MFRN1_HUMAN
ID MFRN1_HUMAN Reviewed; 338 AA.
AC Q9NYZ2; A2RU93; Q53FT7; Q69YJ8; Q969S1; Q9P0J2;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 157.
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; ORFNames=HT015;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
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] (ISOFORM 4).
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hypothalamus;
RA Song H., Gao G., Peng Y., Ren S., Chen Z., Han Z.;
RT "A novel gene expressed in human hypothalamus.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLN-96.
RC TISSUE=Pancreas;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Uterus;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 18-338 (ISOFORM 2).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
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 (By
CC similarity). {ECO:0000250}.
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:0000250|UniProtKB:Q920G8}.
CC -!- INTERACTION:
CC Q9NYZ2; Q9UL41: PNMA3; NbExp=3; IntAct=EBI-13074156, EBI-11278955;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NYZ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NYZ2-2; Sequence=VSP_018402, VSP_018403;
CC Name=4;
CC IsoId=Q9NYZ2-4; Sequence=VSP_018400;
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF64141.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAH10415.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR EMBL; AY032628; AAK38154.1; -; mRNA.
DR EMBL; AF155660; AAF67479.1; -; mRNA.
DR EMBL; AF223466; AAF64141.1; ALT_FRAME; mRNA.
DR EMBL; AK223194; BAD96914.1; -; mRNA.
DR EMBL; CH471080; EAW63617.1; -; Genomic_DNA.
DR EMBL; BC132799; AAI32800.1; -; mRNA.
DR EMBL; BC132801; AAI32802.1; -; mRNA.
DR EMBL; BC015013; AAH15013.1; -; mRNA.
DR EMBL; AL833186; CAH10415.1; ALT_SEQ; mRNA.
DR CCDS; CCDS47828.1; -. [Q9NYZ2-1]
DR RefSeq; NP_001304741.1; NM_001317812.1. [Q9NYZ2-4]
DR RefSeq; NP_001304742.1; NM_001317813.1.
DR RefSeq; NP_001304743.1; NM_001317814.1.
DR RefSeq; NP_057696.2; NM_016612.3. [Q9NYZ2-1]
DR RefSeq; XP_011542856.1; XM_011544554.2. [Q9NYZ2-4]
DR AlphaFoldDB; Q9NYZ2; -.
DR SMR; Q9NYZ2; -.
DR BioGRID; 119463; 6.
DR IntAct; Q9NYZ2; 1.
DR STRING; 9606.ENSP00000429200; -.
DR TCDB; 2.A.29.5.7; the mitochondrial carrier (mc) family.
DR iPTMnet; Q9NYZ2; -.
DR PhosphoSitePlus; Q9NYZ2; -.
DR BioMuta; SLC25A37; -.
DR DMDM; 189047115; -.
DR EPD; Q9NYZ2; -.
DR jPOST; Q9NYZ2; -.
DR MassIVE; Q9NYZ2; -.
DR MaxQB; Q9NYZ2; -.
DR PaxDb; Q9NYZ2; -.
DR PeptideAtlas; Q9NYZ2; -.
DR PRIDE; Q9NYZ2; -.
DR ProteomicsDB; 83303; -. [Q9NYZ2-1]
DR ProteomicsDB; 83304; -. [Q9NYZ2-2]
DR ProteomicsDB; 83305; -. [Q9NYZ2-4]
DR Antibodypedia; 42015; 164 antibodies from 19 providers.
DR DNASU; 51312; -.
DR Ensembl; ENST00000290075.10; ENSP00000290075.6; ENSG00000147454.14. [Q9NYZ2-2]
DR Ensembl; ENST00000519973.6; ENSP00000429200.1; ENSG00000147454.14. [Q9NYZ2-1]
DR GeneID; 51312; -.
DR KEGG; hsa:51312; -.
DR MANE-Select; ENST00000519973.6; ENSP00000429200.1; NM_016612.4; NP_057696.2.
DR UCSC; uc003xds.4; human. [Q9NYZ2-1]
DR CTD; 51312; -.
DR DisGeNET; 51312; -.
DR GeneCards; SLC25A37; -.
DR HGNC; HGNC:29786; SLC25A37.
DR HPA; ENSG00000147454; Tissue enhanced (bone).
DR MIM; 610387; gene.
DR neXtProt; NX_Q9NYZ2; -.
DR OpenTargets; ENSG00000147454; -.
DR PharmGKB; PA142670909; -.
DR VEuPathDB; HostDB:ENSG00000147454; -.
DR eggNOG; KOG0760; Eukaryota.
DR GeneTree; ENSGT00940000158607; -.
DR HOGENOM; CLU_015166_3_1_1; -.
DR InParanoid; Q9NYZ2; -.
DR OMA; MYNSQHQ; -.
DR PhylomeDB; Q9NYZ2; -.
DR TreeFam; TF314118; -.
DR PathwayCommons; Q9NYZ2; -.
DR Reactome; R-HSA-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR SignaLink; Q9NYZ2; -.
DR BioGRID-ORCS; 51312; 29 hits in 1091 CRISPR screens.
DR ChiTaRS; SLC25A37; human.
DR GeneWiki; SLC25A37; -.
DR GenomeRNAi; 51312; -.
DR Pharos; Q9NYZ2; Tbio.
DR PRO; PR:Q9NYZ2; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9NYZ2; protein.
DR Bgee; ENSG00000147454; Expressed in trabecular bone tissue and 189 other tissues.
DR ExpressionAtlas; Q9NYZ2; baseline and differential.
DR Genevisible; Q9NYZ2; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0015093; F:ferrous iron transmembrane transporter activity; IBA:GO_Central.
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 GO; GO:0046985; P:positive regulation of hemoglobin biosynthetic process; ISS:UniProtKB.
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 1: Evidence at protein 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..338
FT /note="Mitoferrin-1"
FT /id="PRO_0000235251"
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..42
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 1..151
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10931946"
FT /id="VSP_018400"
FT VAR_SEQ 149..155
FT /note="AGSMATL -> LKAFVWS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11845285,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
FT ECO:0000303|Ref.4"
FT /id="VSP_018402"
FT VAR_SEQ 156..338
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11845285,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
FT ECO:0000303|Ref.4"
FT /id="VSP_018403"
FT VARIANT 87
FT /note="I -> V (in dbSNP:rs2942194)"
FT /id="VAR_043144"
FT VARIANT 96
FT /note="R -> Q (in dbSNP:rs3736032)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_043145"
SQ SEQUENCE 338 AA; 37323 MW; 14576DF1F1854FAA CRC64;
MELRSGSVGS QAVARRMDGD SRDGGGGKDA TGSEDYENLP TSASVSTHMT AGAMAGILEH
SVMYPVDSVK TRMQSLSPDP KAQYTSIYGA LKKIMRTEGF WRPLRGVNVM IMGAGPAHAM
YFACYENMKR TLNDVFHHQG NSHLANGIAG SMATLLHDAV MNPAEVVKQR LQMYNSQHRS
AISCIRTVWR TEGLGAFYRS YTTQLTMNIP FQSIHFITYE FLQEQVNPHR TYNPQSHIIS
GGLAGALAAA ATTPLDVCKT LLNTQENVAL SLANISGRLS GMANAFRTVY QLNGLAGYFK
GIQARVIYQM PSTAISWSVY EFFKYFLTKR QLENRAPY
