Reviewed, UniProtKB/Swiss-Prot P38310 (FTH1_YEAST)

Names and origin

Protein names

Recommended name:
    Iron transporter FTH1

Gene names

Name:	FTH1
Ordered Locus Names:	YBR207W
ORF Names:	YBR1446

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	465 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	High affinity iron transporter probably involved in transport of intravacuolar stores of iron.
Subunit structure	Interacts with FET5.
Subcellular location	Vacuole membrane; Multi-pass membrane protein.
Miscellaneous	Present with 486 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the oxidase-dependent Fe transporter (OFeT) (TC 9.A.10.1) family. [View classification]

Ontologies

Keywords
Biological process	Ion transport Iron transport Transport
Cellular component	Membrane Vacuole
Domain	Transmembrane
Ligand	Iron
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	endocytosis Inferred from mutant phenotype. Source: SGD high-affinity iron ion transport Ref.1 Inferred from physical interaction. Source: SGD
Cellular component	fungal-type vacuole membrane Ref.1 Inferred from direct assay. Source: SGD
Molecular function	iron ion transmembrane transporter activity Ref.1 Traceable author statement. Source: SGD protein binding Ref.1 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FET5	P43561	3	EBI-20959,EBI-6891

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 465	465	Iron transporter FTH1		PRO_0000159650
Regions
	Topological domain	1 – 11	11	Vacuolar Potential
	Transmembrane	12 – 32	21	Potential
	Topological domain	33 – 135	103	Cytoplasmic Potential
	Transmembrane	136 – 156	21	Potential
	Topological domain	157 – 170	14	Vacuolar Potential
	Transmembrane	171 – 191	21	Potential
	Topological domain	192 – 289	98	Cytoplasmic Potential
	Transmembrane	290 – 310	21	Potential
	Topological domain	311 – 358	48	Vacuolar Potential
	Transmembrane	359 – 379	21	Potential
	Topological domain	380 – 465	86	Cytoplasmic Potential
Amino acid modifications
	Modified residue	285	1	Phosphoserine
	Modified residue	287	1	Phosphoserine
	Modified residue	449	1	Phosphoserine
	Modified residue	453	1	Phosphoserine
Experimental info
	Sequence conflict	18	1	K → E in AAD53168. Ref.1
	Sequence conflict	36	1	D → G in AAD53168. Ref.1
	Sequence conflict	228	1	Q → E in AAD53168. Ref.1
	Sequence conflict	249 – 250	2	YS → VF in AAD53168. Ref.1
	Sequence conflict	334	1	E → G in AAD53168. Ref.1
	Sequence conflict	389 – 390	2	KY → IC in AAD53168. Ref.1
	Sequence conflict	399 – 401	3	GKC → EKY in AAD53168. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P38310-1 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 79EAB530D9FD0AC4	FASTA	465	51,495
	10 20 30 40 50 60 MAFEDYFSFQ IFFIFLRKSL EIVVIVSILL TIVKQDLSVE DDSPFEGSSS SAGLPSPNTN 70 80 90 100 110 120 TNADSTTAFL QAGPSDGNAI GTSATAANNK SRPLNVEEEE EIYEYSNELR DQDRESDEHT 130 140 150 160 170 180 ADNVKLYQKL KIQILAGGAF GLLLCMLIGG AFVSIFYHIG TDLWTLSEHY YEGVLSLVAS 190 200 210 220 230 240 VIISVMGLFF LRMGKLREKF RVKLASIIYS KDNNLLGNKT QKGVKFSQKY SFFILPFITT 250 260 270 280 290 300 LREGLEAVYS IGGIGIDQPL SSIPLSMVLA TAISTVFGIF FFRYSSSLSL KICLVVATCF 310 320 330 340 350 360 LYLIAAGLFS KGVWQLELQD YVNKCNGQDM SEVENGPGSY DISRSVWHVN CCNGEKDGGW 370 380 390 400 410 420 MIFTAIFGWT NSATVGSVIS YNAYWLVLKY ALKLLMIEGK CGYIPYLPIS WQKKRIMKRL 430 440 450 460 SIAKASLDLK HHTSELNSST SEPDSQRRSK DSSVPLIIDS SGSAN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The iron transporter Fth1p forms a complex with the Fet5 iron oxidase and resides on the vacuolar membrane." Urbanowski J.L., Piper R.C. J. Biol. Chem. 274:38061-38070(1999) [PubMed: 10608875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FET5. Strain: ATCC 96099 / S288c / SEY6210.
[2]	"A 12.8 kb segment, on the right arm of chromosome II from Saccharomyces cerevisiae including part of the DUR1,2 gene, contains five putative new genes." Bussereau F., Mallet L., Gaillon L., Jacquet M. Yeast 9:797-806(1993) [PubMed: 8368014] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K. EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]	"A global topology map of the Saccharomyces cerevisiae membrane proteome." Kim H., Melen K., Oesterberg M., von Heijne G. Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed: 16847258] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
[6]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-449, MASS SPECTROMETRY.
[7]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285 AND SER-287, MASS SPECTROMETRY.
[8]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-449 AND SER-453, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF177330 Genomic DNA. Translation: AAD53168.1. Z21487 Genomic DNA. Translation: CAA79694.1. Z36076 Genomic DNA. Translation: CAA85171.1.
PIR	S34929.
RefSeq	NP_009766.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:4165N.
IntAct	P38310.
Genome annotation databases
Ensembl	YBR207W. Saccharomyces cerevisiae. [Contig view]
GeneID	852506.
GenomeReviews	Gene locus YBR207W in contig Y13134_GR.
KEGG	sce:YBR207W.
NMPDR	fig|4932.3.peg.477.
Organism-specific databases
CYGD	YBR207w.
SGD	S000000411. FTH1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P38310.
Gene expression databases
ArrayExpress	P38310.
GermOnline	YBR207W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR004923. FTR1. [Graphical view]
Pfam	PF03239. FTR1. 1 hit. [Graphical view]
BLOCKS	Search...
ProtoNet	Search...
Other Resources
LinkHub	P38310.
NextBio	971519.

Entry information

Entry name

FTH1_YEAST

Accession

Primary (citable) accession number: P38310
Secondary accession number(s): Q9URQ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	November 4, 2008
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)