FET4_SCHPO
ID FET4_SCHPO Reviewed; 584 AA.
AC Q9HFE1;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Low-affinity iron/zinc ion transport protein fet4;
GN Name=fet4; ORFNames=SPBP26C9.03c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=18203864; DOI=10.1128/ec.00408-07;
RA Dainty S.J., Kennedy C.A., Watt S., Baehler J., Whitehall S.K.;
RT "Response of Schizosaccharomyces pombe to zinc deficiency.";
RL Eukaryot. Cell 7:454-464(2008).
CC -!- FUNCTION: Required for Fe(2+) ion low affinity uptake (By similarity).
CC Has a role in zinc uptake under conditions of zinc limitation.
CC {ECO:0000250, ECO:0000269|PubMed:18203864}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16823372}. Cell membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16823372}. Note=Localizes to the cell tip and
CC barrier septum.
CC -!- INDUCTION: By zinc deficiency. {ECO:0000269|PubMed:18203864}.
CC -!- SIMILARITY: Belongs to the FET4 family. {ECO:0000305}.
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DR EMBL; CU329671; CAC08238.1; -; Genomic_DNA.
DR RefSeq; NP_595134.1; NM_001021042.2.
DR AlphaFoldDB; Q9HFE1; -.
DR BioGRID; 277814; 1.
DR STRING; 4896.SPBP26C9.03c.1; -.
DR TCDB; 9.A.9.1.2; the low affinity fe(2+) transporter (fet) family.
DR iPTMnet; Q9HFE1; -.
DR PaxDb; Q9HFE1; -.
DR PRIDE; Q9HFE1; -.
DR EnsemblFungi; SPBP26C9.03c.1; SPBP26C9.03c.1:pep; SPBP26C9.03c.
DR GeneID; 2541302; -.
DR KEGG; spo:SPBP26C9.03c; -.
DR PomBase; SPBP26C9.03c; fet4.
DR VEuPathDB; FungiDB:SPBP26C9.03c; -.
DR eggNOG; ENOG502QRCK; Eukaryota.
DR HOGENOM; CLU_028340_0_0_1; -.
DR InParanoid; Q9HFE1; -.
DR OMA; WQVVMQD; -.
DR PhylomeDB; Q9HFE1; -.
DR PRO; PR:Q9HFE1; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0051286; C:cell tip; HDA:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:PomBase.
DR GO; GO:0005381; F:iron ion transmembrane transporter activity; ISO:PomBase.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0071578; P:zinc ion import across plasma membrane; ISO:PomBase.
DR InterPro; IPR007251; Iron_permease_Fet4.
DR Pfam; PF04120; Iron_permease; 4.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Golgi apparatus; Ion transport; Iron;
KW Iron transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Zinc; Zinc transport.
FT CHAIN 1..584
FT /note="Low-affinity iron/zinc ion transport protein fet4"
FT /id="PRO_0000358871"
FT TOPO_DOM 1..160
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..310
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..389
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 411..418
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 440..493
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 515..526
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 548..584
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 584 AA; 66099 MW; 9472C2B3AAA08EEF CRC64;
MTASITEIDS ISEESNVESV SHLQHSPSFE KKGADFSISL NEKKDFASPI TEEIPSPDGI
ATPEPETKKK LSFGARVWDL ICSPGRQHDV CVAAPTQLVR SCDDYANSAS TLVTNDDGTK
TKVDSDEKKH KHKNVRDYIR FKHVDIGGRI FDLITRLAGT SFTFILMLII LIVWAIVGGI
YRAPDNWQIV MQDGSSIQCY VSDTLLMRQQ QNQHIQVLTM ISQLRSRLLT TSRLLGPVLN
DKTKISSVNV ALMKDDVGDA EKLPTENWFD FICNYVSFMV GSIIFLVVYW IGIFIWIGFG
RMLGWSDEWQ LYINTAVAVE LTFTSVFLQN VRHRHMKYID RCVTSIFRID SVIEEELRRM
MGDKEPNEEI TIKMDKINLG ERSIDYYADL IGSGVGVVVS TCVFVAWIAI GNVMHWDSNW
WLIIGTYTGL VGFLDGFVLR NVYFRESSKE ATEIQTLIDE DYALYQKLDL PLPHEHITNY
KSTFGGSLSQ WIGWLCALPI SVLFSVFVIL GLIIAAGSLR FNETAQLFCN TPTMIIEGAL
LIVLIEAHNI ANLKRRIQFR QIHLRRLTIL KMLAGDNYST TSTV
