MMT2_YEAST
ID MMT2_YEAST Reviewed; 484 AA.
AC Q08970; D6W3E6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Mitochondrial metal transporter 2;
DE Flags: Precursor;
GN Name=MMT2; Synonyms=MFT2; OrderedLocusNames=YPL224C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 17 AND 442.
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 [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9353309; DOI=10.1074/jbc.272.45.28485;
RA Li L., Kaplan J.;
RT "Characterization of two homologous yeast genes that encode mitochondrial
RT iron transporters.";
RL J. Biol. Chem. 272:28485-28493(1997).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
CC -!- FUNCTION: Mitochondrial metal transporter involved in mitochondrial
CC iron accumulation. {ECO:0000269|PubMed:9353309}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:9353309}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:14576278,
CC ECO:0000269|PubMed:9353309}.
CC -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF)
CC transporter (TC 2.A.4) family. SLC30A subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA97939.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z73580; CAA97939.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006949; DAA11212.2; -; Genomic_DNA.
DR PIR; S65243; S65243.
DR RefSeq; NP_015100.2; NM_001184038.2.
DR AlphaFoldDB; Q08970; -.
DR BioGRID; 35961; 106.
DR DIP; DIP-3963N; -.
DR MINT; Q08970; -.
DR STRING; 4932.YPL224C; -.
DR TCDB; 2.A.4.1.6; the cation diffusion facilitator (cdf) family.
DR MaxQB; Q08970; -.
DR PaxDb; Q08970; -.
DR PRIDE; Q08970; -.
DR EnsemblFungi; YPL224C_mRNA; YPL224C; YPL224C.
DR GeneID; 855877; -.
DR KEGG; sce:YPL224C; -.
DR SGD; S000006145; MMT2.
DR VEuPathDB; FungiDB:YPL224C; -.
DR eggNOG; KOG1485; Eukaryota.
DR GeneTree; ENSGT00940000176753; -.
DR HOGENOM; CLU_013430_12_1_1; -.
DR InParanoid; Q08970; -.
DR OMA; LNIYWLD; -.
DR BioCyc; YEAST:G3O-34113-MON; -.
DR PRO; PR:Q08970; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q08970; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0008324; F:cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:SGD.
DR Gene3D; 1.20.1510.10; -; 1.
DR InterPro; IPR002524; Cation_efflux.
DR InterPro; IPR027469; Cation_efflux_TMD_sf.
DR Pfam; PF01545; Cation_efflux; 1.
DR SUPFAM; SSF161111; SSF161111; 1.
DR TIGRFAMs; TIGR01297; CDF; 1.
PE 3: Inferred from homology;
KW Ion transport; Iron; Iron storage; Iron transport; Membrane; Mitochondrion;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..56
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 57..484
FT /note="Mitochondrial metal transporter 2"
FT /id="PRO_0000255968"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 73..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 17
FT /note="P -> T (in Ref. 1; CAA97939)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 484 AA; 52434 MW; F9BD946F38D10B31 CRC64;
MLRISIDSIK QFGSFVPGYN NTSYHAAGRA IRTSSLYSTM ISANPRRCLH SSKLLNKEGQ
EEGYNEQLIS KMSSQNGSNS RQNESEGKKE GKASSVKSLL QHTHSHSHTH MHDNPLLSLN
VQQIKKNPGV RITWIGLASN VGMAVGKFVG GITFHSQALL ADSVHALSDL VSDFLTLFSV
QYASRKPTSE YPYGYGKVET VGSLAVSTIL AMAGISIGWS SLCAIVGPVI PHAILESMAG
LIGETHSHSQ SLTQQATNVN AVWIAAGSIL VKEWVFQATK KVAIQTNSNV LMANAWHHRV
DSLTSLVALV AITSSYFFNI QSLDNLGGLV VSGLIIKTGG QGILSSLKEL VDQSIPPTDP
RYLEIESVIK DSIGSLKTDL DLKQSLHVRD LTILASGPNL RATTTLEVPV LHSGQEVGIR
FLENAISTIR EDLRMKVPNV GKVDVEFVDV TSDSKGDLEH SHDTKSTNHT HTHSDSADTH
THKH
