ID   AXL1_ARATH              Reviewed;         523 AA.
AC   Q9ZV69;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 138.
DE   RecName: Full=NEDD8-activating enzyme E1 regulatory subunit AXL {ECO:0000305};
DE   AltName: Full=Protein AXR1-LIKE {ECO:0000303|PubMed:17655650};
DE   AltName: Full=Protein AXR1-LIKE 1 {ECO:0000303|PubMed:17655650};
GN   Name=AXL1 {ECO:0000303|PubMed:17655650};
GN   Synonyms=AXL {ECO:0000303|PubMed:17655650};
GN   OrderedLocusNames=At2g32410 {ECO:0000312|Araport:AT2G32410};
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
RN   [4]
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   [5]
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).
CC   -!- FUNCTION: Regulatory subunit of the dimeric ECR1-AXL1 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 (Probable).
CC       May function redundantly with AXR1 in the RUB conjugating pathway
CC       (PubMed:17655650). Seems not to be functionally equivalent to AXR1 in
CC       vivo (PubMed:21311953). {ECO:0000269|PubMed:17655650,
CC       ECO:0000269|PubMed:21311953, ECO:0000305|PubMed:21311953}.
CC   -!- PATHWAY: Protein modification; protein neddylation. {ECO:0000305}.
CC   -!- SUBUNIT: Heterodimer of ECR1 and AXL1. The complex binds to RUB1/NEDD8
CC       and RCE1. {ECO:0000269|PubMed:21311953}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P42744}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences. {ECO:0000305};
CC       Name=1;
CC         IsoId=Q9ZV69-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. ULA1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AC005700; AAC69937.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08680.1; -; Genomic_DNA.
DR   EMBL; BX819419; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; G84732; G84732.
DR   RefSeq; NP_180800.1; NM_128800.4. [Q9ZV69-1]
DR   AlphaFoldDB; Q9ZV69; -.
DR   SMR; Q9ZV69; -.
DR   STRING; 3702.AT2G32410.1; -.
DR   PaxDb; Q9ZV69; -.
DR   PRIDE; Q9ZV69; -.
DR   ProteomicsDB; 241162; -. [Q9ZV69-1]
DR   EnsemblPlants; AT2G32410.1; AT2G32410.1; AT2G32410. [Q9ZV69-1]
DR   GeneID; 817802; -.
DR   Gramene; AT2G32410.1; AT2G32410.1; AT2G32410. [Q9ZV69-1]
DR   KEGG; ath:AT2G32410; -.
DR   Araport; AT2G32410; -.
DR   TAIR; locus:2062571; AT2G32410.
DR   eggNOG; KOG2016; Eukaryota.
DR   HOGENOM; CLU_019618_2_1_1; -.
DR   InParanoid; Q9ZV69; -.
DR   OMA; CRYRMIE; -.
DR   OrthoDB; 454386at2759; -.
DR   PhylomeDB; Q9ZV69; -.
DR   UniPathway; UPA00885; -.
DR   PRO; PR:Q9ZV69; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9ZV69; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005777; C:peroxisome; IDA:TAIR.
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:0009791; P:post-embryonic development; IMP: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   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; Nucleotide-binding; Nucleus; Reference proteome;
KW   Ubl conjugation pathway.
FT   CHAIN           1..523
FT                   /note="NEDD8-activating enzyme E1 regulatory subunit AXL"
FT                   /id="PRO_0000436523"
SQ   SEQUENCE   523 AA;  57941 MW;  C7CCEE03B1221843 CRC64;
     MAEPKTKYDR QLRIWGELGQ SALETASICL LNCGPTGSEA LKNLVIGGIG SITIVDGSKV
     EIGDLGNNFM VDAKSVGQSR AKTVCGFLQE LNDSVKANFV EENPDTLIST DPSFFSQFTL
     VIATQLVEDS MVKLDRICRE ANVMLVLARS YGLTGFVRIS VKEHTAIETK PDHSLDDLRL
     NSPWPELKSY VESIDLNVEE PAAHKHIPYV VILVKVAEEW AQHHSGNLPS TREEKNEFKD
     LVKSKMVSAD EENYKEALLA AFKVFAPTGI SQEIQDINHD SCAEVGSNSS DFWVMVAALK
     EFISNEGGGE VPLEGSMPDM ISSTEHYINL QKIYHSKAEA DFLSMEQRVK SILVKVGQDP
     SSISKPTIKS FCKNARKLKV CRYRTIEDEF KSPSTTELHK YLADENYSGA IGFYILLRAV
     DRFAGTYKKF PGQFDGSTDE DASQLKTIAL SLLSEMGCDG YELQEELYNE MCRFGAAEIH
     VVAALIGGIT SQEVIKLITK QFVPKRGTFI FNGIDHKSQS LTL