MFRN_CAEEL
ID MFRN_CAEEL Reviewed; 312 AA.
AC Q23125;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Mitoferrin;
GN Name=mfn-1 {ECO:0000303|PubMed:22253756, ECO:0000312|WormBase:W02B12.9};
GN ORFNames=W02B12.9 {ECO:0000312|WormBase:W02B12.9};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=22253756; DOI=10.1371/journal.pone.0029666;
RA Ren Y., Yang S., Tan G., Ye W., Liu D., Qian X., Ding Z., Zhong Y.,
RA Zhang J., Jiang D., Zhao Y., Lu J.;
RT "Reduction of mitoferrin results in abnormal development and extended
RT lifespan in Caenorhabditis elegans.";
RL PLoS ONE 7:E29666-E29666(2012).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=25769692; DOI=10.1016/j.exger.2015.03.005;
RA Ren Y., Chen S., Ma M., Yao X., Sun D., Li B., Lu J.;
RT "The activation of protein homeostasis protective mechanisms perhaps is not
RT responsible for lifespan extension caused by deficiencies of mitochondrial
RT proteins in C. elegans.";
RL Exp. Gerontol. 65:53-57(2015).
CC -!- FUNCTION: Mitochondrial iron transporter that mediates iron uptake.
CC Probably required for heme synthesis of hemoproteins and Fe-S cluster
CC assembly. {ECO:0000250|UniProtKB:Q9VAY3}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q9VAY3}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9VAY3}.
CC -!- DEVELOPMENTAL STAGE: Expressed in a variety of tissues from embryo to
CC adult. {ECO:0000269|PubMed:22253756}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in smaller, but
CC normally-proportioned animals that are paler and thinner as compared to
CC wild-type, a reduced growth rate, slow movements with a 35% decrease in
CC the number of body bends per 20 seconds, reduced brood size, increased
CC lifespan and inceased sensitivity to the oxidative stress inducer
CC paraquat (PubMed:22253756). RNAi-mediated knockdown results in
CC increased lifespan (PubMed:22253756, PubMed:25769692).
CC {ECO:0000269|PubMed:22253756, ECO:0000269|PubMed:25769692}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; Z66521; CAA91399.1; -; Genomic_DNA.
DR PIR; T26089; T26089.
DR RefSeq; NP_496447.1; NM_064046.4.
DR AlphaFoldDB; Q23125; -.
DR SMR; Q23125; -.
DR STRING; 6239.W02B12.9; -.
DR EPD; Q23125; -.
DR PaxDb; Q23125; -.
DR PeptideAtlas; Q23125; -.
DR EnsemblMetazoa; W02B12.9.1; W02B12.9.1; WBGene00012204.
DR GeneID; 174752; -.
DR KEGG; cel:CELE_W02B12.9; -.
DR UCSC; W02B12.9; c. elegans.
DR CTD; 174752; -.
DR WormBase; W02B12.9; CE03769; WBGene00012204; mfn-1.
DR eggNOG; KOG0760; Eukaryota.
DR GeneTree; ENSGT00940000169345; -.
DR HOGENOM; CLU_015166_3_1_1; -.
DR InParanoid; Q23125; -.
DR OMA; FTTQLTM; -.
DR OrthoDB; 1056670at2759; -.
DR PhylomeDB; Q23125; -.
DR PRO; PR:Q23125; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00012204; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
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: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 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 Ion transport; Iron; Iron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..312
FT /note="Mitoferrin"
FT /id="PRO_0000235261"
FT TRANSMEM 17..36
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..97
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..190
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..297
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 15..103
FT /note="Solcar 1"
FT REPEAT 112..196
FT /note="Solcar 2"
FT REPEAT 203..303
FT /note="Solcar 3"
SQ SEQUENCE 312 AA; 34093 MW; D65FC4DD2936F76A CRC64;
MGGGGEDEYE SLPTHSVPVH LTAGALAGAV EHCVMFPFDS VKTRMQSLCP CPETKCPTPV
HSLMSIVKRE GWLRPLRGVN AVAAGSMPAH ALYFTVYEKM KGYLTGNSAG HSNTLAYGAS
GVVATLIHDA IMNPAEVVKQ RMQMAFSPYG SSLECARCVY NREGVAAFYR SYTTQLAMNV
PFQAIHFMSY EFWQHVLNPE HKYDPKSHLI AGGLAGGLAA ALTTPMDCVK TVLNTQQAAE
ADPANRRIFL QARYRYRGIS DAVRTIYSQR GLSGFSCGLQ ARVIFQVPAT ALSWSVYELF
KFMLSFEGGH SS