ZRG8_YEAST
ID ZRG8_YEAST Reviewed; 1076 AA.
AC P40021; D3DLT2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Zinc-regulated protein 8;
GN Name=ZRG8; OrderedLocusNames=YER033C;
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=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 INDUCTION.
RX PubMed=10978274; DOI=10.1093/genetics/156.1.45;
RA Yuan D.S.;
RT "Zinc-regulated genes in Saccharomyces cerevisiae revealed by transposon
RT tagging.";
RL Genetics 156:45-58(2000).
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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SSD1.
RX PubMed=15972461; DOI=10.1534/genetics.105.042101;
RA Kurischko C., Weiss G., Ottey M., Luca F.C.;
RT "A role for the Saccharomyces cerevisiae regulation of Ace2 and polarized
RT morphogenesis signaling network in cell integrity.";
RL Genetics 171:443-455(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275, 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 [8]
RP INTERACTION WITH BUD27 AND GIS1.
RX PubMed=17043893; DOI=10.1007/s00438-006-0171-3;
RA Tronnersjoe S., Hanefalk C., Balciunas D., Hu G.-Z., Nordberg N., Muren E.,
RA Ronne H.;
RT "The jmjN and jmjC domains of the yeast zinc finger protein Gis1 interact
RT with 19 proteins involved in transcription, sumoylation and DNA repair.";
RL Mol. Genet. Genomics 277:57-70(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-676, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275; SER-403 AND SER-632, AND
RP IDENTIFICATION BY 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275; SER-354; SER-403 AND
RP SER-407, AND 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: Involved in the integrity functions of RAM, a conserved
CC signaling network that regulates maintenance of polarized growth and
CC daughter-cell-specific transcription. {ECO:0000269|PubMed:15972461}.
CC -!- SUBUNIT: Interacts with BUD27, GIS1 and SSD1.
CC {ECO:0000269|PubMed:15972461, ECO:0000269|PubMed:17043893}.
CC -!- INTERACTION:
CC P40021; Q04439: MYO5; NbExp=2; IntAct=EBI-22484, EBI-11687;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Bud. Bud neck. Bud tip. Note=Localized
CC to the cortex of small and large buds during bud growth, to the bud
CC neck during mitotic exit and to the tips of mating projections in
CC pheromone-treated cells.
CC -!- INDUCTION: Repressed by zinc. {ECO:0000269|PubMed:10978274}.
CC -!- SIMILARITY: Belongs to the ZRG8 family. {ECO:0000305}.
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DR EMBL; U18796; AAB64568.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07686.1; -; Genomic_DNA.
DR PIR; S50536; S50536.
DR RefSeq; NP_010950.1; NM_001178924.1.
DR AlphaFoldDB; P40021; -.
DR SMR; P40021; -.
DR BioGRID; 36768; 45.
DR IntAct; P40021; 7.
DR MINT; P40021; -.
DR STRING; 4932.YER033C; -.
DR iPTMnet; P40021; -.
DR MaxQB; P40021; -.
DR PaxDb; P40021; -.
DR PRIDE; P40021; -.
DR EnsemblFungi; YER033C_mRNA; YER033C; YER033C.
DR GeneID; 856755; -.
DR KEGG; sce:YER033C; -.
DR SGD; S000000835; ZRG8.
DR VEuPathDB; FungiDB:YER033C; -.
DR eggNOG; ENOG502QSM8; Eukaryota.
DR HOGENOM; CLU_301677_0_0_1; -.
DR InParanoid; P40021; -.
DR OMA; QSLKYHD; -.
DR BioCyc; YEAST:G3O-30214-MON; -.
DR PRO; PR:P40021; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40021; protein.
DR GO; GO:0005933; C:cellular bud; IDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..1076
FT /note="Zinc-regulated protein 8"
FT /id="PRO_0000202624"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1000..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1042..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..129
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..450
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 676
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
SQ SEQUENCE 1076 AA; 119350 MW; 4C0B1AB003617BBC CRC64;
MRSFIKAHKK STSFDESPKR HSNFSGNTNN SSQRSSDDSL DFLPSTPSQM NYDSIPPPAK
HSPGFESFHR LANKTSKLFK KTSNSNLNSH LASTPTTSTN QTTSNSFVLQ NPPTKNTGPP
PPLPPPLFPS SSTSSFSRHD NESEYTAYKK TSPAKDFNRT TDSLPAIKGT ITHSWGDSKV
ESHVIILNDP ASPASNTSEA TSSKQFKTPI IGNENLTSTT SPSNLEPAIR ILNKNKGKQQ
ENIDDAEDGS SKKEHHVYKA LALAKNRNRQ ARIHSHDDII NLGKASQMDM SLLAAAFSGN
STTTINNDQS SNEQTDEKIL DIERVTTTST LTSSETTSPI NKSPCFYSQT LSLSPKIRHG
DLQSSPSKVN KNDSQNETLN KKKVRISLNR KEEEKVYSLN NNSDEYSVNE KETHKANDCN
DESSENGDGD NDHDDDYDDD DDDDDDDDES EFSFEYAGIN VRTSSVKYYS KPEPAANVYI
DDLYEDENFD DDMNCIEDDE SGNEGNEICG LSTRFEETSL KSNKVKKFND LFNLSDDDEE
EDGKDNSNNG DENESDNLYQ KRLENGKETF NGNHGGHHDD ASLGETVDNK EQFLINDNVK
KPIQKYNDLF DLSDEDDNDD KEMSEAESYM FSDEAPSIES GPANAKSTRG IYSQSNKNII
RDGKPNYSFS LKRNNSDDET EHTSAIKASL TGTTGSTKPT VKSFSDIFNV DDSASDAESD
SGTGGNNSNG LVSNDSERQV SLQSSLYETK SESHPPNHPH SQILQTPAKI VITPSVSDAQ
SQALAITDDD GEDDDDDTSS ILRTPFQLID SSHSQQPHYA SPQYTAVLNS PPLPPPARSQ
SLKYHDLNCD LDSEVPRPMS NLFFIDEAEE DEYNQKSKFF DFDHYDIDEI NGIPEDFNFS
DSERDDLNRR TLKSPLRGGS KNREVSPFSS VSSSFRSTHS FNGKLTINQG AKELAPMKNK
IELTNKTVTF FNSNNWNTYD CNSLSRKTSS QMRDSKYQNH NVGQNVEPSS VLSPQHQISN
GLDGKCNDNY VISPNLPTTI TPTNSFTKPT PEFSNDYSLS PIQETPSSVQ SSPKRA
