ZRT1_YEAST
ID ZRT1_YEAST Reviewed; 376 AA.
AC P32804; D6VV80;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Zinc-regulated transporter 1;
DE AltName: Full=High-affinity zinc transport protein ZRT1;
GN Name=ZRT1; OrderedLocusNames=YGL255W; ORFNames=NRC376;
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].
RC STRAIN=ATCC 200060 / W303;
RX PubMed=8322518; DOI=10.1002/yea.320090512;
RA Breitwieser W., Price C., Schuster T.;
RT "Identification of a gene encoding a novel zinc finger protein in
RT Saccharomyces cerevisiae.";
RL Yeast 9:551-556(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8972578;
RX DOI=10.1002/(sici)1097-0061(199612)12:15<1555::aid-yea43>3.0.co;2-q;
RA Coissac E., Maillier E., Robineau S., Netter P.;
RT "Sequence of a 39,411 bp DNA fragment covering the left end of chromosome
RT VII of Saccharomyces cerevisiae.";
RL Yeast 12:1555-1562(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
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 [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=8798516; DOI=10.1074/jbc.271.38.23203;
RA Zhao H., Eide D.;
RT "The ZRT2 gene encodes the low affinity zinc transporter in Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 271:23203-23210(1996).
RN [6]
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 zinc transport protein.
CC {ECO:0000269|PubMed:8798516}.
CC -!- INTERACTION:
CC P32804; P51533: PDR10; NbExp=2; IntAct=EBI-29677, EBI-3761544;
CC P32804; Q04182: PDR15; NbExp=2; IntAct=EBI-29677, EBI-13072;
CC P32804; P33302: PDR5; NbExp=2; IntAct=EBI-29677, EBI-13038;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Induced in activity >100-fold in response to zinc-limiting
CC growth conditions. Not expressed in zinc-replete cells.
CC {ECO:0000269|PubMed:8798516}.
CC -!- MISCELLANEOUS: Inhibited by Cu(2+) and Fe(3+) ions.
CC -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC {ECO:0000305}.
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DR EMBL; X67787; CAA47997.1; -; Genomic_DNA.
DR EMBL; Z72777; CAA96975.1; -; Genomic_DNA.
DR EMBL; X94357; CAA64132.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07864.1; -; Genomic_DNA.
DR PIR; S33654; S33654.
DR RefSeq; NP_011259.1; NM_001181121.1.
DR AlphaFoldDB; P32804; -.
DR BioGRID; 33024; 188.
DR IntAct; P32804; 5.
DR MINT; P32804; -.
DR STRING; 4932.YGL255W; -.
DR TCDB; 2.A.5.1.1; the zinc (zn(2+))-iron (fe(2+)) permease (zip) family.
DR iPTMnet; P32804; -.
DR MaxQB; P32804; -.
DR PaxDb; P32804; -.
DR PRIDE; P32804; -.
DR EnsemblFungi; YGL255W_mRNA; YGL255W; YGL255W.
DR GeneID; 852637; -.
DR KEGG; sce:YGL255W; -.
DR SGD; S000003224; ZRT1.
DR VEuPathDB; FungiDB:YGL255W; -.
DR eggNOG; KOG1558; Eukaryota.
DR HOGENOM; CLU_027089_0_2_1; -.
DR InParanoid; P32804; -.
DR OMA; VGMTGGW; -.
DR BioCyc; YEAST:G3O-30724-MON; -.
DR PRO; PR:P32804; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P32804; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:SGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0000006; F:high-affinity zinc transmembrane transporter activity; IMP:SGD.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0071578; P:zinc ion import across plasma membrane; IMP:SGD.
DR GO; GO:0071577; P:zinc ion transmembrane transport; IBA:GO_Central.
DR InterPro; IPR003689; ZIP.
DR InterPro; IPR004698; Zn/Fe_permease_fun/pln.
DR Pfam; PF02535; Zip; 1.
DR TIGRFAMs; TIGR00820; zip; 1.
PE 1: Evidence at protein level;
KW Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Zinc; Zinc transport.
FT CHAIN 1..376
FT /note="Zinc-regulated transporter 1"
FT /id="PRO_0000068768"
FT TOPO_DOM 1..50
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..122
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..242
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..310
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..354
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 177..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 376 AA; 41582 MW; 7A1F8367D49BAC3C CRC64;
MSNVTTPWWK QWDPSEVTLA DKTPDDVWKT CVLQGVYFGG NEYNGNLGAR ISSVFVILFV
STFFTMFPLI STKVKRLRIP LYVYLFAKYF GSGVIVATAF IHLMDPAYGA IGGTTCVGQT
GNWGLYSWCP AIMLTSLTFT FLTDLFSSVW VERKYGLSHD HTHDEIKDTV VRNTAAVSSE
NDNENGTANG SHDTKNGVEY YEDSDATSMD VVQSFQAQFY AFLILEFGVI FHSVMIGLNL
GSVGDEFSSL YPVLVFHQSF EGLGIGARLS AIEFPRSKRW WPWALCVAYG LTTPICVAIG
LGVRTRYVSG SYTALVISGV LDAISAGILL YTGLVELLAR DFIFNPQRTK DLRELSFNVI
CTLFGAGIMA LIGKWA
