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AB1E_ARATH
ID   AB1E_ARATH              Reviewed;         603 AA.
AC   Q9LID6;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=ABC transporter E family member 1;
DE            Short=ABC transporter ABCE.1;
DE            Short=AtABCE1;
DE   AltName: Full=RNase L inhibitor-like protein 1;
DE            Short=AtRLI1;
DE            Short=AthaRLI1;
GN   Name=ABCE1; Synonyms=RLI1; OrderedLocusNames=At3g13640; ORFNames=MMM17.7;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(2000).
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=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   [4]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=11346655; DOI=10.1074/jbc.m103104200;
RA   Sanchez-Fernandez R., Davies T.G., Coleman J.O., Rea P.A.;
RT   "The Arabidopsis thaliana ABC protein superfamily, a complete inventory.";
RL   J. Biol. Chem. 276:30231-30244(2001).
RN   [5]
RP   GENE FAMILY.
RX   PubMed=11855639; DOI=10.1007/s004250100661;
RA   Martinoia E., Klein M., Geisler M., Bovet L., Forestier C.,
RA   Kolukisaoglu H.U., Mueller-Roeber B., Schulz B.;
RT   "Multifunctionality of plant ABC transporters -- more than just
RT   detoxifiers.";
RL   Planta 214:345-355(2002).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=15383904; DOI=10.1007/s00239-004-2600-4;
RA   Braz A.S.K., Finnegan J., Waterhouse P., Margis R.;
RT   "A plant orthologue of RNase L inhibitor (RLI) is induced in plants showing
RT   RNA interference.";
RL   J. Mol. Evol. 59:20-30(2004).
RN   [7]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=18299247; DOI=10.1016/j.tplants.2008.02.001;
RA   Verrier P.J., Bird D., Burla B., Dassa E., Forestier C., Geisler M.,
RA   Klein M., Kolukisaoglu H.U., Lee Y., Martinoia E., Murphy A., Rea P.A.,
RA   Samuels L., Schulz B., Spalding E.J., Yazaki K., Theodoulou F.L.;
RT   "Plant ABC proteins - a unified nomenclature and updated inventory.";
RL   Trends Plant Sci. 13:151-159(2008).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC       siliques. {ECO:0000269|PubMed:15383904}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCE family.
CC       {ECO:0000305}.
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DR   EMBL; AP001307; BAB01911.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75386.1; -; Genomic_DNA.
DR   EMBL; BT003947; AAO41992.1; -; mRNA.
DR   EMBL; BT005042; AAO50575.1; -; mRNA.
DR   RefSeq; NP_187973.1; NM_112210.3.
DR   AlphaFoldDB; Q9LID6; -.
DR   SMR; Q9LID6; -.
DR   BioGRID; 5902; 1.
DR   IntAct; Q9LID6; 1.
DR   STRING; 3702.AT3G13640.1; -.
DR   PaxDb; Q9LID6; -.
DR   PRIDE; Q9LID6; -.
DR   ProteomicsDB; 244600; -.
DR   EnsemblPlants; AT3G13640.1; AT3G13640.1; AT3G13640.
DR   GeneID; 820568; -.
DR   Gramene; AT3G13640.1; AT3G13640.1; AT3G13640.
DR   KEGG; ath:AT3G13640; -.
DR   Araport; AT3G13640; -.
DR   TAIR; locus:2091506; AT3G13640.
DR   eggNOG; KOG0063; Eukaryota.
DR   HOGENOM; CLU_017344_4_1_1; -.
DR   InParanoid; Q9LID6; -.
DR   OMA; DAYMHPQ; -.
DR   OrthoDB; 359213at2759; -.
DR   PhylomeDB; Q9LID6; -.
DR   PRO; PR:Q9LID6; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LID6; baseline and differential.
DR   Genevisible; Q9LID6; AT.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IBA:GO_Central.
DR   GO; GO:0043024; F:ribosomal small subunit binding; IBA:GO_Central.
DR   GO; GO:0000054; P:ribosomal subunit export from nucleus; IBA:GO_Central.
DR   GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR   GO; GO:0006415; P:translational termination; IBA:GO_Central.
DR   CDD; cd03236; ABC_RNaseL_inhibitor_domain1; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013283; RLI1.
DR   InterPro; IPR034348; RLI_dom_1.
DR   InterPro; IPR007209; RNaseL-inhib-like_metal-bd_dom.
DR   PANTHER; PTHR19248; PTHR19248; 1.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF00037; Fer4; 1.
DR   Pfam; PF04068; RLI; 1.
DR   PRINTS; PR01868; ABCEFAMILY.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   2: Evidence at transcript level;
KW   4Fe-4S; ATP-binding; Iron; Iron-sulfur; Membrane; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Repeat; Transport.
FT   CHAIN           1..603
FT                   /note="ABC transporter E family member 1"
FT                   /id="PRO_0000379137"
FT   DOMAIN          7..39
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   DOMAIN          46..75
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   DOMAIN          70..315
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          344..566
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         110..117
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         381..388
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   603 AA;  68161 MW;  B5DE663E568BF543 CRC64;
     MSDRLTRIAI VSEDRCKPKK CRQECKKSCP VVKTGKLCIE VGSTSKSAFI SEELCIGCGI
     CVKKCPFEAI QIINLPKDLA KDTTHRYGAN GFKLHRLPIP RPGQVLGLVG TNGIGKSTAL
     KILAGKLKPN LGRFNTPPDW EEILTHFRGS ELQSYFIRVV EENLKTAIKP QHVDYIKEVV
     RGNLGKMLEK LDERGLMEEI CADMELNQVL EREARQVSGG ELQRFAIAAV FVKKADIYMF
     DEPSSYLDVR QRLKAAQVIR SLLRHDSYVI VVEHDLSVLD YLSDFVCCLY GKPGAYGVVT
     LPFSVREGIN VFLAGFIPTE NLRFRDESLT FRVSETTQEN DGEVKSYARY KYPNMTKQLG
     DFKLEVMEGE FTDSQIIVML GENGTGKTTF IRMLAGAFPR EEGVQSEIPE FNVSYKPQGN
     DSKRECTVRQ LLHDKIRDAC AHPQFMSDVI RPLQIEQLMD QVVKTLSGGE KQRVAITLCL
     GKPADIYLID EPSAHLDSEQ RITASKVIKR FILHAKKTAF IVEHDFIMAT YLADRVIVYE
     GQPAVKCIAH SPQSLLSGMN HFLSHLNITF RRDPTNFRPR INKLESIKDK EQKTAGSYYY
     LDD
 
 
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