ID   ZRG17_YEAST             Reviewed;         605 AA.
AC   P53735; D6W1L5; E9P919;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=Protein ZRG17;
DE   AltName: Full=Zinc-regulated gene 17 protein;
GN   Name=ZRG17; OrderedLocusNames=YNR039C; ORFNames=N3403;
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=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(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   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(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-498, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498, AND IDENTIFICATION BY
RP   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   -!- INTERACTION:
CC       P53735; Q03455: MSC2; NbExp=3; IntAct=EBI-28507, EBI-34990;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:14562095}.
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DR   EMBL; Z71654; CAA96319.1; -; Genomic_DNA.
DR   EMBL; AY693105; AAT93124.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10581.1; -; Genomic_DNA.
DR   PIR; S63370; S63370.
DR   RefSeq; NP_014437.1; NM_001183216.1.
DR   AlphaFoldDB; P53735; -.
DR   BioGRID; 35865; 62.
DR   DIP; DIP-5210N; -.
DR   IntAct; P53735; 6.
DR   MINT; P53735; -.
DR   STRING; 4932.YNR039C; -.
DR   TCDB; 2.A.4.4.1; the cation diffusion facilitator (cdf) family.
DR   GlyGen; P53735; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; P53735; -.
DR   MaxQB; P53735; -.
DR   PaxDb; 4932-YNR039C; -.
DR   PeptideAtlas; P53735; -.
DR   EnsemblFungi; YNR039C_mRNA; YNR039C; YNR039C.
DR   GeneID; 855775; -.
DR   KEGG; sce:YNR039C; -.
DR   AGR; SGD:S000005322; -.
DR   SGD; S000005322; ZRG17.
DR   VEuPathDB; FungiDB:YNR039C; -.
DR   eggNOG; ENOG502QV77; Eukaryota.
DR   HOGENOM; CLU_423382_0_0_1; -.
DR   InParanoid; P53735; -.
DR   OMA; FEVWSTG; -.
DR   OrthoDB; 2730679at2759; -.
DR   BioCyc; YEAST:G3O-33349-MONOMER; -.
DR   BioGRID-ORCS; 855775; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P53735; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P53735; Protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005385; F:zinc ion transmembrane transporter activity; IMP:SGD.
DR   GO; GO:0006829; P:zinc ion transport; IMP:SGD.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..605
FT                   /note="Protein ZRG17"
FT                   /id="PRO_0000203477"
FT   TOPO_DOM        1..225
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        247..254
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        255..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        276..287
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        288..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        309
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        310..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        331..363
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        364..384
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        385..399
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        400..420
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        421..422
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        423..443
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        444..545
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        546..566
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        567..605
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          118..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          473..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..177
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         16
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         131
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         498
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   CONFLICT        239
FT                   /note="A -> V (in Ref. 3; AAT93124)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   605 AA;  67461 MW;  299A89B0E4FCDBC8 CRC64;
     METPQMNAIQ EEDNLSPEVA FQTPKLNDSD ASSFSLSNMN AVGNVDGIPS QNRTFFASPR
     PSSLFYSAKE GNNSSSSIIY NPSFTFGENA SSNANINEAA LMKGKGNEGR RQSLKYIPAP
     KLVPPPPRTR SPVRGISPDA GSSKRSSMTL DSPFNFTTST LQPHQQTPPS SAASRTSFRK
     GHRYKHSSVS MNFFQEPEVK IPLNIAKSLP IPDFNDLLSN LPWPKAYIQL SIAALQIFAC
     LITFQVGHLY SWSNFITLSH FITYDIIGSL VIIFVENLSQ FQVWFTGTIT FPFGLNRIDV
     LLSFALAVSL CFVGLDLLFH IIEEFIVLFV ESGSSLTNNH DHDEINEQIP HSHIANANDS
     QNENITLWYS ILMINLVLST LSLYKTFYAN KYSNLKTKNP IITITYTAYL FIYPLLLDLL
     SSISDYLATL VISSLILWHG LTIARWTSTV LLMGFSTTSL SNSALFNNND STDTTAHTQQ
     VESKAAKEKP SVRPRSMSSL PIATKNTKIR KTGFLNSAGF TENPTTIKNM IKDQIERLSE
     FKSRYILNYD DIVISKVNFT LYVVLIKITM KGGSDDDELM LRLAIDKCIQ TSIPTCETTI
     DIDRI
//