AXR1_ARATH
ID AXR1_ARATH Reviewed; 540 AA.
AC P42744;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 145.
DE RecName: Full=NEDD8-activating enzyme E1 regulatory subunit AXR1 {ECO:0000305};
DE AltName: Full=Auxin-resistance protein AXR1 {ECO:0000303|PubMed:8321287};
DE AltName: Full=Protein AUXIN-RESISTANT 1 {ECO:0000303|PubMed:21311953};
GN Name=AXR1 {ECO:0000303|PubMed:8321287};
GN OrderedLocusNames=At1g05180 {ECO:0000312|Araport:AT1G05180};
GN ORFNames=YUP8H12.21 {ECO:0000312|EMBL:AAB71460.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTANT AXR1-3.
RC STRAIN=cv. Columbia;
RX PubMed=8321287; DOI=10.1038/364161a0;
RA Leyser H.M.O., Lincoln C.A., Timpte C., Lammer D., Turner J., Estelle M.;
RT "Arabidopsis auxin-resistance gene AXR1 encodes a protein related to
RT ubiquitin-activating enzyme E1.";
RL Nature 364:161-164(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ECR1 AND RUB1.
RX PubMed=9624055; DOI=10.1126/science.280.5370.1760;
RA del Pozo J.C., Timpte C., Tan S., Callis J., Estelle M.;
RT "The ubiquitin-related protein RUB1 and auxin response in Arabidopsis.";
RL Science 280:1760-1763(1998).
RN [6]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11884684; DOI=10.1105/tpc.010282;
RA del Pozo J.C., Dharmasiri S., Hellmann H., Walker L., Gray W.M.,
RA Estelle M.;
RT "AXR1-ECR1-dependent conjugation of RUB1 to the Arabidopsis Cullin AtCUL1
RT is required for auxin response.";
RL Plant Cell 14:421-433(2002).
RN [7]
RP FUNCTION.
RX PubMed=12368504; DOI=10.1105/tpc.003434;
RA Schwechheimer C., Serino G., Deng X.W.;
RT "Multiple ubiquitin ligase-mediated processes require COP9 signalosome and
RT AXR1 function.";
RL Plant Cell 14:2553-2563(2002).
RN [8]
RP FUNCTION.
RX PubMed=17655650; DOI=10.1111/j.1365-313x.2007.03211.x;
RA Dharmasiri N., Dharmasiri S., Weijers D., Karunarathna N., Jurgens G.,
RA Estelle M.;
RT "AXL and AXR1 have redundant functions in RUB conjugation and growth and
RT development in Arabidopsis.";
RL Plant J. 52:114-123(2007).
RN [9]
RP FUNCTION, AND INTERACTION WITH ECR1 AND RUB1.
RX PubMed=21311953; DOI=10.1007/s11103-011-9750-8;
RA Hotton S.K., Eigenheer R.A., Castro M.F., Bostick M., Callis J.;
RT "AXR1-ECR1 and AXL1-ECR1 heterodimeric RUB-activating enzymes diverge in
RT function in Arabidopsis thaliana.";
RL Plant Mol. Biol. 75:515-526(2011).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=25116939; DOI=10.1371/journal.pbio.1001930;
RA Jahns M.T., Vezon D., Chambon A., Pereira L., Falque M., Martin O.C.,
RA Chelysheva L., Grelon M.;
RT "Crossover localisation is regulated by the neddylation posttranslational
RT regulatory pathway.";
RL PLoS Biol. 12:E1001930-E1001930(2014).
CC -!- FUNCTION: Regulatory subunit of the dimeric ECR1-AXR1 E1 enzyme. E1
CC activates RUB1/NEDD8 by first adenylating its C-terminal glycine
CC residue with ATP, thereafter linking this residue to the side chain of
CC the catalytic cysteine, yielding a RUB1-ECR1 thioester and free AMP. E1
CC finally transfers RUB1 to the catalytic cysteine of RCE1. Plays an
CC important role in auxin response (PubMed:8321287). Regulates the
CC chromosomal localization of meiotic recombination by crossovers (COs)
CC and subsequent synapsis, probably through the activation of a CRL4
CC complex (PubMed:25116939). Required for E3-mediated protein degradation
CC in response to auxin, jasmonic acid and cold stress. Required for the
CC COP1-COP10-CSN-mediated repression of photomorphogenesis in the dark
CC (PubMed:12368504). May function redundantly with AXL1 in the RUB
CC conjugating pathway (PubMed:17655650). Seems not to be functionally
CC equivalent to AXL1 in vivo (PubMed:21311953).
CC {ECO:0000269|PubMed:12368504, ECO:0000269|PubMed:17655650,
CC ECO:0000269|PubMed:21311953, ECO:0000269|PubMed:25116939,
CC ECO:0000269|PubMed:8321287}.
CC -!- PATHWAY: Protein modification; protein neddylation.
CC -!- SUBUNIT: Heterodimer of ECR1 and AXR1. The complex binds to RUB1/NEDD8
CC and RCE1. {ECO:0000269|PubMed:21311953, ECO:0000269|PubMed:9624055}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9624055}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P42744-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in shoot, root and floral meristems, in
CC vascular tissues of cotyledons and mature leaves, and in the stele of
CC the root. Expressed at higher levels on the lower side of an emerging
CC root during germination and at higher levels on the underside of the
CC apical hook. {ECO:0000269|PubMed:11884684}.
CC -!- DEVELOPMENTAL STAGE: Expressed during ovules and embryo development and
CC very early during the formation of lateral roots.
CC {ECO:0000269|PubMed:11884684}.
CC -!- DISRUPTION PHENOTYPE: Impaired meiotic recombination characterized by a
CC shortage in bivalent formation due to a mislocalization of class I
CC crossovers (COs) and correlated with strong synapsis defects. Dwarf
CC plants, highly branched, with small crinkled leaves, small flowers and
CC short fruits, symptoms of fertility defects.
CC {ECO:0000269|PubMed:25116939}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. ULA1
CC subfamily. {ECO:0000305}.
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DR EMBL; L13922; AAB59348.1; -; mRNA.
DR EMBL; AC000098; AAB71460.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27800.1; -; Genomic_DNA.
DR EMBL; AY050379; AAK91397.1; -; mRNA.
DR PIR; S35071; S35071.
DR RefSeq; NP_172010.1; NM_100396.4. [P42744-1]
DR AlphaFoldDB; P42744; -.
DR SMR; P42744; -.
DR BioGRID; 24521; 10.
DR IntAct; P42744; 1.
DR STRING; 3702.AT1G05180.1; -.
DR iPTMnet; P42744; -.
DR PaxDb; P42744; -.
DR PRIDE; P42744; -.
DR ProteomicsDB; 240941; -. [P42744-1]
DR EnsemblPlants; AT1G05180.1; AT1G05180.1; AT1G05180. [P42744-1]
DR GeneID; 839286; -.
DR Gramene; AT1G05180.1; AT1G05180.1; AT1G05180. [P42744-1]
DR KEGG; ath:AT1G05180; -.
DR Araport; AT1G05180; -.
DR TAIR; locus:2207220; AT1G05180.
DR eggNOG; KOG2016; Eukaryota.
DR HOGENOM; CLU_019618_2_1_1; -.
DR InParanoid; P42744; -.
DR OMA; LHEICRY; -.
DR PhylomeDB; P42744; -.
DR UniPathway; UPA00885; -.
DR PRO; PR:P42744; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P42744; baseline and differential.
DR Genevisible; P42744; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019781; F:NEDD8 activating enzyme activity; IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0010252; P:auxin homeostasis; NAS:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IMP:TAIR.
DR GO; GO:0006281; P:DNA repair; IMP:TAIR.
DR GO; GO:0009965; P:leaf morphogenesis; IGI:TAIR.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0045116; P:protein neddylation; IBA:GO_Central.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:UniProtKB.
DR GO; GO:0009735; P:response to cytokinin; IGI:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR InterPro; IPR030667; APP-BP1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR Pfam; PF00899; ThiF; 1.
DR PIRSF; PIRSF039099; APP-BP1; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Auxin signaling pathway; Nucleotide-binding; Nucleus;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..540
FT /note="NEDD8-activating enzyme E1 regulatory subunit AXR1"
FT /id="PRO_0000194960"
FT MUTAGEN 154
FT /note="C->Y: In axr1-3; auxin-resistant."
FT /evidence="ECO:0000269|PubMed:8321287"
SQ SEQUENCE 540 AA; 60035 MW; 9CD0091114654B06 CRC64;
MQAVKRSRRH VEEEPTMVEP KTKYDRQLRI WGEVGQAALE EASICLLNCG PTGSEALKNL
VLGGVGSITV VDGSKVQFGD LGNNFMVDAK SVGQSKAKSV CAFLQELNDS VNAKFIEENP
DTLITTNPSF FSQFTLVIAT QLVEDSMLKL DRICRDANVK LVLVRSYGLA GFVRISVKEH
PIIDSKPDHF LDDLRLNNPW PELKSFVETI DLNVSEPAAA HKHIPYVVIL VKMAEEWAQS
HSGNLPSTRE EKKEFKDLVK SKMVSTDEDN YKEAIEAAFK VFAPRGISSE VQKLINDSCA
EVNSNSSAFW VMVAALKEFV LNEGGGEAPL EGSIPDMTSS TEHYINLQKI YLAKAEADFL
VIEERVKNIL KKIGRDPSSI PKPTIKSFCK NARKLKLCRY RMVEDEFRNP SVTEIQKYLA
DEDYSGAMGF YILLRAADRF AANYNKFPGQ FDGGMDEDIS RLKTTALSLL TDLGCNGSVL
PDDLIHEMCR FGASEIHVVS AFVGGIASQE VIKLVTKQFV PMLGTYIFNG IDHKSQLLKL
