AEE18_ARATH
ID AEE18_ARATH Reviewed; 727 AA.
AC Q84P17; F4I094; Q8GZ95; Q9C8A3;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Probable acyl-activating enzyme 18, peroxisomal;
DE EC=6.2.1.-;
GN Name=AAE18; OrderedLocusNames=At1g55320; ORFNames=F7A10.14;
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] (ISOFORM 1), TISSUE SPECIFICITY, GENE FAMILY,
RP AND NOMENCLATURE.
RX PubMed=12805634; DOI=10.1104/pp.103.020552;
RA Shockey J.M., Fulda M.S., Browse J.;
RT "Arabidopsis contains a large superfamily of acyl-activating enzymes.
RT Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme
RT a synthetases.";
RL Plant Physiol. 132:1065-1076(2003).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19043666; DOI=10.1007/s11103-008-9431-4;
RA Wiszniewski A.A., Zhou W., Smith S.M., Bussell J.D.;
RT "Identification of two Arabidopsis genes encoding a peroxisomal
RT oxidoreductase-like protein and an acyl-CoA synthetase-like protein that
RT are required for responses to pro-auxins.";
RL Plant Mol. Biol. 69:503-515(2009).
CC -!- FUNCTION: May be involved in the peroxisomal activation of 2,4-
CC dichlorophenoxybutyric acid (2,4-DB), a precursor of active auxins that
CC inhibit root growth. {ECO:0000269|PubMed:19043666}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:19043666}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q84P17-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q84P17-2; Sequence=VSP_042325;
CC -!- TISSUE SPECIFICITY: Expressed in flowers.
CC {ECO:0000269|PubMed:12805634}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but plants are resistant to 2,4-DB.
CC {ECO:0000269|PubMed:19043666}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51574.1; Type=Erroneous gene model prediction; Note=The predicted gene At1g55325 has been split into 2 genes: At1g55320 and At1g55325.; Evidence={ECO:0000305};
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DR EMBL; AY250845; AAP03028.1; -; mRNA.
DR EMBL; AC027034; AAG51574.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33225.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33226.1; -; Genomic_DNA.
DR EMBL; AK117129; BAC41807.1; -; mRNA.
DR PIR; D96595; D96595.
DR RefSeq; NP_001077723.1; NM_001084254.1. [Q84P17-2]
DR RefSeq; NP_175929.3; NM_104408.5. [Q84P17-1]
DR AlphaFoldDB; Q84P17; -.
DR SMR; Q84P17; -.
DR STRING; 3702.AT1G55320.1; -.
DR PaxDb; Q84P17; -.
DR PRIDE; Q84P17; -.
DR ProteomicsDB; 244908; -. [Q84P17-1]
DR EnsemblPlants; AT1G55320.1; AT1G55320.1; AT1G55320. [Q84P17-1]
DR EnsemblPlants; AT1G55320.2; AT1G55320.2; AT1G55320. [Q84P17-2]
DR GeneID; 841977; -.
DR Gramene; AT1G55320.1; AT1G55320.1; AT1G55320. [Q84P17-1]
DR Gramene; AT1G55320.2; AT1G55320.2; AT1G55320. [Q84P17-2]
DR KEGG; ath:AT1G55320; -.
DR Araport; AT1G55320; -.
DR TAIR; locus:2035721; AT1G55320.
DR eggNOG; KOG1175; Eukaryota.
DR OMA; WYSSTGW; -.
DR PhylomeDB; Q84P17; -.
DR BioCyc; ARA:AT1G55320-MON; -.
DR PRO; PR:Q84P17; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q84P17; baseline and differential.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0009850; P:auxin metabolic process; IMP:TAIR.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Peroxisome; Reference proteome.
FT CHAIN 1..727
FT /note="Probable acyl-activating enzyme 18, peroxisomal"
FT /id="PRO_0000415728"
FT MOTIF 725..727
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..216
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_042325"
FT CONFLICT 298
FT /note="S -> G (in Ref. 4; BAC41807)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 727 AA; 81135 MW; 3EC1EDDFC040032C CRC64;
MWKSIGELSC DDYVKAGLTL EDAKEFDKLV SDVITKAIET DPRDQWKALV DESVLKPWHP
HPLHQLLYYS VYSNWDSSVH GPPLYWFPSL SQSKSTNLGK LMEYHGPRLL GPSYKNPLES
FELFRRFSVE HPEVYWSFVI DELSLVFHTP PRCILNKSKP EGTWLPDAVL NIAECCLMPS
SHPKKEDDSV AVVWRNEGFD DSPVNRMTIK ELREQVMLVA NAISGSFEKG DTIAIDMPMT
VDAVIIYLAI ILAGCIVVSI ADSFAAKEIA TRLKISKAKG IFTQDYILRG GRRFPLYSRV
VEAAPSKVIV LPASGTELHV QLREQDVSWM DFLSNAKPHS SGENYYRPIY LPVESVINIL
FSSGTTGEPK AIPWTQLSPI RSACDGWAHL DVQVGHTYCW PTNLGWVMGP TLMFSCFLTG
ATLALYSGSP LGRGFGKFVQ DAGVTVLGTV PSLVKTWKRT NCMEGLNWTK IKFFATTGEA
SNVDDVLWLS SKADYKPVIE CCGGTELASS YIIGSPLQPQ AFGAFSTPSM TTRIIIFDEN
GVPYPDDQPC TGEVGLFPQH LGATDRLLNA NHDEVYFKGM PMYKETRLRR HGDIVKRTVG
GYYNVQGRAD DTMNLGGIKT SSIEIERVCD QADECISETA AVTLTPPNGG PELLVIFAVL
KEGFKQQSGE ELKMKFSRTI QKDLNPLFKV SFVKIVPEFP RTASSKLLRR VLRDQIKQEL
LSLRSRI
