MFRN2_MOUSE
ID MFRN2_MOUSE Reviewed; 364 AA.
AC Q8R0Z5; Q8K4J8; Q8K4J9; Q8R578;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Mitoferrin-2;
DE AltName: Full=Mitochondrial RNA-splicing protein 3/4 homolog;
DE Short=MRS3/4;
DE AltName: Full=Mitochondrial iron transporter 2;
DE AltName: Full=Solute carrier family 25 member 28;
GN Name=Slc25a28; Synonyms=Mfrn2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 24-364 (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Muscle;
RX PubMed=11297739; DOI=10.1016/s0014-5793(01)02319-5;
RA Li F.-Y., Nikali K., Gregan J., Leibiger I., Leibiger B., Schweyen R.,
RA Larsson C., Suomalainen A.;
RT "Characterization of a novel human putative mitochondrial transporter
RT homologous to the yeast mitochondrial RNA splicing proteins 3 and 4.";
RL FEBS Lett. 494:79-84(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Kidney, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16511496; DOI=10.1038/nature04512;
RA Shaw G.C., Cope J.J., Li L., Corson K., Hersey C., Ackermann G.E.,
RA Gwynn B., Lambert A.J., Wingert R.A., Traver D., Trede N.S., Barut B.A.,
RA Zhou Y., Minet E., Donovan A., Brownlie A., Balzan R., Weiss M.J.,
RA Peters L.L., Kaplan J., Zon L.I., Paw B.H.;
RT "Mitoferrin is essential for erythroid iron assimilation.";
RL Nature 440:96-100(2006).
CC -!- FUNCTION: Mitochondrial iron transporter that mediates iron uptake.
CC Probably required for heme synthesis of hemoproteins and Fe-S cluster
CC assembly in non-erythroid cells. The iron delivered into the
CC mitochondria, presumably as Fe(2+), is then probably delivered to
CC ferrochelatase to catalyze Fe(2+) incorporation into protoprophyrin IX
CC to make heme (Probable). {ECO:0000305|PubMed:11297739,
CC ECO:0000305|PubMed:16511496}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:11297739}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11297739}. Note=Isoform 1 and isoform 2 are both
CC localized in the mitochondrion.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R0Z5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R0Z5-2; Sequence=VSP_018416;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed at low level. Expressed at
CC higher level in heart, liver, kidney and testis. Expression does not
CC vary during erythroid maturation. {ECO:0000269|PubMed:11297739,
CC ECO:0000269|PubMed:16511496}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF377993; AAM46109.1; -; mRNA.
DR EMBL; AF377994; AAM46110.1; -; mRNA.
DR EMBL; BC023172; AAH23172.1; -; mRNA.
DR EMBL; BC025908; AAH25908.1; -; mRNA.
DR CCDS; CCDS29834.1; -. [Q8R0Z5-1]
DR RefSeq; NP_660138.1; NM_145156.1. [Q8R0Z5-1]
DR RefSeq; XP_006527161.1; XM_006527098.3.
DR AlphaFoldDB; Q8R0Z5; -.
DR SMR; Q8R0Z5; -.
DR STRING; 10090.ENSMUSP00000036913; -.
DR TCDB; 2.A.29.5.4; the mitochondrial carrier (mc) family.
DR PhosphoSitePlus; Q8R0Z5; -.
DR EPD; Q8R0Z5; -.
DR MaxQB; Q8R0Z5; -.
DR PaxDb; Q8R0Z5; -.
DR PeptideAtlas; Q8R0Z5; -.
DR PRIDE; Q8R0Z5; -.
DR ProteomicsDB; 295598; -. [Q8R0Z5-1]
DR ProteomicsDB; 295599; -. [Q8R0Z5-2]
DR Antibodypedia; 31086; 140 antibodies from 19 providers.
DR DNASU; 246696; -.
DR Ensembl; ENSMUST00000046038; ENSMUSP00000036913; ENSMUSG00000040414. [Q8R0Z5-1]
DR GeneID; 246696; -.
DR KEGG; mmu:246696; -.
DR UCSC; uc008hom.2; mouse. [Q8R0Z5-2]
DR UCSC; uc008hon.2; mouse. [Q8R0Z5-1]
DR CTD; 81894; -.
DR MGI; MGI:2180509; Slc25a28.
DR VEuPathDB; HostDB:ENSMUSG00000040414; -.
DR eggNOG; KOG0760; Eukaryota.
DR GeneTree; ENSGT00940000157049; -.
DR HOGENOM; CLU_015166_3_1_1; -.
DR InParanoid; Q8R0Z5; -.
DR OMA; KVMNPSQ; -.
DR OrthoDB; 1056670at2759; -.
DR PhylomeDB; Q8R0Z5; -.
DR TreeFam; TF314118; -.
DR BioGRID-ORCS; 246696; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Slc25a28; mouse.
DR PRO; PR:Q8R0Z5; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8R0Z5; protein.
DR Bgee; ENSMUSG00000040414; Expressed in saccule of membranous labyrinth and 264 other tissues.
DR ExpressionAtlas; Q8R0Z5; baseline and differential.
DR Genevisible; Q8R0Z5; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0015093; F:ferrous iron transmembrane transporter activity; EXP:Reactome.
DR GO; GO:0048250; P:iron import into the mitochondrion; IBA:GO_Central.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR Gene3D; 1.50.40.10; -; 1.
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 Alternative splicing; Ion transport; Iron; Iron transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..364
FT /note="Mitoferrin-2"
FT /id="PRO_0000235256"
FT TRANSMEM 72..91
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..152
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..189
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..246
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..280
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..346
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 70..158
FT /note="Solcar 1"
FT REPEAT 168..252
FT /note="Solcar 2"
FT REPEAT 263..352
FT /note="Solcar 3"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..187
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11297739,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_018416"
FT CONFLICT 276
FT /note="A -> D (in Ref. 2; AAH23172)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 364 AA; 39358 MW; E21D1DED9E9D5AC5 CRC64;
MELEGRSAGG VAGGPAAGPG RSPGESALLD GWLQRGVGRG AGGGEAGAYQ PPVRLDPESG
PEYEALPAGA TVTTHMVAGA VAGILEHCVM YPIDCVKTRM QSLQPDPAAR YRNVLEALWR
IMRTEGLWRP MRGLNVTATG AGPAHALYFA CYEKLKKTLS DVIHPGGNSH IANGAAGCVA
TLLHDAAMNP AEVVKQRMQM YNSPYHRVTD CVRAVWQNEG AGAFYRSYTT QLTMNVPFQA
IHFMTYEFLQ EHFNPQRRYN PSSHVLCGAC AGAVAAAATT PLDVCKTLLN TQESLALNSN
ITGHITGMAS AFRTVYQVGG VTAYFRGVQA RVIYQIPSTA IAWSVYEFFK YLITKRQEEW
RAGK
