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Solute carrier family 40 member 3, chloroplastic (Ferroportin-3) (Iron-regulated transporter 3) (AtIREG3) (Protein MULTIPLE ANTIBIOTIC RESISTANCE 1)

 S40A3_ARATH             Reviewed;         598 AA.
Q8W4E7; O04629;
21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
22-NOV-2017, entry version 76.
RecName: Full=Solute carrier family 40 member 3, chloroplastic;
AltName: Full=Ferroportin-3;
AltName: Full=Iron-regulated transporter 3;
Short=AtIREG3;
AltName: Full=Protein MULTIPLE ANTIBIOTIC RESISTANCE 1;
Flags: Precursor;
Name=IREG3; Synonyms=FPN3, MAR1, RTS3; OrderedLocusNames=At5g26820;
ORFNames=F2P16.6;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION,
DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ALA-441.
PubMed=19675150; DOI=10.1104/pp.109.143487;
Conte S., Stevenson D., Furner I., Lloyd A.;
"Multiple antibiotic resistance in Arabidopsis is conferred by
mutations in a chloroplast-localized transport protein.";
Plant Physiol. 151:559-573(2009).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=20592808; DOI=10.4161/psb.5.1.10142;
Conte S.S., Lloyd A.M.;
"The MAR1 transporter is an opportunistic entry point for
antibiotics.";
Plant Signal. Behav. 5:49-52(2010).
-!- FUNCTION: Probable plastid transporter that may play a role in
iron chelation, storage or sequestration under limiting iron
conditions. In presence of exogenous antibiotics, may allow
opportunistic entry of multiple aminoglycoside antibiotics into
the chloroplast. {ECO:0000269|PubMed:19675150,
ECO:0000269|PubMed:20592808}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}. Plastid, chloroplast envelope.
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:19675150}.
-!- INDUCTION: Down-regulated by iron deficiency.
{ECO:0000269|PubMed:19675150}.
-!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
conditions, but plants are resistant to several aminoglycoside
antibiotics, such as kanamycin, streptomycin, gentamicin,
amikacin, tobramycin and apramycin. {ECO:0000269|PubMed:19675150,
ECO:0000269|PubMed:20592808}.
-!- SIMILARITY: Belongs to the ferroportin (FP) (TC 2.A.100) family.
SLC40A subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB61047.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF007270; AAB61047.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002688; AED93609.1; -; Genomic_DNA.
EMBL; AY062606; AAL32684.1; -; mRNA.
EMBL; AY128787; AAM91187.1; -; mRNA.
PIR; T01762; T01762.
RefSeq; NP_198034.2; NM_122564.5.
UniGene; At.27285; -.
ProteinModelPortal; Q8W4E7; -.
STRING; 3702.AT5G26820.1; -.
TCDB; 2.A.100.1.2; the ferroportin (fpn) family.
PaxDb; Q8W4E7; -.
PRIDE; Q8W4E7; -.
EnsemblPlants; AT5G26820.1; AT5G26820.1; AT5G26820.
GeneID; 832740; -.
Gramene; AT5G26820.1; AT5G26820.1; AT5G26820.
KEGG; ath:AT5G26820; -.
Araport; AT5G26820; -.
TAIR; locus:2148523; AT5G26820.
eggNOG; KOG2601; Eukaryota.
eggNOG; ENOG410XS3F; LUCA.
HOGENOM; HOG000241195; -.
InParanoid; Q8W4E7; -.
OMA; CSIMGLV; -.
OrthoDB; EOG09360636; -.
PhylomeDB; Q8W4E7; -.
PRO; PR:Q8W4E7; -.
Proteomes; UP000006548; Chromosome 5.
Genevisible; Q8W4E7; AT.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005381; F:iron ion transmembrane transporter activity; IEA:InterPro.
GO; GO:0005215; F:transporter activity; IDA:TAIR.
GO; GO:0006879; P:cellular iron ion homeostasis; IMP:TAIR.
InterPro; IPR009716; Ferroportin-1.
InterPro; IPR036259; MFS_trans_sf.
PANTHER; PTHR11660; PTHR11660; 1.
Pfam; PF06963; FPN1; 1.
SUPFAM; SSF103473; SSF103473; 1.
1: Evidence at protein level;
Chloroplast; Complete proteome; Ion transport; Membrane; Plastid;
Reference proteome; Transit peptide; Transmembrane;
Transmembrane helix; Transport.
TRANSIT 1 54 Chloroplast. {ECO:0000255}.
CHAIN 55 598 Solute carrier family 40 member 3,
chloroplastic.
/FTId=PRO_0000415900.
TRANSMEM 182 202 Helical. {ECO:0000255}.
TRANSMEM 216 236 Helical. {ECO:0000255}.
TRANSMEM 252 272 Helical. {ECO:0000255}.
TRANSMEM 297 317 Helical. {ECO:0000255}.
TRANSMEM 326 346 Helical. {ECO:0000255}.
TRANSMEM 402 422 Helical. {ECO:0000255}.
TRANSMEM 432 452 Helical. {ECO:0000255}.
TRANSMEM 463 483 Helical. {ECO:0000255}.
TRANSMEM 493 513 Helical. {ECO:0000255}.
TRANSMEM 530 550 Helical. {ECO:0000255}.
TRANSMEM 557 577 Helical. {ECO:0000255}.
MUTAGEN 441 441 A->V: In mar1-1; confers resistance to
resistance to kanamycin, streptomycin,
gentamicin, amikacin, tobramycin and
apramycin. {ECO:0000269|PubMed:19675150}.
SEQUENCE 598 AA; 64486 MW; 26C42C4115A4C293 CRC64;
MVVSMALVRH SPSFDFLFHF PVDRSRFLSP VAFSSVRYHR FHSCRWLSLR SSPSCSRRLN
SFSSRCSITN TDVCHEFVTT DDEIHEDLLT PIEDHSIPIV HLDTNISVTE SLTLLTECTY
VDTVLTALPV LSEEEQTVIA ATPAHPEGLY VLYASCLVGN LVEQLWNFAW PSAIAMLYPS
LLPVAVMGFV TKLAIIAGGP VVGKFMDYSP RVPTYISLNV IQAAAQVLSA GMIIHAYTVP
STSASSILLQ PWFFALLFAG AIDSLCGIAS GVAIERDWVV LLAGINRPIA LAQANAVLHR
IDLLCEIAGT MLFGILLSKY DPVTCLKFAA TLMVGSLPTM TALIWLTNKF SSGVLDRPKC
SLNSCSAEGS RTNTDSIFDI GMETIKLGWK EYIQQPVLPA SLAYVLLYFN IVLTPGSLMT
AFLTQRCVNP SVIGGFSGLC AVMGVAATFL SANLVKRVGI LKAGAVGLFF QASLLAVAVA
VYCSSSLSHK SPLFFFLSMI VLSRLGHMSY GVVGAQILQT GIPSSKANLI GATEISVASL
AESLMLGVAI AANDASHFGF LAVLSLLSVV AASLIFCRLL RNPTDEQRRL FSFDPLSN


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