SMF1_YEAST
ID SMF1_YEAST Reviewed; 575 AA.
AC P38925; D6W1U6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Manganese transporter SMF1;
GN Name=SMF1; Synonyms=ESP1; OrderedLocusNames=YOL122C;
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 [GENOMIC DNA].
RC STRAIN=ATCC 200060 / W303;
RX PubMed=8643535; DOI=10.1073/pnas.93.10.5105;
RA Supek F., Supekova L., Nelson H., Nelson N.;
RT "A yeast manganese transporter related to the macrophage protein involved
RT in conferring resistance to mycobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:5105-5110(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8896268;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1041::aid-yea989>3.0.co;2-i;
RA Lafuente M.J., Gamo F.-J., Gancedo C.;
RT "DNA sequence analysis of a 10 624 bp fragment of the left arm of
RT chromosome XV from Saccharomyces cerevisiae reveals a RNA binding protein,
RT a mitochondrial protein, two ribosomal proteins and two new open reading
RT frames.";
RL Yeast 12:1041-1045(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [5]
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 [6]
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 [7]
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).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [9]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [10]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-33 AND LYS-34, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: High-affinity manganese transporter involved in manganese
CC uptake from the extracellular environment. Contributes also to cellular
CC accumulation of other divalent metal ions such as cadmium, cobalt,
CC copper, iron and nickel. {ECO:0000269|PubMed:10930410,
CC ECO:0000269|PubMed:11027260}.
CC -!- SUBCELLULAR LOCATION: Cell 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; U15929; AAB48984.1; -; Genomic_DNA.
DR EMBL; X95258; CAA64547.1; -; Genomic_DNA.
DR EMBL; Z74864; CAA99141.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10662.1; -; Genomic_DNA.
DR PIR; S58647; S58647.
DR RefSeq; NP_014519.1; NM_001183376.1.
DR AlphaFoldDB; P38925; -.
DR SMR; P38925; -.
DR BioGRID; 34279; 67.
DR IntAct; P38925; 3.
DR MINT; P38925; -.
DR STRING; 4932.YOL122C; -.
DR TCDB; 2.A.55.1.1; the metal ion (mn(2+)-iron) transporter (nramp) family.
DR iPTMnet; P38925; -.
DR MaxQB; P38925; -.
DR PaxDb; P38925; -.
DR PRIDE; P38925; -.
DR TopDownProteomics; P38925; -.
DR EnsemblFungi; YOL122C_mRNA; YOL122C; YOL122C.
DR GeneID; 854027; -.
DR KEGG; sce:YOL122C; -.
DR SGD; S000005482; SMF1.
DR VEuPathDB; FungiDB:YOL122C; -.
DR eggNOG; KOG1291; Eukaryota.
DR HOGENOM; CLU_020088_4_1_1; -.
DR InParanoid; P38925; -.
DR OMA; SPKWLRY; -.
DR BioCyc; YEAST:G3O-33518-MON; -.
DR PRO; PR:P38925; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P38925; protein.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
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:0015295; F:solute:proton symporter activity; IDA:SGD.
DR GO; GO:0015691; P:cadmium ion transport; IGI:SGD.
DR GO; GO:0006876; P:cellular cadmium ion homeostasis; IGI:SGD.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IGI:SGD.
DR GO; GO:0030026; P:cellular manganese ion homeostasis; IMP:SGD.
DR GO; GO:0006825; P:copper ion transport; IGI:SGD.
DR GO; GO:0006826; P:iron ion transport; IGI:SGD.
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 1: Evidence at protein level;
KW Cell membrane; Isopeptide bond; Manganese; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport; Ubl conjugation.
FT CHAIN 1..575
FT /note="Manganese transporter SMF1"
FT /id="PRO_0000212605"
FT TOPO_DOM 1..70
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..156
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..218
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..344
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 366..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..463
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 485..543
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 544..564
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 565..575
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 498..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT CROSSLNK 33
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 34
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 305
FT /note="E -> D (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="S -> A (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 575 AA; 63264 MW; AC0EEEF1BBF34ACB CRC64;
MVNVGPSHAA VAVDASEARK RNISEEVFEL RDKKDSTVVI EGEAPVRTFT SSSSNHERED
TYVSKRQVMR DIFAKYLKFI GPGLMVSVAY IDPGNYSTAV DAGASNQFSL LCIILLSNFI
AIFLQCLCIK LGSVTGLDLS RACREYLPRW LNWTLYFFAE CAVIATDIAE VIGTAIALNI
LIKVPLPAGV AITVVDVFLI MFTYKPGASS IRFIRIFECF VAVLVVGVCI CFAIELAYIP
KSTSVKQVFR GFVPSAQMFD HNGIYTAISI LGATVMPHSL FLGSALVQPR LLDYDVKHGN
YTVSEEQDKV KKSKSTEEIM EEKYFNYRPT NAAIKYCMKY SMVELSITLF TLALFVNCAI
LVVAGSTLYN SPEADGADLF TIHELLSRNL APAAGTIFML ALLLSGQSAG VVCTMSGQIV
SEGHINWKLQ PWQRRLATRC ISIIPCLVIS ICIGREALSK ALNASQVVLS IVLPFLVAPL
IFFTCKKSIM KTEITVDHTE EDSHNHQNNN DRSAGSVIEQ DGSSGMEIEN GKDVKIVYMA
NNWIITVIAI IVWLFLSLLN VYAIVQLGMS HGDIS
