S40A3_ARATH
ID S40A3_ARATH Reviewed; 598 AA.
AC Q8W4E7; O04629;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Solute carrier family 40 member 3, chloroplastic;
DE AltName: Full=Ferroportin-3;
DE AltName: Full=Iron-regulated transporter 3;
DE Short=AtIREG3;
DE AltName: Full=Protein MULTIPLE ANTIBIOTIC RESISTANCE 1;
DE Flags: Precursor;
GN Name=IREG3; Synonyms=FPN3, MAR1, RTS3; OrderedLocusNames=At5g26820;
GN ORFNames=F2P16.6;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF ALA-441.
RX PubMed=19675150; DOI=10.1104/pp.109.143487;
RA Conte S., Stevenson D., Furner I., Lloyd A.;
RT "Multiple antibiotic resistance in Arabidopsis is conferred by mutations in
RT a chloroplast-localized transport protein.";
RL Plant Physiol. 151:559-573(2009).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20592808; DOI=10.4161/psb.5.1.10142;
RA Conte S.S., Lloyd A.M.;
RT "The MAR1 transporter is an opportunistic entry point for antibiotics.";
RL Plant Signal. Behav. 5:49-52(2010).
CC -!- FUNCTION: Probable plastid transporter that may play a role in iron
CC chelation, storage or sequestration under limiting iron conditions. In
CC presence of exogenous antibiotics, may allow opportunistic entry of
CC multiple aminoglycoside antibiotics into the chloroplast.
CC {ECO:0000269|PubMed:19675150, ECO:0000269|PubMed:20592808}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Plastid, chloroplast envelope.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:19675150}.
CC -!- INDUCTION: Down-regulated by iron deficiency.
CC {ECO:0000269|PubMed:19675150}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but plants are resistant to several aminoglycoside
CC antibiotics, such as kanamycin, streptomycin, gentamicin, amikacin,
CC tobramycin and apramycin. {ECO:0000269|PubMed:19675150,
CC ECO:0000269|PubMed:20592808}.
CC -!- SIMILARITY: Belongs to the ferroportin (FP) (TC 2.A.100) family. SLC40A
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB61047.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF007270; AAB61047.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93609.1; -; Genomic_DNA.
DR EMBL; AY062606; AAL32684.1; -; mRNA.
DR EMBL; AY128787; AAM91187.1; -; mRNA.
DR PIR; T01762; T01762.
DR RefSeq; NP_198034.2; NM_122564.5.
DR AlphaFoldDB; Q8W4E7; -.
DR SMR; Q8W4E7; -.
DR STRING; 3702.AT5G26820.1; -.
DR TCDB; 2.A.100.1.2; the ferroportin (fpn) family.
DR PaxDb; Q8W4E7; -.
DR PRIDE; Q8W4E7; -.
DR EnsemblPlants; AT5G26820.1; AT5G26820.1; AT5G26820.
DR GeneID; 832740; -.
DR Gramene; AT5G26820.1; AT5G26820.1; AT5G26820.
DR KEGG; ath:AT5G26820; -.
DR Araport; AT5G26820; -.
DR TAIR; locus:2148523; AT5G26820.
DR eggNOG; KOG2601; Eukaryota.
DR HOGENOM; CLU_033119_0_1_1; -.
DR InParanoid; Q8W4E7; -.
DR OMA; CGLMICS; -.
DR OrthoDB; 334057at2759; -.
DR PhylomeDB; Q8W4E7; -.
DR PRO; PR:Q8W4E7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8W4E7; baseline and differential.
DR Genevisible; Q8W4E7; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005381; F:iron ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:TAIR.
DR GO; GO:0006826; P:iron ion transport; IBA:GO_Central.
DR CDD; cd17480; MFS_SLC40A1_like; 1.
DR InterPro; IPR009716; Ferroportin-1.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR11660; PTHR11660; 1.
DR Pfam; PF06963; FPN1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Ion transport; Membrane; Plastid; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..54
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 55..598
FT /note="Solute carrier family 40 member 3, chloroplastic"
FT /id="PRO_0000415900"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 463..483
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 557..577
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 441
FT /note="A->V: In mar1-1; confers resistance to resistance to
FT kanamycin, streptomycin, gentamicin, amikacin, tobramycin
FT and apramycin."
FT /evidence="ECO:0000269|PubMed:19675150"
SQ 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
