Reviewed, UniProtKB/Swiss-Prot P42744 (ULA1_ARATH)

Names and origin

Protein names

Recommended name:
    NEDD8-activating enzyme E1 regulatory subunit
Alternative name(s):
    Auxin-resistance protein AXR1

Gene names

Name:	AXR1
Ordered Locus Names:	At1g05180
ORF Names:	YUP8H12.21

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

General annotation (Comments)

Function	Regulatory subunit of the dimeric ECR1-AXR1 E1 enzyme. E1 activates NEDD8/RUB1 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-ECR1 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of RCE1. Plays an important role in auxin response. Ref.1
Pathway	Protein modification; protein neddylation.
Subunit structure	Heterodimer of ECR1 and AXR1. The complex binds NEDD8 and RCE1.
Subcellular location	Nucleus. Ref.4
Tissue specificity	Expressed in shoot, root and floral meristems, in vascular tissues of cotyledons and mature leaves, and in the stele of the root. Expressed at higher levels on the lower side of an emerging root during germination and at higher levels on the underside of the apical hook. Ref.5
Developmental stage	Expressed during ovules and embryo development and very early during the formation of lateral roots. Ref.5
Sequence similarities	Belongs to the ubiquitin-activating E1 family. ULA1 subfamily.

Ontologies

Keywords
Biological process	Auxin signaling pathway Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from mutant phenotype. Source: TAIR auxin homeostasis Non-traceable author statement. Source: TAIR auxin mediated signaling pathway Inferred from mutant phenotype. Source: TAIR leaf morphogenesis Inferred from genetic interaction. Source: TAIR modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW protein ubiquitination Inferred from genetic interaction. Source: TAIR response to water deprivation Inferred from mutant phenotype. Source: TAIR
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW catalytic activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RCE1	Q9SDY5	1	EBI-595161,EBI-595116

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: P42744-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 540	540	NEDD8-activating enzyme E1 regulatory subunit		PRO_0000194960
Regions
	Nucleotide binding	51 – 75	25	ATP By similarity
Sites
	Active site	154	1	Glycyl thioester intermediate Probable
Experimental info
	Mutagenesis	154	1	C → Y in axr1-3; auxin-resistant.

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 9CD0091114654B06	FASTA	540	60,035
	10 20 30 40 50 60 MQAVKRSRRH VEEEPTMVEP KTKYDRQLRI WGEVGQAALE EASICLLNCG PTGSEALKNL 70 80 90 100 110 120 VLGGVGSITV VDGSKVQFGD LGNNFMVDAK SVGQSKAKSV CAFLQELNDS VNAKFIEENP 130 140 150 160 170 180 DTLITTNPSF FSQFTLVIAT QLVEDSMLKL DRICRDANVK LVLVRSYGLA GFVRISVKEH 190 200 210 220 230 240 PIIDSKPDHF LDDLRLNNPW PELKSFVETI DLNVSEPAAA HKHIPYVVIL VKMAEEWAQS 250 260 270 280 290 300 HSGNLPSTRE EKKEFKDLVK SKMVSTDEDN YKEAIEAAFK VFAPRGISSE VQKLINDSCA 310 320 330 340 350 360 EVNSNSSAFW VMVAALKEFV LNEGGGEAPL EGSIPDMTSS TEHYINLQKI YLAKAEADFL 370 380 390 400 410 420 VIEERVKNIL KKIGRDPSSI PKPTIKSFCK NARKLKLCRY RMVEDEFRNP SVTEIQKYLA 430 440 450 460 470 480 DEDYSGAMGF YILLRAADRF AANYNKFPGQ FDGGMDEDIS RLKTTALSLL TDLGCNGSVL 490 500 510 520 530 540 PDDLIHEMCR FGASEIHVVS AFVGGIASQE VIKLVTKQFV PMLGTYIFNG IDHKSQLLKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Arabidopsis auxin-resistance gene AXR1 encodes a protein related to ubiquitin-activating enzyme E1." Leyser H.M.O., Lincoln C.A., Timpte C., Lammer D., Turner J., Estelle M. Nature 364:161-164(1993) [PubMed: 8321287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTANT AXR1-3. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [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]	"The ubiquitin-related protein RUB1 and auxin response in Arabidopsis." del Pozo J.C., Timpte C., Tan S., Callis J., Estelle M. Science 280:1760-1763(1998) [PubMed: 9624055] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ECR1 AND RUB1.
[5]	"AXR1-ECR1-dependent conjugation of RUB1 to the Arabidopsis Cullin AtCUL1 is required for auxin response." del Pozo J.C., Dharmasiri S., Hellmann H., Walker L., Gray W.M., Estelle M. Plant Cell 14:421-433(2002) [PubMed: 11884684] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L13922 mRNA. Translation: AAB59348.1. AC000098 Genomic DNA. Translation: AAB71460.1. AY050379 mRNA. Translation: AAK91397.1.
IPI	IPI00532206.
PIR	S35071.
RefSeq	NP_172010.1.
UniGene	At.10217
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P42744. 1 interaction.
Proteomic databases
PRIDE	P42744.
Genome annotation databases
GeneID	839286.
GenomeReviews	Gene locus AT1G05180 in contig CT485782_GR.
NMPDR	fig|3702.1.peg.672.
Organism-specific databases
TAIR	At1g05180.
Phylogenomic databases
OMA	P42744. KICLINA.
Gene expression databases
ArrayExpress	P42744.
Family and domain databases
InterPro	IPR016040. NAD(P)-bd_dom. IPR000594. ThiF_NAD_FAD_bd. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF00899. ThiF. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ULA1_ARATH

Accession

Primary (citable) accession number: P42744

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)