FET4_YEAST
ID FET4_YEAST Reviewed; 552 AA.
AC P40988; D6W0E7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Low-affinity Fe(2+) transport protein;
DE AltName: Full=Low-affinity Fe(II) transport protein;
GN Name=FET4; OrderedLocusNames=YMR319C; ORFNames=YM9924.11C;
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 [MRNA].
RX PubMed=7929320; DOI=10.1016/s0021-9258(18)47163-3;
RA Dix D.R., Bridgham J.T., Broderius M.A., Byersdorfer C.A., Eide D.J.;
RT "The FET4 gene encodes the low affinity Fe(II) transport protein of
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 269:26092-26099(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
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 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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND SER-50, 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).
RN [7]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-39, AND IDENTIFICATION BY MASS
RP 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: Required for Fe(2+) ion low affinity uptake.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- INDUCTION: By iron deprivation.
CC -!- MISCELLANEOUS: Present with 573 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the FET4 family. {ECO:0000305}.
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DR EMBL; L34837; AAA53129.1; -; mRNA.
DR EMBL; Z54141; CAA90837.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10221.1; -; Genomic_DNA.
DR PIR; S50313; S50313.
DR RefSeq; NP_014052.1; NM_001182832.1.
DR AlphaFoldDB; P40988; -.
DR BioGRID; 35499; 107.
DR DIP; DIP-5543N; -.
DR IntAct; P40988; 16.
DR MINT; P40988; -.
DR STRING; 4932.YMR319C; -.
DR TCDB; 9.A.9.1.1; the low affinity fe(2+) transporter (fet) family.
DR iPTMnet; P40988; -.
DR MaxQB; P40988; -.
DR PaxDb; P40988; -.
DR PRIDE; P40988; -.
DR EnsemblFungi; YMR319C_mRNA; YMR319C; YMR319C.
DR GeneID; 855369; -.
DR KEGG; sce:YMR319C; -.
DR SGD; S000004938; FET4.
DR VEuPathDB; FungiDB:YMR319C; -.
DR eggNOG; ENOG502QRCK; Eukaryota.
DR HOGENOM; CLU_028340_0_0_1; -.
DR InParanoid; P40988; -.
DR OMA; WQVVMQD; -.
DR BioCyc; YEAST:G3O-32983-MON; -.
DR PRO; PR:P40988; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P40988; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005375; F:copper ion transmembrane transporter activity; IDA:SGD.
DR GO; GO:0005381; F:iron ion transmembrane transporter activity; IMP:SGD.
DR GO; GO:0015677; P:copper ion import; IMP:SGD.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0034755; P:iron ion transmembrane transport; IMP:SGD.
DR GO; GO:0015680; P:protein maturation by copper ion transfer; IMP:SGD.
DR GO; GO:0006829; P:zinc ion transport; IMP:SGD.
DR InterPro; IPR007251; Iron_permease_Fet4.
DR Pfam; PF04120; Iron_permease; 2.
PE 1: Evidence at protein level;
KW Ion transport; Iron; Iron transport; Isopeptide bond; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport; Ubl conjugation.
FT CHAIN 1..552
FT /note="Low-affinity Fe(2+) transport protein"
FT /id="PRO_0000087233"
FT TOPO_DOM 1..97
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..271
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..354
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..383
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..465
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 487..493
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 515..552
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 39
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 283
FT /note="V -> I (in Ref. 1; AAA53129)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="F -> L (in Ref. 1; AAA53129)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="T -> I (in Ref. 1; AAA53129)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 552 AA; 62792 MW; 9AB1AEA5DC6BA08E CRC64;
MGKIAEFLGN PGARPDVHHR APTVDCKQYE EFGDSNDYKN DDVVRVVSHS DESTDDELCN
VNLTETGAIF TSKGFTGLSK GFTDKTLDFL VRVAGSQAVF FIVWIILIIW VVIGIVYNAP
FNWQVVMQDG QSIQSYVWDT LLMRQQLMST HEQILICGRL KSRLASFKNY LTRSTPEEEK
ADCTVEANEV SSVENHIDPS AINGELPVEN WYDRLSNVAS RYMGSIAAMV IFWIGIFVWI
GCGAIPKDAG NTPPYTGETT GSNPRLKKFS DAWQMYINTA VAVSLLICTT FLQNIRARHD
YFTGRFLVDI FDMDEKIDYR IRKHFNDFET PHPVVTIESK KRSTGRKMID WYADIIGTGI
GVLIGVAVFA TWIGIGSPMK WDDNWWLIIG TYTGLIGFLD GFVLREVYFR IVQHEEKNYS
DVAKEDLELF QELGIECPEE FSGKAPEINT IGYRTSQYIN RICSTPWSVL VSVIIIIGLI
CIASGLRWST TGQLIANTPT MIIEEFFLLV LLQAHNWADR QRRVEVTALY ARRRILLSYV
EKRFPEVMML EK
