MFRN1_MOUSE
ID MFRN1_MOUSE Reviewed; 338 AA.
AC Q920G8; Q8C367; Q8CEJ7; Q91ZY0; Q9D2G3; Q9D547;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Mitoferrin-1;
DE AltName: Full=Mitochondrial iron transporter 1;
DE AltName: Full=Mitochondrial solute carrier protein;
DE AltName: Full=Solute carrier family 25 member 37;
GN Name=Slc25a37; Synonyms=Mfrn, Mscp;
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] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RX PubMed=11845285; DOI=10.1007/s00335001-2075-1;
RA Li Q.-Z., Eckenrode S., Ruan Q.-G., Wang C.-Y., Shi J.-D., McIndoe R.A.,
RA She J.-X.;
RT "Rapid decrease of RNA level of a novel mouse mitochondria solute carrier
RT protein (Mscp) gene at 4-5 weeks of age.";
RL Mamm. Genome 12:830-836(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 4 AND 5).
RC STRAIN=C57BL/6J; TISSUE=Liver, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PROTEIN SEQUENCE OF 288-305, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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).
RN [5]
RP INTERACTION WITH ABCB10.
RX PubMed=19805291; DOI=10.1073/pnas.0904519106;
RA Chen W., Paradkar P.N., Li L., Pierce E.L., Langer N.B.,
RA Takahashi-Makise N., Hyde B.B., Shirihai O.S., Ward D.M., Kaplan J.,
RA Paw B.H.;
RT "Abcb10 physically interacts with mitoferrin-1 (Slc25a37) to enhance its
RT stability and function in the erythroid mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16263-16268(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Mitochondrial iron transporter that specifically mediates
CC iron uptake in developing erythroid cells, thereby playing an essential
CC role in heme biosynthesis. The iron delivered into the mitochondria,
CC presumably as Fe(2+), is then probably delivered to ferrochelatase to
CC catalyze Fe(2+) incorporation into protoprophyrin IX to make heme.
CC {ECO:0000269|PubMed:16511496}.
CC -!- SUBUNIT: Interacts with ACB10; this interaction stabilizes SLC25A37 and
CC enhances the function of SLC25A37 to import mitochondrial iron during
CC erythroid differentiation. {ECO:0000269|PubMed:19805291}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q920G8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q920G8-2; Sequence=VSP_018411, VSP_018412;
CC Name=3;
CC IsoId=Q920G8-3; Sequence=VSP_018405, VSP_018410;
CC Name=4;
CC IsoId=Q920G8-4; Sequence=VSP_018407, VSP_018408;
CC Name=5;
CC IsoId=Q920G8-5; Sequence=VSP_018406, VSP_018409;
CC -!- TISSUE SPECIFICITY: Highly expressed in hematopoietic organs, fetal
CC liver, bone marrow and spleen. {ECO:0000269|PubMed:11845285,
CC ECO:0000269|PubMed:16511496}.
CC -!- DEVELOPMENTAL STAGE: In the developing embryo, it is first detected at
CC 7.5 dpc in the extraembryonic yolk sac, coincident with the appearance
CC of blood islands. Later, restricted expression is seen in 14.5 dpc
CC fetal liver, the primary source of erythrocyte production in mid-
CC gestation. Expression decreases in the spleen around 4-5 weeks of age,
CC suggesting that it is decreased during splenic lymphocyte maturation.
CC {ECO:0000269|PubMed:16511496}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB29978.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC25649.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF288621; AAL23859.1; -; mRNA.
DR EMBL; AF361699; AAL27990.1; -; mRNA.
DR EMBL; AK015790; BAB29978.1; ALT_INIT; mRNA.
DR EMBL; AK019700; BAB31839.2; -; mRNA.
DR EMBL; AK021203; BAC25649.1; ALT_FRAME; mRNA.
DR EMBL; AK050414; BAC34243.1; -; mRNA.
DR EMBL; AK086749; BAC39735.1; -; mRNA.
DR CCDS; CCDS27238.1; -. [Q920G8-1]
DR RefSeq; NP_080607.2; NM_026331.3. [Q920G8-1]
DR AlphaFoldDB; Q920G8; -.
DR SMR; Q920G8; -.
DR BioGRID; 212387; 3.
DR STRING; 10090.ENSMUSP00000039990; -.
DR TCDB; 2.A.29.5.5; the mitochondrial carrier (mc) family.
DR PhosphoSitePlus; Q920G8; -.
DR MaxQB; Q920G8; -.
DR PaxDb; Q920G8; -.
DR PRIDE; Q920G8; -.
DR ProteomicsDB; 292308; -. [Q920G8-1]
DR ProteomicsDB; 292309; -. [Q920G8-2]
DR ProteomicsDB; 292310; -. [Q920G8-3]
DR Antibodypedia; 42015; 164 antibodies from 19 providers.
DR DNASU; 67712; -.
DR Ensembl; ENSMUST00000037064; ENSMUSP00000039990; ENSMUSG00000034248. [Q920G8-1]
DR Ensembl; ENSMUST00000179116; ENSMUSP00000135940; ENSMUSG00000093954. [Q920G8-4]
DR Ensembl; ENSMUST00000183695; ENSMUSP00000138883; ENSMUSG00000093954. [Q920G8-3]
DR Ensembl; ENSMUST00000183840; ENSMUSP00000138845; ENSMUSG00000093954. [Q920G8-5]
DR Ensembl; ENSMUST00000184816; ENSMUSP00000138904; ENSMUSG00000093954. [Q920G8-3]
DR Ensembl; ENSMUST00000184914; ENSMUSP00000139104; ENSMUSG00000034248. [Q920G8-2]
DR GeneID; 67712; -.
DR KEGG; mmu:67712; -.
DR UCSC; uc029sla.1; mouse. [Q920G8-1]
DR UCSC; uc029sll.1; mouse. [Q920G8-4]
DR CTD; 51312; -.
DR MGI; MGI:1914962; Slc25a37.
DR VEuPathDB; HostDB:ENSMUSG00000034248; -.
DR VEuPathDB; HostDB:ENSMUSG00000093954; -.
DR eggNOG; KOG0760; Eukaryota.
DR GeneTree; ENSGT00940000158607; -.
DR GeneTree; ENSGT00940000172945; -.
DR HOGENOM; CLU_015166_3_1_1; -.
DR InParanoid; Q920G8; -.
DR OMA; MYNSQHQ; -.
DR PhylomeDB; Q920G8; -.
DR TreeFam; TF314118; -.
DR BioGRID-ORCS; 67712; 12 hits in 71 CRISPR screens.
DR ChiTaRS; Slc25a37; mouse.
DR PRO; PR:Q920G8; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q920G8; protein.
DR Bgee; ENSMUSG00000034248; Expressed in fetal liver hematopoietic progenitor cell and 237 other tissues.
DR ExpressionAtlas; Q920G8; baseline and differential.
DR Genevisible; Q920G8; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0015093; F:ferrous iron transmembrane transporter activity; EXP:Reactome.
DR GO; GO:0005381; F:iron ion transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0048250; P:iron import into the mitochondrion; IMP:UniProtKB.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0046985; P:positive regulation of hemoglobin biosynthetic process; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Ion transport; Iron;
KW Iron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..338
FT /note="Mitoferrin-1"
FT /id="PRO_0000235252"
FT TRANSMEM 45..64
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..125
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..162
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..219
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..253
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..320
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 43..131
FT /note="Solcar 1"
FT REPEAT 141..225
FT /note="Solcar 2"
FT REPEAT 232..326
FT /note="Solcar 3"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 71..112
FT /note="TRMQSLNPDPKARYTSIYGALKRIMHTEGFWRPLRGLNVMMM -> GHCSAS
FT LNLKFINSARMVGPTASWMGLSSLPNAQLVVGTEVL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018405"
FT VAR_SEQ 71..108
FT /note="TRMQSLNPDPKARYTSIYGALKRIMHTEGFWRPLRGLN -> GHCSASLNLK
FT FINSARMVGPTASWMGLSSLPNAQDIGK (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018406"
FT VAR_SEQ 71..81
FT /note="TRMQSLNPDPK -> MDYLSPEKRIY (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018407"
FT VAR_SEQ 82..338
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018408"
FT VAR_SEQ 109..338
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018409"
FT VAR_SEQ 113..338
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018410"
FT VAR_SEQ 148..182
FT /note="VAGSMATLLHDAVMNPAEVVKQRLQMYNSQHQSAF -> ILKAFVWSWEALL
FT SGASSPGPSNLHPRQTENSRVT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11845285,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_018411"
FT VAR_SEQ 183..338
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11845285,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_018412"
FT CONFLICT 115
FT /note="G -> R (in Ref. 2; BAC25649)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="H -> P (in Ref. 2; BAC25649)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="N -> T (in Ref. 2; BAC25649)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 37510 MW; BB35B1F70C56A3FE CRC64;
MELRRGGVGN QAAGRRMDGD CRDGGCGSKD AGSEDYENLP TSASVSTHMT AGAMAGILEH
SIMYPVDSVK TRMQSLNPDP KARYTSIYGA LKRIMHTEGF WRPLRGLNVM MMGAGPAHAM
YFACYENMKR TLNDVFSHQG NSHLANGVAG SMATLLHDAV MNPAEVVKQR LQMYNSQHQS
AFSCIRTVWR TEGLGAFYRS YTTQLTMNIP FQSIHFITYE FLQEQVNPRR DYNPQSHIIS
GGLAGALAAA ATTPLDVCKT LLNTQENMAL SLANVSGRLS GMANAFRTVY QLNGLAGYFK
GIQARVIYQM PSTAISWSVY EFFKYILTKR QLENRTLY
