ID ZRT2_YEAST Reviewed; 422 AA.
AC Q12436; D6VYC5;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 24-JAN-2024, entry version 153.
DE RecName: Full=Zinc-regulated transporter 2;
DE AltName: Full=Low-affinity zinc transport protein ZRT2;
GN Name=ZRT2; OrderedLocusNames=YLR130C; ORFNames=L3120, L9606.9;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION.
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148; SER-149; SER-162;
RP SER-170 AND THR-188, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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: Low-affinity zinc transport protein. Active in zinc-replete
CC cells and is time-, temperature- and concentration-dependent and
CC prefers zinc over other metals as its substrate.
CC {ECO:0000269|PubMed:8798516}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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; Z73302; CAA97701.1; -; Genomic_DNA.
DR EMBL; U53881; AAB82397.1; -; Genomic_DNA.
DR EMBL; X91258; CAA62642.1; -; Genomic_DNA.
DR EMBL; AY693187; AAT93206.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09441.1; -; Genomic_DNA.
DR PIR; S59319; S59319.
DR RefSeq; NP_013231.1; NM_001182017.1.
DR AlphaFoldDB; Q12436; -.
DR BioGRID; 31399; 30.
DR DIP; DIP-2924N; -.
DR IntAct; Q12436; 3.
DR MINT; Q12436; -.
DR STRING; 4932.YLR130C; -.
DR TCDB; 2.A.5.1.14; the zinc (zn(2+))-iron (fe(2+)) permease (zip) family.
DR iPTMnet; Q12436; -.
DR MaxQB; Q12436; -.
DR PaxDb; 4932-YLR130C; -.
DR PeptideAtlas; Q12436; -.
DR EnsemblFungi; YLR130C_mRNA; YLR130C; YLR130C.
DR GeneID; 850821; -.
DR KEGG; sce:YLR130C; -.
DR AGR; SGD:S000004120; -.
DR SGD; S000004120; ZRT2.
DR VEuPathDB; FungiDB:YLR130C; -.
DR eggNOG; KOG1558; Eukaryota.
DR HOGENOM; CLU_027089_0_2_1; -.
DR InParanoid; Q12436; -.
DR OMA; HHHGHFN; -.
DR OrthoDB; 1112460at2759; -.
DR BioCyc; YEAST:G3O-32272-MONOMER; -.
DR BioGRID-ORCS; 850821; 1 hit in 10 CRISPR screens.
DR PRO; PR:Q12436; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12436; Protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IMP:SGD.
DR GO; GO:0000007; F:low-affinity zinc ion transmembrane transporter activity; IMP:SGD.
DR GO; GO:0071578; P:zinc ion import across plasma membrane; IMP:SGD.
DR InterPro; IPR003689; ZIP.
DR InterPro; IPR004698; Zn/Fe_permease_fun/pln.
DR NCBIfam; TIGR00820; zip; 1.
DR PANTHER; PTHR11040:SF69; ZINC-REGULATED TRANSPORTER 2; 1.
DR PANTHER; PTHR11040; ZINC/IRON TRANSPORTER; 1.
DR Pfam; PF02535; Zip; 1.
PE 1: Evidence at protein level;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Zinc; Zinc transport.
FT CHAIN 1..422
FT /note="Zinc-regulated transporter 2"
FT /id="PRO_0000068769"
FT TOPO_DOM 1..27
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..99
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..262
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..290
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..358
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 380..400
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 422
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 188
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 422 AA; 46363 MW; 9A05A0BF714B04E7 CRC64;
MVDLIARDDS VDTCQASNGY NGHAGLRILA VFIILISSGL GVYFPILSSR YSFIRLPNWC
FFIAKFFGSG VIVATAFVHL LQPAAEALGD ECLGGTFAEY PWAFGICLMS LFLLFFTEII
THYFVAKTLG HDHGDHGEVT SIDVDAPSSG FVIRNMDSDP VSFNNEAAYS IHNDKTPYTT
RNEEIVATPI KEKEPGSNVT NYDLEPGKTE SLANELVPTS SHATNLASVP GKDHYSHEND
HQDVSQLATR IEEEDKEQYL NQILAVFILE FGIIFHSVFV GLSLSVAGEE FETLFIVLTF
HQMFEGLGLG TRVAETNWPE SKKYMPWLMG LAFTLTSPIA VAVGIGVRHS WIPGSRRALI
ANGVFDSISS GILIYTGLVE LMAHEFLYSN QFKGPDGLKK MLSAYLIMCC GAALMALLGK
WA
//
