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MTM1_YEAST
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   03-AUG-2022, entry version 166.
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}.
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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; 58.
DR   DIP; DIP-5452N; -.
DR   IntAct; P53320; 1.
DR   MINT; P53320; -.
DR   STRING; 4932.YGR257C; -.
DR   MaxQB; P53320; -.
DR   PaxDb; P53320; -.
DR   PRIDE; P53320; -.
DR   EnsemblFungi; YGR257C_mRNA; YGR257C; YGR257C.
DR   GeneID; 853173; -.
DR   KEGG; sce:YGR257C; -.
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   BioCyc; YEAST:G3O-30927-MON; -.
DR   PRO; PR:P53320; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53320; protein.
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:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IDA:SGD.
DR   GO; GO:0006879; P:cellular 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; -; 2.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   InterPro; IPR045315; Mtm1-like.
DR   PANTHER; PTHR45760; PTHR45760; 1.
DR   Pfam; PF00153; Mito_carr; 3.
DR   SUPFAM; SSF103506; SSF103506; 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
 
 
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