MFL1_ARATH
ID MFL1_ARATH Reviewed; 412 AA.
AC Q9FHX2;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Protein MITOFERRINLIKE 1, chloroplastic;
DE Short=AtMFL1;
DE Flags: Precursor;
GN Name=MFL1; OrderedLocusNames=At5g42130; ORFNames=MJC20.24;
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=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(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 FUNCTION, INDUCTION BY IRON, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=21371898; DOI=10.1016/j.plaphy.2011.02.003;
RA Tarantino D., Morandini P., Ramirez L., Soave C., Murgia I.;
RT "Identification of an Arabidopsis mitoferrinlike carrier protein involved
RT in Fe metabolism.";
RL Plant Physiol. Biochem. 49:520-529(2011).
CC -!- FUNCTION: Probably involved in iron transport into chloroplasts.
CC {ECO:0000269|PubMed:21371898}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000305|PubMed:21371898}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:21371898}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, developing flowers and
CC siliques. {ECO:0000269|PubMed:21371898}.
CC -!- INDUCTION: Up-regulated by iron excess. {ECO:0000269|PubMed:21371898}.
CC -!- DISRUPTION PHENOTYPE: Reduced vegetative growth and reduced expression
CC of ferritin. {ECO:0000269|PubMed:21371898}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; AB017067; BAB08446.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94771.1; -; Genomic_DNA.
DR RefSeq; NP_199028.1; NM_123578.4.
DR AlphaFoldDB; Q9FHX2; -.
DR SMR; Q9FHX2; -.
DR STRING; 3702.AT5G42130.1; -.
DR PaxDb; Q9FHX2; -.
DR PRIDE; Q9FHX2; -.
DR ProteomicsDB; 250631; -.
DR EnsemblPlants; AT5G42130.1; AT5G42130.1; AT5G42130.
DR GeneID; 834218; -.
DR Gramene; AT5G42130.1; AT5G42130.1; AT5G42130.
DR KEGG; ath:AT5G42130; -.
DR Araport; AT5G42130; -.
DR TAIR; locus:2165755; AT5G42130.
DR eggNOG; KOG0768; Eukaryota.
DR HOGENOM; CLU_015166_3_7_1; -.
DR InParanoid; Q9FHX2; -.
DR OMA; LMTQVHS; -.
DR OrthoDB; 1538959at2759; -.
DR PhylomeDB; Q9FHX2; -.
DR PRO; PR:Q9FHX2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FHX2; baseline and differential.
DR Genevisible; Q9FHX2; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0000095; F:S-adenosyl-L-methionine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006826; P:iron ion transport; IMP:TAIR.
DR GO; GO:0010039; P:response to iron ion; IEP:TAIR.
DR Gene3D; 1.50.40.10; -; 2.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00153; Mito_carr; 3.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 2: Evidence at transcript level;
KW Chloroplast; Membrane; Plastid; Plastid inner membrane; Reference proteome;
KW Repeat; Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..92
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 93..412
FT /note="Protein MITOFERRINLIKE 1, chloroplastic"
FT /id="PRO_0000413208"
FT TRANSMEM 115..135
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 112..198
FT /note="Solcar 1"
FT REPEAT 206..288
FT /note="Solcar 2"
FT REPEAT 298..392
FT /note="Solcar 3"
FT REGION 43..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 412 AA; 44361 MW; E23FD31848EB51D7 CRC64;
MEARLSETLG LPSPNLNHCH FPNEFNSLFT HFSDLTSVQS PIVRNPKLKT KSSQKPPKFS
ANFRRSDPPF ASTSISDPTH EKPGPEFLKW IKPASRSSPR IQTLIKQLSV WERAIIGAGA
GGLAGAFTYV TLLPLDAIKT KLQTKGASQV YSNTFDAIVK TFQAKGILGF YSGVSAVIVG
STFSSAVYFG TCEFGKSLLS KFPDFPTVLI PPTAGAMGNI ISSAIMVPKE LITQRMQAGA
SGRSYQVLLK ILEKDGILGL YAGYSATLLR NLPAGVLSYS SFEYLKAAVL EKTKQSHLEP
LQSVCCGALA GAISASITTP LDVVKTRLMT QIHVEAVDKL GGAMYTGVAG TVKQILTEEG
WVGFTRGMGP RVVHSACFSA IGYFAFETAR LTILNEYLKR KEESEANVAA DS