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   27-MAR-2024, entry version 146.
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; 10090-ENSMUSP00000025388; -.
DR   ProteomicsDB; 266878; -.
DR   Antibodypedia; 52782; 87 antibodies from 19 providers.
DR   DNASU; 67634; -.
DR   Ensembl; ENSMUST00000025388.7; ENSMUSP00000025388.6; ENSMUSG00000024510.7.
DR   GeneID; 67634; -.
DR   KEGG; mmu:67634; -.
DR   UCSC; uc008exc.2; mouse.
DR   AGR; MGI:1914884; -.
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; WGTVLEA; -.
DR   OrthoDB; 4611704at2759; -.
DR   PhylomeDB; Q9D5H4; -.
DR   TreeFam; TF313885; -.
DR   Reactome; R-MMU-917937; Iron uptake and transport.
DR   BioGRID-ORCS; 67634; 1 hit in 77 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 cell types or tissues.
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; IDA:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; ISO:MGI.
DR   GO; GO:0006879; P:intracellular 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:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR   CDD; cd01056; Euk_Ferritin; 1.
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; FERRITIN; 1.
DR   PANTHER; PTHR11431:SF30; FERRITIN, MITOCHONDRIAL; 1.
DR   Pfam; PF00210; Ferritin; 1.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
DR   PROSITE; PS00540; FERRITIN_1; 1.
DR   PROSITE; PS00204; FERRITIN_2; 1.
DR   PROSITE; PS50905; FERRITIN_LIKE; 1.
DR   Genevisible; Q9D5H4; MM.
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
//