ID MTM1_YEAST Reviewed; 366 AA. AC P53320; D6VV37; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 172. DE RecName: Full=Mitochondrial carrier protein MTM1; DE AltName: Full=Manganese trafficking factor for mitochondrial SOD2; GN Name=MTM1; OrderedLocusNames=YGR257C; ORFNames=G9175; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9133741; RX DOI=10.1002/(sici)1097-0061(19970330)13:4<369::aid-yea81>3.0.co;2-v; RA Mazzoni C., Ruzzi M., Rinaldi T., Solinas F., Montebove F., Frontali L.; RT "Sequence analysis of a 10.5 kb DNA fragment from the yeast chromosome VII RT reveals the presence of three new open reading frames and of a tRNAThr RT gene."; RL Yeast 13:369-372(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169869; RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H., RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."; RL Nature 387:81-84(1997). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [5] RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE. RX PubMed=12890866; DOI=10.1073/pnas.1632471100; RA Luk E., Carroll M., Baker M., Culotta V.C.; RT "Manganese activation of superoxide dismutase 2 in Saccharomyces cerevisiae RT requires MTM1, a member of the mitochondrial carrier family."; RL Proc. Natl. Acad. Sci. U.S.A. 100:10353-10357(2003). RN [6] RP DISRUPTION PHENOTYPE. RX PubMed=16601688; DOI=10.1038/sj.emboj.7601064; RA Yang M., Cobine P.A., Molik S., Naranuntarat A., Lill R., Winge D.R., RA Culotta V.C.; RT "The effects of mitochondrial iron homeostasis on cofactor specificity of RT superoxide dismutase 2."; RL EMBO J. 25:1775-1783(2006). RN [7] RP FUNCTION. RX PubMed=18281282; DOI=10.1074/jbc.m801160200; RA Kumanovics A., Chen O.S., Li L., Bagley D., Adkins E.M., Lin H., RA Dingra N.N., Outten C.E., Keller G., Winge D., Ward D.M., Kaplan J.; RT "Identification of FRA1 and FRA2 as genes involved in regulating the yeast RT iron regulon in response to decreased mitochondrial iron-sulfur cluster RT synthesis."; RL J. Biol. Chem. 283:10276-10286(2008). RN [8] RP FUNCTION. RX PubMed=18679056; RA Lee Y.-L., Lee C.-K.; RT "Transcriptional response according to strength of calorie restriction in RT Saccharomyces cerevisiae."; RL Mol. Cells 26:299-307(2008). CC -!- FUNCTION: Involved in the mitochondrial activation of SOD2 by CC specifically facilitating insertion of the essential manganese CC cofactor. Has the ability to activate iron regulon in an iron-dependent CC manner. Responds to calorie restriction (CR) strength. CC {ECO:0000269|PubMed:12890866, ECO:0000269|PubMed:18281282, CC ECO:0000269|PubMed:18679056}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305}; CC Multi-pass membrane protein {ECO:0000305}. CC -!- DISRUPTION PHENOTYPE: Loss of mitochondrial manganese superoxide CC dismutase SOD2 activity due to misincorporation of iron into SOD2 CC rather than manganese. Normal SOD2 activity when in association with CC YFH1 deletion. Doesn't impair activity of a cytosolic version of CC manganese SOD. The iron regulatory transcription factor AFT1 is CC constitutively active. Accumulates mtDNA mutations. Elevated CC mitochondrial iron and manganese levels. {ECO:0000269|PubMed:12890866, CC ECO:0000269|PubMed:16601688}. CC -!- MISCELLANEOUS: Present with 538 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X99228; CAA67613.1; -; Genomic_DNA. DR EMBL; Z73042; CAA97286.1; -; Genomic_DNA. DR EMBL; BK006941; DAA08348.1; -; Genomic_DNA. DR PIR; S64589; S64589. DR RefSeq; NP_011773.3; NM_001181386.3. DR AlphaFoldDB; P53320; -. DR SMR; P53320; -. DR BioGRID; 33509; 73. DR DIP; DIP-5452N; -. DR IntAct; P53320; 1. DR MINT; P53320; -. DR STRING; 4932.YGR257C; -. DR MaxQB; P53320; -. DR PaxDb; 4932-YGR257C; -. DR PeptideAtlas; P53320; -. DR EnsemblFungi; YGR257C_mRNA; YGR257C; YGR257C. DR GeneID; 853173; -. DR KEGG; sce:YGR257C; -. DR AGR; SGD:S000003489; -. DR SGD; S000003489; MTM1. DR VEuPathDB; FungiDB:YGR257C; -. DR eggNOG; KOG0761; Eukaryota. DR GeneTree; ENSGT00940000167433; -. DR HOGENOM; CLU_015166_0_0_1; -. DR InParanoid; P53320; -. DR OMA; YWWGYES; -. DR OrthoDB; 3490716at2759; -. DR BioCyc; YEAST:G3O-30927-MONOMER; -. DR BioGRID-ORCS; 853173; 8 hits in 10 CRISPR screens. DR PRO; PR:P53320; -. DR Proteomes; UP000002311; Chromosome VII. DR RNAct; P53320; Protein. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:SGD. DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:SGD. DR GO; GO:0006879; P:intracellular iron ion homeostasis; IMP:SGD. DR GO; GO:1990542; P:mitochondrial transmembrane transport; IEA:InterPro. DR GO; GO:0031921; P:pyridoxal phosphate transport; IMP:SGD. DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 2. DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier. DR InterPro; IPR023395; Mt_carrier_dom_sf. DR InterPro; IPR045315; Mtm1-like. DR PANTHER; PTHR45760; FI19922P1-RELATED; 1. DR PANTHER; PTHR45760:SF2; FI19922P1-RELATED; 1. DR Pfam; PF00153; Mito_carr; 3. DR SUPFAM; SSF103506; Mitochondrial carrier; 1. DR PROSITE; PS50920; SOLCAR; 3. PE 1: Evidence at protein level; KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome; KW Repeat; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..366 FT /note="Mitochondrial carrier protein MTM1" FT /id="PRO_0000090697" FT TRANSMEM 17..36 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TRANSMEM 126..146 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TRANSMEM 162..182 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TRANSMEM 229..249 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TRANSMEM 268..286 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TRANSMEM 331..352 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT REPEAT 14..149 FT /note="Solcar 1" FT REPEAT 156..250 FT /note="Solcar 2" FT REPEAT 266..359 FT /note="Solcar 3" SQ SEQUENCE 366 AA; 40763 MW; B0358B6EE818CB1E CRC64; MSDRNTSNSL TLKERMLSAG AGSVLTSLIL TPMDVVRIRL QQQQMIPDCS CDGAAEVPNA VSSGSKMKTF TNVGGQNLNN AKIFWESACF QELHCKNSSL KFNGTLEAFT KIASVEGITS LWRGISLTLL MAIPANMVYF SGYEYIRDVS PIASTYPTLN PLFCGAIARV FAATSIAPLE LVKTKLQSIP RSSKSTKTWM MVKDLLNETR QEMKMVGPSR ALFKGLEITL WRDVPFSAIY WSSYELCKER LWLDSTRFAS KDANWVHFIN SFASGCISGM IAAICTHPFD VGKTRWQISM MNNSDPKGGN RSRNMFKFLE TIWRTEGLAA LYTGLAARVI KIRPSCAIMI SSYEISKKVF GNKLHQ //