FTMT_MOUSE
ID FTMT_MOUSE Reviewed; 237 AA.
AC Q9D5H4; Q14BZ8; Q3V0N6; Q9D5F4;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Ferritin, mitochondrial {ECO:0000305};
DE EC=1.16.3.1 {ECO:0000269|PubMed:15201052};
DE Flags: Precursor;
GN Name=Ftmt {ECO:0000312|MGI:MGI:1914884};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15201052; DOI=10.1016/j.jmb.2004.04.036;
RA Langlois d'Estaintot B., Santambrogio P., Granier T., Gallois B.,
RA Chevalier J.M., Precigoux G., Levi S., Arosio P.;
RT "Crystal structure and biochemical properties of the human mitochondrial
RT ferritin and its mutant Ser144Ala.";
RL J. Mol. Biol. 340:277-293(2004).
CC -!- FUNCTION: Catalyzes the oxidation of ferrous iron(II) to ferric
CC iron(III) and stores iron in a soluble, non-toxic, readily available
CC form. Important for iron homeostasis. Iron is taken up in the ferrous
CC form and deposited as ferric hydroxides after oxidation.
CC {ECO:0000269|PubMed:15201052}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
CC Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1;
CC Evidence={ECO:0000269|PubMed:15201052};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11149;
CC Evidence={ECO:0000305|PubMed:15201052};
CC -!- SUBUNIT: Homooligomer of 24 subunits. The functional molecule is
CC roughly spherical and contains a central cavity into which the
CC polymeric mineral iron core is deposited (By similarity).
CC {ECO:0000250|UniProtKB:Q8N4E7}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8N4E7}.
CC -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB29806.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK015346; BAB29806.1; ALT_INIT; mRNA.
DR EMBL; AK015400; BAB29831.1; -; mRNA.
DR EMBL; AK133009; BAE21468.1; -; mRNA.
DR EMBL; BC115514; AAI15515.1; -; mRNA.
DR EMBL; BC115515; AAI15516.1; -; mRNA.
DR CCDS; CCDS29246.1; -.
DR RefSeq; NP_080562.2; NM_026286.3.
DR AlphaFoldDB; Q9D5H4; -.
DR SMR; Q9D5H4; -.
DR STRING; 10090.ENSMUSP00000025388; -.
DR MaxQB; Q9D5H4; -.
DR PaxDb; Q9D5H4; -.
DR PRIDE; Q9D5H4; -.
DR ProteomicsDB; 266878; -.
DR Antibodypedia; 52782; 67 antibodies from 19 providers.
DR DNASU; 67634; -.
DR Ensembl; ENSMUST00000025388; ENSMUSP00000025388; ENSMUSG00000024510.
DR GeneID; 67634; -.
DR KEGG; mmu:67634; -.
DR UCSC; uc008exc.2; mouse.
DR CTD; 94033; -.
DR MGI; MGI:1914884; Ftmt.
DR VEuPathDB; HostDB:ENSMUSG00000024510; -.
DR eggNOG; KOG2332; Eukaryota.
DR GeneTree; ENSGT00940000163120; -.
DR HOGENOM; CLU_065681_4_0_1; -.
DR InParanoid; Q9D5H4; -.
DR OMA; ANNRATM; -.
DR OrthoDB; 1249457at2759; -.
DR PhylomeDB; Q9D5H4; -.
DR TreeFam; TF313885; -.
DR Reactome; R-MMU-917937; Iron uptake and transport.
DR BioGRID-ORCS; 67634; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q9D5H4; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9D5H4; protein.
DR Bgee; ENSMUSG00000024510; Expressed in seminiferous tubule of testis and 4 other tissues.
DR Genevisible; Q9D5H4; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0008199; F:ferric iron binding; IBA:GO_Central.
DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR GO; GO:0004322; F:ferroxidase activity; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; TAS:MGI.
DR GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
DR GO; GO:0006880; P:intracellular sequestering of iron ion; IBA:GO_Central.
DR GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR GO; GO:1904234; P:positive regulation of aconitate hydratase activity; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0051349; P:positive regulation of lyase activity; ISO:MGI.
DR GO; GO:1904231; P:positive regulation of succinate dehydrogenase activity; ISO:MGI.
DR Gene3D; 1.20.1260.10; -; 1.
DR InterPro; IPR001519; Ferritin.
DR InterPro; IPR012347; Ferritin-like.
DR InterPro; IPR009040; Ferritin-like_diiron.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR014034; Ferritin_CS.
DR InterPro; IPR008331; Ferritin_DPS_dom.
DR PANTHER; PTHR11431; PTHR11431; 1.
DR Pfam; PF00210; Ferritin; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS00540; FERRITIN_1; 1.
DR PROSITE; PS00204; FERRITIN_2; 1.
DR PROSITE; PS50905; FERRITIN_LIKE; 1.
PE 1: Evidence at protein level;
KW Iron; Iron storage; Metal-binding; Mitochondrion; Oxidoreductase;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..49
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 50..237
FT /note="Ferritin, mitochondrial"
FT /id="PRO_0000008851"
FT DOMAIN 66..215
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 83
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8N4E7"
FT BINDING 118
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8N4E7"
FT BINDING 118
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8N4E7"
FT BINDING 121
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8N4E7"
FT BINDING 163
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8N4E7"
FT BINDING 197
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8N4E7"
FT CONFLICT 163
FT /note="E -> G (in Ref. 1; BAB29831)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="K -> R (in Ref. 1; BAB29806)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="N -> T (in Ref. 1; BAB29806)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 237 AA; 27158 MW; 6EC3D9B1539B3B5E CRC64;
MLSCFWFFSK HISSALMSLP RVLHRFTAPQ CLASRYPLGP LLASPRRLLA SVASSQDSTR
PSRVRQNFHP DSEAAINRQI NLELYASYVY LSMAYYFSRD DVALYNFSKY FLRQSLEERE
HAEKLMKLQN QRGGRICLQD IKKPDKDDWE CGLRAMECAL LLEKNVNQSL LDLHTLASEK
GDPHLCDFLE THYLHEQVKS IKELGDHVHN LVTMGAPAAG LAEYLFDKHT LGSESKH
