FOI_DROME
ID FOI_DROME Reviewed; 706 AA.
AC Q9VSL7;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Zinc transporter foi;
DE AltName: Full=Protein fear-of-intimacy;
DE AltName: Full=Protein kastchen;
DE Flags: Precursor;
GN Name=foi {ECO:0000312|EMBL:AAF50401.3}; ORFNames=CG6817;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=12702650; DOI=10.1242/dev.00454;
RA Van Doren M., Mathews W.R., Samuels M., Moore L.A., Broihier H.T.,
RA Lehmann R.;
RT "fear of intimacy encodes a novel transmembrane protein required for gonad
RT morphogenesis in Drosophila.";
RL Development 130:2355-2364(2003).
RN [2] {ECO:0000305}
RP PARTIAL NUCLEOTIDE SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=15464587; DOI=10.1016/j.ydbio.2004.07.039;
RA Pielage J., Kippert A., Zhu M., Klambt C.;
RT "The Drosophila transmembrane protein Fear-of-intimacy controls glial cell
RT migration.";
RL Dev. Biol. 275:245-257(2004).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAF50401.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAF50401.3}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, AND MUTAGENESIS OF ASP-308;
RP HIS-554; GLU-584; GLU-588; ASP-591 AND TYR-646.
RX PubMed=15509557; DOI=10.1074/jbc.m411308200;
RA Mathews W.R., Wang F., Eide D.J., Van Doren M.;
RT "Drosophila fear of intimacy encodes a Zrt/IRT-like protein (ZIP) family
RT zinc transporter functionally related to mammalian ZIP proteins.";
RL J. Biol. Chem. 280:787-795(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376; SER-377 AND SER-381, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Required for the normal migration of longitudinal and
CC peripheral glial cells. During larval development, required for the
CC migration of the subretinal glia into the eye disk. During embryonic
CC development, also controls the migration of muscle cells toward their
CC attachment sites. Required in the mesoderm for the correct
CC morphogenesis of embryonic gonad and for tracheal branch fusion during
CC tracheal development. Shg may be cooperating with foi to mediate a
CC common mechanism for gonad and tracheal morphogenesis. Acts as a zinc
CC transporter in both yeast and mammalian cells.
CC {ECO:0000269|PubMed:12702650, ECO:0000269|PubMed:15464587,
CC ECO:0000269|PubMed:15509557}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12702650,
CC ECO:0000269|PubMed:15464587, ECO:0000269|PubMed:15509557}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:12702650,
CC ECO:0000269|PubMed:15464587, ECO:0000269|PubMed:15509557}.
CC -!- TISSUE SPECIFICITY: Maternal foi has almost completely disappeared by
CC embryonic stage 3 except in the pole cells. In stage 6 embryos,
CC expression is enriched in the invaginating mesoderm. In stage 9
CC embryos, high levels in the anterior and posterior midgut primordia. In
CC stage 14 embryos, broad expression with low levels in the epidermis.
CC {ECO:0000269|PubMed:12702650}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:15464587}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:15509557}.
CC -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC {ECO:0000269|PubMed:15509557}.
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DR EMBL; AE014296; AAF50401.3; -; Genomic_DNA.
DR RefSeq; NP_001261584.1; NM_001274655.1.
DR RefSeq; NP_001261585.1; NM_001274656.1.
DR RefSeq; NP_001286985.1; NM_001300056.1.
DR RefSeq; NP_523974.3; NM_079250.2.
DR AlphaFoldDB; Q9VSL7; -.
DR BioGRID; 64386; 12.
DR IntAct; Q9VSL7; 1.
DR STRING; 7227.FBpp0076350; -.
DR TCDB; 2.A.5.4.16; the zinc (zn(2+))-iron (fe(2+)) permease (zip) family.
DR GlyGen; Q9VSL7; 6 sites.
DR iPTMnet; Q9VSL7; -.
DR PaxDb; Q9VSL7; -.
DR PRIDE; Q9VSL7; -.
DR EnsemblMetazoa; FBtr0076624; FBpp0076350; FBgn0024236.
DR EnsemblMetazoa; FBtr0331417; FBpp0303834; FBgn0024236.
DR EnsemblMetazoa; FBtr0331418; FBpp0303835; FBgn0024236.
DR EnsemblMetazoa; FBtr0345601; FBpp0311670; FBgn0024236.
DR GeneID; 38976; -.
DR KEGG; dme:Dmel_CG6817; -.
DR CTD; 38976; -.
DR FlyBase; FBgn0024236; foi.
DR VEuPathDB; VectorBase:FBgn0024236; -.
DR eggNOG; KOG2693; Eukaryota.
DR GeneTree; ENSGT00940000169482; -.
DR HOGENOM; CLU_015114_13_1_1; -.
DR InParanoid; Q9VSL7; -.
DR OMA; YEGDLMS; -.
DR OrthoDB; 657777at2759; -.
DR PhylomeDB; Q9VSL7; -.
DR Reactome; R-DME-442380; Zinc influx into cells by the SLC39 gene family.
DR BioGRID-ORCS; 38976; 1 hit in 3 CRISPR screens.
DR ChiTaRS; foi; fly.
DR GenomeRNAi; 38976; -.
DR PRO; PR:Q9VSL7; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0024236; Expressed in wing disc and 22 other tissues.
DR ExpressionAtlas; Q9VSL7; baseline and differential.
DR Genevisible; Q9VSL7; DM.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:FlyBase.
DR GO; GO:0009986; C:cell surface; IDA:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IDA:FlyBase.
DR GO; GO:0035147; P:branch fusion, open tracheal system; IMP:FlyBase.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IBA:GO_Central.
DR GO; GO:0007417; P:central nervous system development; IMP:FlyBase.
DR GO; GO:0008354; P:germ cell migration; IMP:FlyBase.
DR GO; GO:0008406; P:gonad development; TAS:FlyBase.
DR GO; GO:0035262; P:gonad morphogenesis; IMP:FlyBase.
DR GO; GO:0007506; P:gonadal mesoderm development; IMP:FlyBase.
DR GO; GO:0007280; P:pole cell migration; TAS:FlyBase.
DR GO; GO:0071578; P:zinc ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0006829; P:zinc ion transport; IMP:UniProtKB.
DR InterPro; IPR003689; ZIP.
DR Pfam; PF02535; Zip; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Differentiation; Glycoprotein;
KW Ion transport; Membrane; Neurogenesis; Phosphoprotein; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix; Transport; Zinc;
KW Zinc transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..706
FT /note="Zinc transporter foi"
FT /evidence="ECO:0000255"
FT /id="PRO_0000041653"
FT TOPO_DOM 22..261
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..329
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..604
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 605..625
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 626..631
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 632..652
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 653..665
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 666..686
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 687..706
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 40..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 308
FT /note="D->A: 4-fold reduction in zinc transport activity in
FT yeast assay."
FT /evidence="ECO:0000269|PubMed:15509557"
FT MUTAGEN 554
FT /note="H->A: Severely reduced zinc transport activity in
FT yeast assay."
FT /evidence="ECO:0000269|PubMed:15509557"
FT MUTAGEN 584
FT /note="E->A: 2-fold reduction in zinc transport activity in
FT yeast assay; when in association with A-588 and A-591."
FT /evidence="ECO:0000269|PubMed:15509557"
FT MUTAGEN 588
FT /note="E->A: 2-fold reduction in zinc transport activity in
FT yeast assay; when in association with A-584 and A-591."
FT /evidence="ECO:0000269|PubMed:15509557"
FT MUTAGEN 591
FT /note="D->A: 2-fold reduction in zinc transport activity in
FT yeast assay; when in association with A-584 and A-588."
FT /evidence="ECO:0000269|PubMed:15509557"
FT MUTAGEN 646
FT /note="Y->A: 2-fold reduction zinc transport activity in
FT yeast assay."
FT /evidence="ECO:0000269|PubMed:15509557"
SQ SEQUENCE 706 AA; 77376 MW; 80212B9213D91B07 CRC64;
MARHIMAVCV VCLLCAHRLH CQDHIESLLG PARVTTHNSQ DQLNARVYTN LSPSSETTDR
RQQRSASGDD DTFNYSISPP SRREKRHAGH EHGPTSESRV PQITQYYLEK LMAQDELMNS
SGFDGLLQQL SLHSLASGAS EGTCVPGSRL VHHVQPHDHH HAHHHEEEDH SLQLNNCTLI
QNGTTSNVIC PSLPNNNTHP LGKEAKNFTL SDKDLLHLCP ILLYELKAQS GGCIEPAILS
DIDTTEELLE AEKDKDIFYV WIYAFISVFA CGILGLVGVA IIPFMGSRYY KYIIQYLVAL
AVGTMTGDAL LHLLPHSLAG QDERGMIMKG LGCLGGIIFF YVMEHALTMI SEWRKSVEKK
ETKKPSRAKV MRDPDSSVNN SVAGDKICKQ KYSSYPYCYD EITMNNKQSE WMHLPFDVAA
GAGGDAPSVA ELRNGVGDHD GSNDMAAAAE SLISPLHTNC VEMNHHNHNH KHNSHQQNHE
GQDSNTIVTD LDGNAVYAVN KAKDKDSRND HVTVILREHE SSHHGHSHRH GHVHSPPETL
SAVAWMIIMG DGLHNFTDGM AIGAAFAENI AGGFSTSLAV FCHELPHELG DFAILIKAGM
SVKSAVYYNL LTGVLSFIGM IFGIAFGQSQ DVAQWMFAVA AGLFIYIALV DMMPEISASH
KSLGQFLLQI LGMLSGVGIM LLIALYEGDL MSAFGTAGAA SHQHAH
