334GTP By similarity
Nucleotide binding160 – 1612GTP By similarity
Motif46 – 549Effector region By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.9
Lipidation2201S-geranylgeranyl cysteine By similarity
Lipidation2211S-geranylgeranyl cysteine By similarity

Experimental info

Sequence conflict1911G → C in AAA87884. Ref.1
Sequence conflict2081G → A in AAM66946. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9SMQ6 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: FA2C5E5A0DC2025B

FASTA22424,407
        10         20         30         40         50         60 
MAGGGGYGGA SGKVDYVFKV VLIGDSAVGK SQLLARFARD EFSMDSKATI GVEFQTRTLS 

        70         80         90        100        110        120 
IEQKSIKAQI WDTAGQERYR AVTSAYYRGA VGAMLVYDMT KRETFEHIPR WLEELRAHAD 

       130        140        150        160        170        180 
KNIVIILIGN KSDLEDQRAV PTEDAKEFAE KEGLFFLETS ALNATNVENS FNTLMTQIYN 

       190        200        210        220 
TVNKKNLASE GDSNNPGSLA GKKILIPGSG QEIPAKTSTC CTSS 

« Hide

References

« Hide 'large scale' references
[1]"Identification and isoprenylation of plant GTP-binding proteins."
Biermann B.J., Randall S.K., Crowell D.N.
Plant Mol. Biol. 31:1021-1028(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Analysis of the small GTPase gene superfamily of Arabidopsis."
Vernoud V., Horton A.C., Yang Z., Nielsen E.
Plant Physiol. 131:1191-1208(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[7]"The Arabidopsis Rab GTPase RabA4b localizes to the tips of growing root hair cells."
Preuss M.L., Serna J., Falbel T.G., Bednarek S.Y., Nielsen E.
Plant Cell 16:1589-1603(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[8]"Electron tomography of RabA4b- and PI-4K?1-labeled trans Golgi network compartments in Arabidopsis."
Kang B.H., Nielsen E., Preuss M.L., Mastronarde D., Staehelin L.A.
Traffic 12:313-329(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U46926 mRNA. Translation: AAA87884.1.
AL035708 Genomic DNA. Translation: CAB38912.1.
AL161596 Genomic DNA. Translation: CAB80662.1.
CP002687 Genomic DNA. Translation: AEE87150.1.
AY072448 mRNA. Translation: AAL62440.1.
AY128914 mRNA. Translation: AAM91314.1.
AY088624 mRNA. Translation: AAM66946.1.
PIRT06105.
RefSeqNP_195709.1. NM_120163.4.
UniGeneAt.1649.
At.48966.

3D structure databases

ProteinModelPortalQ9SMQ6.
SMRQ9SMQ6. Positions 15-179.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid15440. 1 interaction.
IntActQ9SMQ6. 1 interaction.
STRING3702.AT4G39990.1-P.

Proteomic databases

PaxDbQ9SMQ6.
PRIDEQ9SMQ6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G39990.1; AT4G39990.1; AT4G39990.
GeneID830160.
KEGGath:AT4G39990.

Organism-specific databases

TAIRAT4G39990.

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
InParanoidQ9SMQ6.
OMAFEHIPRW.
PhylomeDBQ9SMQ6.

Gene expression databases

GenevestigatorQ9SMQ6.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRAA4B_ARATH
AccessionPrimary (citable) accession number: Q9SMQ6
Secondary accession number(s): Q38923, Q8L958
Entry history
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names