FTH1_YEAST
ID FTH1_YEAST Reviewed; 465 AA.
AC P38310; D6VQK4; Q9URQ1;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Iron transporter FTH1;
GN Name=FTH1; OrderedLocusNames=YBR207W; ORFNames=YBR1446;
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], FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH FET5.
RC STRAIN=ATCC 96099 / S288c / SEY6210;
RX PubMed=10608875; DOI=10.1074/jbc.274.53.38061;
RA Urbanowski J.L., Piper R.C.;
RT "The iron transporter Fth1p forms a complex with the Fet5 iron oxidase and
RT resides on the vacuolar membrane.";
RL J. Biol. Chem. 274:38061-38070(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8368014; DOI=10.1002/yea.320090714;
RA Bussereau F., Mallet L., Gaillon L., Jacquet M.;
RT "A 12.8 kb segment, on the right arm of chromosome II from Saccharomyces
RT cerevisiae including part of the DUR1,2 gene, contains five putative new
RT genes.";
RL Yeast 9:797-806(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 18; 36; 228; 249-250; 334;
RP 389-390 AND 399-401.
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 [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
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 [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-449, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-449, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-449 AND SER-453, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: High affinity iron transporter probably involved in transport
CC of intravacuolar stores of iron. {ECO:0000269|PubMed:10608875}.
CC -!- SUBUNIT: Interacts with FET5. {ECO:0000269|PubMed:10608875}.
CC -!- INTERACTION:
CC P38310; P32798: COT1; NbExp=3; IntAct=EBI-20959, EBI-5006;
CC P38310; P43561: FET5; NbExp=7; IntAct=EBI-20959, EBI-6891;
CC P38310; P38929: PMC1; NbExp=3; IntAct=EBI-20959, EBI-3097;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:10608875,
CC ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10608875, ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 486 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the oxidase-dependent Fe transporter (OFeT) (TC
CC 9.A.10.1) family. {ECO:0000305}.
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DR EMBL; AF177330; AAD53168.1; -; Genomic_DNA.
DR EMBL; Z21487; CAA79694.1; -; Genomic_DNA.
DR EMBL; Z36076; CAA85171.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07324.2; -; Genomic_DNA.
DR PIR; S34929; S34929.
DR RefSeq; NP_009766.4; NM_001178555.4.
DR AlphaFoldDB; P38310; -.
DR BioGRID; 32903; 87.
DR ComplexPortal; CPX-869; FET5-FTH1 high affinity iron exporter complex.
DR DIP; DIP-4165N; -.
DR IntAct; P38310; 63.
DR MINT; P38310; -.
DR STRING; 4932.YBR207W; -.
DR TCDB; 2.A.108.1.4; the iron/lead transporter (ilt) family.
DR iPTMnet; P38310; -.
DR MaxQB; P38310; -.
DR PaxDb; P38310; -.
DR PRIDE; P38310; -.
DR EnsemblFungi; YBR207W_mRNA; YBR207W; YBR207W.
DR GeneID; 852506; -.
DR KEGG; sce:YBR207W; -.
DR SGD; S000000411; FTH1.
DR VEuPathDB; FungiDB:YBR207W; -.
DR eggNOG; ENOG502QQ3X; Eukaryota.
DR GeneTree; ENSGT00940000176478; -.
DR HOGENOM; CLU_046738_1_1_1; -.
DR InParanoid; P38310; -.
DR OMA; NCCNGER; -.
DR BioCyc; YEAST:G3O-29146-MON; -.
DR PRO; PR:P38310; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38310; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0061841; C:high-affinity iron exporter complex; IPI:ComplexPortal.
DR GO; GO:0033573; C:high-affinity iron permease complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015093; F:ferrous iron transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005381; F:iron ion transmembrane transporter activity; ISS:SGD.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:0055072; P:iron ion homeostasis; IDA:ComplexPortal.
DR GO; GO:0034755; P:iron ion transmembrane transport; IDA:ComplexPortal.
DR InterPro; IPR004923; FTR1/Fip1/EfeU.
DR PANTHER; PTHR31632; PTHR31632; 1.
DR Pfam; PF03239; FTR1; 1.
PE 1: Evidence at protein level;
KW Ion transport; Iron; Iron transport; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..465
FT /note="Iron transporter FTH1"
FT /id="PRO_0000159650"
FT TOPO_DOM 1..11
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..170
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..358
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 380..465
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 44..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 18
FT /note="E -> K (in Ref. 2; CAA79694 and 3; CAA85171)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="G -> D (in Ref. 2; CAA79694 and 3; CAA85171)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="E -> Q (in Ref. 2; CAA79694 and 3; CAA85171)"
FT /evidence="ECO:0000305"
FT CONFLICT 249..250
FT /note="VF -> YS (in Ref. 2; CAA79694 and 3; CAA85171)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="G -> E (in Ref. 2; CAA79694 and 3; CAA85171)"
FT /evidence="ECO:0000305"
FT CONFLICT 389..390
FT /note="IC -> KY (in Ref. 2; CAA79694 and 3; CAA85171)"
FT /evidence="ECO:0000305"
FT CONFLICT 399..401
FT /note="EKY -> GKC (in Ref. 2; CAA79694 and 3; CAA85171)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 465 AA; 51420 MW; 7B4E620ABC39A053 CRC64;
MAFEDYFSFQ IFFIFLRESL EIVVIVSILL TIVKQGLSVE DDSPFEGSSS SAGLPSPNTN
TNADSTTAFL QAGPSDGNAI GTSATAANNK SRPLNVEEEE EIYEYSNELR DQDRESDEHT
ADNVKLYQKL KIQILAGGAF GLLLCMLIGG AFVSIFYHIG TDLWTLSEHY YEGVLSLVAS
VIISVMGLFF LRMGKLREKF RVKLASIIYS KDNNLLGNKT QKGVKFSEKY SFFILPFITT
LREGLEAVVF IGGIGIDQPL SSIPLSMVLA TAISTVFGIF FFRYSSSLSL KICLVVATCF
LYLIAAGLFS KGVWQLELQD YVNKCNGQDM SEVGNGPGSY DISRSVWHVN CCNGEKDGGW
MIFTAIFGWT NSATVGSVIS YNAYWLVLIC ALKLLMIEEK YGYIPYLPIS WQKKRIMKRL
SIAKASLDLK HHTSELNSST SEPDSQRRSK DSSVPLIIDS SGSAN
