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Q9FFS0 (RTNLD_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Reticulon-like protein B4
Short name=AtRTNLB4
Alternative name(s):
VirB2-interacting protein 3
Gene names
Name:RTNLB4
Synonyms:BTI3
Ordered Locus Names:At5g41600
ORF Names:MBK23.13
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length257 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in the Agrobacterium-mediated plant transformation via its interaction with VirB2, the major component of the T-pilus. Ref.6

Subunit structure

Interacts with VirB2. Ref.6

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.7.

Sequence similarities

Contains 1 reticulon domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 257257Reticulon-like protein B4
PRO_0000371285

Regions

Transmembrane78 – 9821Helical; Potential
Transmembrane99 – 11921Helical; Potential
Transmembrane173 – 19321Helical; Potential
Domain68 – 257190Reticulon
Compositional bias25 – 4723Ser-rich

Amino acid modifications

Modified residue261Phosphoserine Ref.4
Modified residue271Phosphoserine Ref.4
Modified residue291Phosphoserine Ref.4
Modified residue311Phosphoserine Ref.4 Ref.5
Modified residue2451Phosphoserine Ref.8

Sequences

Sequence LengthMass (Da)Tools
Q9FFS0 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 29B47FB77C64DB04

FASTA25728,949
        10         20         30         40         50         60 
MVEDHKHEES ILEKIVEKIH GHGDSSSLSD SDDDKKSTSS SSSSFKSKIY RLFGREKPVH 

        70         80         90        100        110        120 
KVLGGGKPAD IFLWRNKKVS GGVLGAVTAS WVLFELFEYH LLAFLCHFAI FALAALFLWS 

       130        140        150        160        170        180 
NACTFIHKST PHIPEVHIPE DPILQLVSGL RIEINRGLTL LRNIASGKDV KKFILVIAGL 

       190        200        210        220        230        240 
WVLSIIGSCY NFLTLFYTAT VLLFTIPVLY EKYEDKVDAY GEKAMREIKK QYAVLDEKVL 

       250 
RKVISKIPRG ALNKKKD

« Hide

References

« Hide 'large scale' references
[1]"Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence features of the 1.6 Mb regions covered by twenty physically assigned P1 clones."
Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., Miyajima N., Tabata S.
DNA Res. 4:215-230(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"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.
[4]"Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry."
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.
Mol. Cell. Proteomics 2:1234-1243(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-27; SER-29 AND SER-31, MASS SPECTROMETRY.
Strain: cv. La-0.
[5]"Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database."
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.
Plant Cell 16:2394-2405(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, MASS SPECTROMETRY.
[6]"Plant proteins that interact with VirB2, the Agrobacterium tumefaciens pilin protein, mediate plant transformation."
Hwang H.-H., Gelvin S.B.
Plant Cell 16:3148-3167(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH VIRB2.
[7]"Reticulon-like proteins in Arabidopsis thaliana: structural organization and ER localization."
Nziengui H., Bouhidel K., Pillon D., Der C., Marty F., Schoefs B.
FEBS Lett. 581:3356-3362(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE, SUBCELLULAR LOCATION.
[8]"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, MASS SPECTROMETRY.
Strain: cv. Columbia.
Tissue: Seedling.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB005233 Genomic DNA. Translation: BAB11466.1.
CP002688 Genomic DNA. Translation: AED94696.1.
AY035169 mRNA. Translation: AAK59673.1.
AY057638 mRNA. Translation: AAL15269.1.
AY150449 mRNA. Translation: AAN12890.1.
IPIIPI00523388.
RefSeqNP_198975.1. NM_123524.3.
UniGeneAt.8344.

3D structure databases

ProteinModelPortalQ9FFS0.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9FFS0. 36 interactions.
STRING3702.AT5G41600.1-P.

Proteomic databases

PaxDbQ9FFS0.
PRIDEQ9FFS0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G41600.1; AT5G41600.1; AT5G41600.
GeneID834162.
KEGGath:AT5G41600.

Organism-specific databases

TAIRAt5g41600.

Phylogenomic databases

eggNOGNOG303514.
HOGENOMHOG000237479.
InParanoidQ9FFS0.
OMAVMWLLTY.
PhylomeDBQ9FFS0.
ProtClustDBCLSN2682625.

Gene expression databases

GenevestigatorQ9FFS0.

Family and domain databases

InterProIPR003388. Reticulon.
[Graphical view]
PANTHERPTHR10994. PTHR10994. 1 hit.
PfamPF02453. Reticulon. 1 hit.
[Graphical view]
PROSITEPS50845. RETICULON. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRTNLD_ARATH
AccessionPrimary (citable) accession number: Q9FFS0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: March 1, 2001
Last modified: May 1, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents