Q9LY87 (RGLG2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
E3 ubiquitin-protein ligase RGLG2
EC=6.3.2.-

Alternative name(s):
RING domain ligase 2

Gene names

Name:	RGLG2
Ordered Locus Names:	At5g14420
ORF Names:	F18O22.210

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	468 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	E3 ubiquitin-protein ligase that mediates the formation of 'Lys-63'-linked multiubiquitin chains. Regulates apical dominance by acting on the auxin transport proteins abundance. Ref.5
Subunit structure	Interacts with the heterodimer UBC35/UEV1B, UBC35 alone, PIN1, but not with UCB2, UCB9, UEV1B or UEV1C alone. Ref.5
Subcellular location	Cell membrane; Lipid-anchor.
Tissue specificity	Ubiquitously expressed. Ref.5
Domain	A C-terminal fragment containing the RING domain interacts with UBC35 while the full-length protein does not.
Post-translational modification	N-myristoylated.
Disruption phenotype	Plants do not show any phenotype alteration due to the redundancy with RGLG1. Double mutant RGLG1-RGLG2 shows a complete loss of apical dominance. Ref.5
Sequence similarities	Contains 1 RING-type zinc finger. Contains 1 VWFA domain.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cell membrane Membrane
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Lipoprotein Myristate
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	auxin metabolic process Inferred from genetic interaction Ref.5. Source: TAIR cytokinin metabolic process Inferred from genetic interaction Ref.5. Source: TAIR
Cellular component	plasma membrane Inferred from direct assay Ref.5. Source: TAIR
Molecular function	ubiquitin-protein ligase activity Inferred from direct assay Ref.1. Source: TAIR zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Potential
	Chain	2 – 468	467	E3 ubiquitin-protein ligase RGLG2		PRO_0000344784
Regions
	Domain	122 – 342	221	VWFA
	Zinc finger	425 – 458	34	RING-type
	Compositional bias	13 – 35	23	Ser-rich
	Compositional bias	47 – 80	34	Pro-rich
	Compositional bias	366 – 415	50	Pro-rich
Amino acid modifications
	Lipidation	2	1	N-myristoyl glycine Probable
Experimental info
	Mutagenesis	2	1	G → A: Loss of myristoylation. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9LY87 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 2AC6D3FA427FD0B9	FASTA	468	51,578
	10 20 30 40 50 60 MGTGNSKENW RQSSFRSTSA SSASPSSSSW ASQQSYPQYG AESYNYPPPP SYAQPPEYTQ 70 80 90 100 110 120 PPPPLYSTQP YSAPSYSAPP SQSYGSDNKK RLERKYSKIS DDYSSLEQVT EALARAGLES 130 140 150 160 170 180 SNLIVGIDFT KSNEWTGARS FNRKSLHFIG SSPNPYEQAI TIIGRTLAAF DEDNLIPCYG 190 200 210 220 230 240 FGDASTHDQD VFSFNSEDRF CNGFEEVLSR YKEIVPQLKL AGPTSFAPII DMAMTIVEQS 250 260 270 280 290 300 GGQYHVLVII ADGQVTRSVD TENGQLSPQE QKTVDAIVQA SKLPLSIVLV GVGDGPWDMM 310 320 330 340 350 360 REFDDNIPAR AFDNFQFVNF TEIMAKNKAQ SLKETEFALS ALMEIPQQYK ATIELNLLGR 370 380 390 400 410 420 RNGYIPERFP LPPPMRGGSS SYNSPKPSRL PSFKPSVPPH PTEGYHVRSS PVPPPTSSAS 430 440 450 460 DNQLCPICLS NPKDMAFGCG HQTCCECGPD LQMCPICRAP IQTRIKLY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Functional analysis of the RING-type ubiquitin ligase family of Arabidopsis." Stone S.L., Hauksdottir H., Troy A., Herschleb J., Kraft E., Callis J. Plant Physiol. 137:13-30(2005) [PubMed: 15644464] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F. Nature 408:823-826(2000) [PubMed: 11130714] [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. , 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.
[5]	"Ubiquitin lysine 63 chain forming ligases regulate apical dominance in Arabidopsis." Yin X.-J., Volk S., Ljung K., Mehlmer N., Dolezal K., Ditengou F., Hanano S., Davis S.J., Schmelzer E., Sandberg G., Teige M., Palme K., Pickart C., Bachmair A. Plant Cell 19:1898-1911(2007) [PubMed: 17586653] [Abstract] Cited for: IDENTIFICATION, FUNCTION, TISSUE SPECIFICITY, MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2, INTERACTION WITH UBC35 AND PIN1, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Web resources

PlantsUBQ

A functional genomics database for the ubiquitin/26S proteasome proteolytic pathway in plants

Cross-references

Sequence databases
EMBL GenBank DDBJ	DQ086862 mRNA. Translation: AAZ14078.1. AL163817 Genomic DNA. Translation: CAB87781.1. CP002688 Genomic DNA. Translation: AED92028.1. CP002688 Genomic DNA. Translation: AED92029.1. CP002688 Genomic DNA. Translation: AED92030.1. CP002688 Genomic DNA. Translation: AED92031.1. AY099597 mRNA. Translation: AAM20448.1. BT000249 mRNA. Translation: AAN15568.1.
IPI	IPI00535253.
PIR	T48615.
RefSeq	NP_196946.1. NM_121446.4. NP_850818.1. NM_180487.3. NP_974779.1. NM_203050.2. NP_974780.1. NM_203051.2.
UniGene	At.5177.
3D structure databases
ProteinModelPortal	Q9LY87.
SMR	Q9LY87. Positions 423-466.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9LY87.
Proteomic databases
PRIDE	Q9LY87.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G14420.1; AT5G14420.1; AT5G14420. AT5G14420.2; AT5G14420.2; AT5G14420. AT5G14420.3; AT5G14420.3; AT5G14420. AT5G14420.4; AT5G14420.4; AT5G14420.
GeneID	831293.
GenomeReviews	Gene locus AT5G14420 in contig BA000015_GR.
KEGG	ath:AT5G14420.
NMPDR	fig|3702.1.peg.23573.
Organism-specific databases
TAIR	At5g14420.
Phylogenomic databases
GeneTree	EPGT00070000028159.
HOGENOM	HBG746179.
InParanoid	Q9LY87.
OMA	EMATTIV.
PhylomeDB	Q9LY87.
ProtClustDB	CLSN2687222.
Gene expression databases
ArrayExpress	Q9LY87.
Genevestigator	Q9LY87.
Family and domain databases
InterPro	IPR010734. Copine. IPR002035. VWF_A. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Gene3D	G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 1 hit.
Pfam	PF07002. Copine. 1 hit. [Graphical view]
SMART	SM00184. RING. 1 hit. SM00327. VWA. 1 hit. [Graphical view]
PROSITE	PS50234. VWFA. False negative. PS00518. ZF_RING_1. False negative. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RGLG2_ARATH

Accession

Primary (citable) accession number: Q9LY87

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 22, 2008
Last sequence update:	October 1, 2000
Last modified:	December 14, 2011
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program