SMF2_YEAST
ID SMF2_YEAST Reviewed; 549 AA.
AC P38778; D3DKZ8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Manganese transporter SMF2;
GN Name=SMF2; OrderedLocusNames=YHR050W;
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].
RX PubMed=1447206; DOI=10.1016/s0021-9258(18)35810-1;
RA West A.H., Clark D.J., Martin J., Neupert W., Hartl F.-U., Horwich A.L.;
RT "Two related genes encoding extremely hydrophobic proteins suppress a
RT lethal mutation in the yeast mitochondrial processing enhancing protein.";
RL J. Biol. Chem. 267:24625-24633(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 FUNCTION.
RX PubMed=10930410; DOI=10.1074/jbc.m004611200;
RA Cohen A., Nelson H., Nelson N.;
RT "The family of SMF metal ion transporters in yeast cells.";
RL J. Biol. Chem. 275:33388-33394(2000).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11027260; DOI=10.1128/mcb.20.21.7893-7902.2000;
RA Portnoy M.E., Liu X.F., Culotta V.C.;
RT "Saccharomyces cerevisiae expresses three functionally distinct homologues
RT of the nramp family of metal transporters.";
RL Mol. Cell. Biol. 20:7893-7902(2000).
CC -!- FUNCTION: High-affinity manganese transporter involved in mobilizing
CC manganese from vesicular stores iin conditions of low manganese ion
CC concentrations. {ECO:0000269|PubMed:10930410,
CC ECO:0000269|PubMed:11027260}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:11027260};
CC Multi-pass membrane protein {ECO:0000269|PubMed:11027260}.
CC Note=Targeted to the vacuolar lumen in presence of excess manganese,
CC where it is degraded.
CC -!- SIMILARITY: Belongs to the NRAMP family. {ECO:0000305}.
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DR EMBL; U00062; AAB68900.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06742.1; -; Genomic_DNA.
DR PIR; B45154; B45154.
DR RefSeq; NP_011917.1; NM_001179180.1.
DR AlphaFoldDB; P38778; -.
DR SMR; P38778; -.
DR BioGRID; 36482; 108.
DR DIP; DIP-4171N; -.
DR IntAct; P38778; 2.
DR MINT; P38778; -.
DR STRING; 4932.YHR050W; -.
DR TCDB; 2.A.55.1.2; the metal ion (mn(2+)-iron) transporter (nramp) family.
DR PaxDb; P38778; -.
DR PRIDE; P38778; -.
DR EnsemblFungi; YHR050W_mRNA; YHR050W; YHR050W.
DR GeneID; 856447; -.
DR KEGG; sce:YHR050W; -.
DR SGD; S000001092; SMF2.
DR VEuPathDB; FungiDB:YHR050W; -.
DR eggNOG; KOG1291; Eukaryota.
DR GeneTree; ENSGT00970000196577; -.
DR HOGENOM; CLU_020088_4_1_1; -.
DR InParanoid; P38778; -.
DR OMA; QCLCAKL; -.
DR BioCyc; YEAST:G3O-31105-MON; -.
DR PRO; PR:P38778; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38778; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015086; F:cadmium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0022890; F:inorganic cation transmembrane transporter activity; IDA:SGD.
DR GO; GO:0005384; F:manganese ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006877; P:cellular cobalt ion homeostasis; IGI:SGD.
DR GO; GO:0030026; P:cellular manganese ion homeostasis; IMP:SGD.
DR GO; GO:0006824; P:cobalt ion transport; IGI:SGD.
DR GO; GO:0006826; P:iron ion transport; IBA:GO_Central.
DR GO; GO:0006828; P:manganese ion transport; IMP:SGD.
DR HAMAP; MF_00221; NRAMP; 1.
DR InterPro; IPR001046; NRAMP_fam.
DR PANTHER; PTHR11706; PTHR11706; 1.
DR Pfam; PF01566; Nramp; 1.
DR PRINTS; PR00447; NATRESASSCMP.
DR TIGRFAMs; TIGR01197; nramp; 1.
PE 3: Inferred from homology;
KW Manganese; Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..549
FT /note="Manganese transporter SMF2"
FT /id="PRO_0000212606"
FT TRANSMEM 91..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 521..541
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 549 AA; 59768 MW; 4C200057B82D65E3 CRC64;
MTSQEYEPIQ WSDESQTNND SVNDAYADVN TTHESRRRTT LQPNSTSQSM IGTLRKYARF
IGPGLMVSVS YMDPGNYSTA VAAGSAHRYK LLFSVLVSNF MAAFWQYLCA RLGAVTGLDL
AQNCKKHLPF GLNITLYILA EMAIIATDLA EVVGTAISLN ILFHIPLALG VILTVVDVLI
VLLAYKPNGS MKGIRIFEAF VSLLVVLTVV CFTVELFYAK LGPAKEIFSG FLPSKAVFEG
DGLYLSLAIL GATVMPHSLY LGSGVVQPRL REYDIKNGHY LPDANDMDNN HDNYRPSYEA
ISETLHFTIT ELLISLFTVA LFVNCAILIV SGATLYGSTQ NAEEADLFSI YNLLCSTLSK
GAGTVFVLAL LFSGQSAGIV CTLSGQMVSE GFLNWTVSPA LRRSATRAVA ITPCLILVLV
AGRSGLSGAL NASQVVLSLL LPFVSAPLLY FTSSKKIMRV QLNRTKELSR TTDKKPVADR
TEDDETIELE EMGIGSSSQE RSLVSPAPEY KDMSNGMIVT VLAIIVWLII SGLNFYMLLG
FTTGKEVHL
