Reviewed, UniProtKB/Swiss-Prot O80837 (REMO_ARATH)

Names and origin

Protein names

Recommended name:
    Remorin
Alternative name(s):
    DNA-binding protein

Gene names

Name:	DBP
Ordered Locus Names:	At2g45820
ORF Names:	F4I18.20

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	190 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Exhibits a non sequence-specific DNA-binding activity.
Subunit structure	May polymerize to form filamentous structures. Ref.4
Tissue specificity	Expressed in roots, leaves, stems, flowers and siliques, with a maximal expression in apical regions. Ref.1
Induction	10-fold by auxin, 2-fold by gibberellic acid and not by cytokinin. Ref.1
Post-translational modification	Phosphorylation level varies significantly during early response to general elicitors.
Sequence similarities	Belongs to the remorin family.

Ontologies

Keywords
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	plasma membrane Ref.6 Inferred from direct assay. Source: TAIR
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARR4	O82798	3	EBI-1788073,EBI-625213

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 190	190	Remorin		PRO_0000311119
Regions
	Coiled coil	92 – 147	56	Potential
Amino acid modifications
	Modified residue	14	1	Phosphoserine Ref.5 Ref.6
	Modified residue	58	1	Phosphothreonine Ref.6 Ref.7
Experimental info
	Sequence conflict	168	1	K → E in AAA57124. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O80837-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 092A817CF7E1B476	FASTA	190	20,968
	10 20 30 40 50 60 MAEEQKTSKV DVESPAVLAP AKEPTPAPVE VADEKIHNPP PVESKALAVV EKPIEEHTPK 70 80 90 100 110 120 KASSGSADRD VILADLEKEK KTSFIKAWEE SEKSKAENRA QKKISDVHAW ENSKKAAVEA 130 140 150 160 170 180 QLRKIEEKLE KKKAQYGEKM KNKVAAIHKL AEEKRAMVEA KKGEELLKAE EMGAKYRATG 190 VVPKATCGCF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"An auxin-regulated gene of Arabidopsis thaliana encodes a DNA-binding protein." Alliotte T., Tire C., Engler G., Peleman J., Caplan A., van Montagu M., Inze D. Plant Physiol. 89:743-752(1989) [PubMed: 16666616] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, INDUCTION, DNA-BINDING. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed: 10617197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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. , 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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Remorins form a novel family of coiled coil-forming oligomeric and filamentous proteins associated with apical, vascular and embryonic tissues in plants." Bariola P.A., Retelska D., Stasiak A., Kammerer R.A., Fleming A., Hijri M., Frank S., Farmer E.E. Plant Mol. Biol. 55:579-594(2004) [PubMed: 15604702] [Abstract] Cited for: SUBUNIT.
[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: 15308754] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, MASS SPECTROMETRY.
[6]	"Quantitative phosphoproteomics of early elicitor signaling in Arabidopsis." Benschop J.J., Mohammed S., O'Flaherty M., Heck A.J.R., Slijper M., Menke F.L.H. Mol. Cell. Proteomics 6:1198-1214(2007) [PubMed: 17317660] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND THR-58, MASS SPECTROMETRY.
[7]	"Temporal analysis of sucrose-induced phosphorylation changes in plasma membrane proteins of Arabidopsis." Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B., Schulze W.X. Mol. Cell. Proteomics 6:1711-1726(2007) [PubMed: 17586839] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-58, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M25268 Genomic DNA. Translation: AAA57124.1. AC004665 Genomic DNA. Translation: AAC28542.1. AY045996 mRNA. Translation: AAK76670.1. AY079329 mRNA. Translation: AAL85060.1.
IPI	IPI00539171.
PIR	T02465.
RefSeq	NP_182106.1.
UniGene	At.24530
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	O80837. 2 interactions.
Proteomic databases
PRIDE	O80837.
ProMEX	O80837.
Genome annotation databases
GeneID	819190.
GenomeReviews	Gene locus AT2G45820 in contig CT485783_GR.
KEGG	ath:AT2G45820.
NMPDR	fig|3702.1.peg.29069.
Organism-specific databases
TAIR	At2g45820.
Phylogenomic databases
OMA	O80837. RATGHAP.
Gene expression databases
ArrayExpress	O80837.
Family and domain databases
InterPro	IPR005516. Remorin_C. IPR005518. Remorin_N. [Graphical view]
Pfam	PF03763. Remorin_C. 1 hit. PF03766. Remorin_N. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

REMO_ARATH

Accession

Primary (citable) accession number: O80837
Secondary accession number(s): Q39087

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	November 1, 1998
Last modified:	July 7, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)