ID   ZPR1_YEAST              Reviewed;         486 AA.
AC   P53303; D6VUZ4; Q02807; Q02808;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 189.
DE   RecName: Full=Zinc finger chaperone ZPR1 {ECO:0000305};
GN   Name=ZPR1 {ECO:0000312|SGD:S000003443};
GN   OrderedLocusNames=YGR211W {ECO:0000312|SGD:S000003443};
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], INTERACTION WITH ELONGATION FACTOR
RP   1-ALPHA, AND SUBCELLULAR LOCATION.
RX   PubMed=9852145; DOI=10.1083/jcb.143.6.1471;
RA   Gangwani L., Mikrut M., Galcheva-Gargova Z., Davis R.J.;
RT   "Interaction of ZPR1 with translation elongation factor-1alpha in
RT   proliferating cells.";
RL   J. Cell Biol. 143:1471-1484(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9290212;
RX   DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA   Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT   "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT   chromosome VII.";
RL   Yeast 13:1077-1090(1997).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-459.
RC   STRAIN=S288c / GRF88;
RA   Song J.M., Cheung E., Rabinowitz J.C.;
RT   "Analysis of the 15.6-kb fragment encompassing the ADE3 gene.";
RL   Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-407, 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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, 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).
RN   [9]
RP   FUNCTION, INTERACTION WITH ELONGATION FACTOR 1-ALPHA, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=36630955; DOI=10.1016/j.molcel.2022.12.012;
RA   Sabbarini I.M., Reif D., McQuown A.J., Nelliat A.R., Prince J.,
RA   Membreno B.S., Wu C.C., Murray A.W., Denic V.;
RT   "Zinc-finger protein Zpr1 is a bespoke chaperone essential for eEF1A
RT   biogenesis.";
RL   Mol. Cell 83:1-14(2023).
CC   -!- FUNCTION: Acts as a protein folding chaperone for elongation factor 1-
CC       alpha. {ECO:0000269|PubMed:36630955}.
CC   -!- SUBUNIT: Interacts with elongation factor 1-alpha.
CC       {ECO:0000269|PubMed:36630955, ECO:0000269|PubMed:9852145}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9852145}. Nucleus
CC       {ECO:0000269|PubMed:9852145}. Note=Translocates to the nucleus after
CC       nutrient stimulation. {ECO:0000269|PubMed:9852145}.
CC   -!- DISRUPTION PHENOTYPE: Leads to misfolding of elongation factor 1-alpha
CC       resulting in proteotoxic stress, accumulation of cytosolic protein
CC       aggregates, increased expression of heat shock transcription factor
CC       HSF1, and inhibition of protein synthesis (PubMed:36630955). Inviable
CC       (PubMed:36630955). {ECO:0000269|PubMed:36630955}.
CC   -!- MISCELLANEOUS: Present with 39900 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the ZPR1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA85586.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAA85587.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF019769; AAC33516.1; -; Genomic_DNA.
DR   EMBL; Z72996; CAA97238.1; -; Genomic_DNA.
DR   EMBL; U40843; AAA85586.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U40843; AAA85587.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; BK006941; DAA08305.1; -; Genomic_DNA.
DR   PIR; S64534; S64534.
DR   RefSeq; NP_011727.3; NM_001181340.3.
DR   AlphaFoldDB; P53303; -.
DR   SMR; P53303; -.
DR   BioGRID; 33464; 282.
DR   DIP; DIP-4419N; -.
DR   IntAct; P53303; 7.
DR   MINT; P53303; -.
DR   STRING; 4932.YGR211W; -.
DR   iPTMnet; P53303; -.
DR   MaxQB; P53303; -.
DR   PaxDb; 4932-YGR211W; -.
DR   PeptideAtlas; P53303; -.
DR   EnsemblFungi; YGR211W_mRNA; YGR211W; YGR211W.
DR   GeneID; 853125; -.
DR   KEGG; sce:YGR211W; -.
DR   AGR; SGD:S000003443; -.
DR   SGD; S000003443; ZPR1.
DR   VEuPathDB; FungiDB:YGR211W; -.
DR   eggNOG; KOG2703; Eukaryota.
DR   GeneTree; ENSGT00390000005306; -.
DR   HOGENOM; CLU_024138_5_0_1; -.
DR   InParanoid; P53303; -.
DR   OMA; PVQSQKG; -.
DR   OrthoDB; 1113465at2759; -.
DR   BioCyc; YEAST:G3O-30893-MONOMER; -.
DR   BioGRID-ORCS; 853125; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P53303; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53303; Protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0044183; F:protein folding chaperone; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:SGD.
DR   GO; GO:0006457; P:protein folding; IDA:UniProtKB.
DR   GO; GO:0009749; P:response to glucose; IDA:UniProtKB.
DR   Gene3D; 2.60.120.1040; ZPR1, A/B domain; 2.
DR   Gene3D; 2.20.25.420; ZPR1, zinc finger domain; 2.
DR   InterPro; IPR004457; Znf_ZPR1.
DR   InterPro; IPR040141; ZPR1.
DR   InterPro; IPR042451; ZPR1_A/B_dom.
DR   InterPro; IPR042452; ZPR1_Znf1/2.
DR   NCBIfam; TIGR00310; ZPR1_znf; 2.
DR   PANTHER; PTHR10876; ZINC FINGER PROTEIN ZPR1; 1.
DR   PANTHER; PTHR10876:SF0; ZINC FINGER PROTEIN ZPR1; 1.
DR   Pfam; PF03367; zf-ZPR1; 2.
DR   SMART; SM00709; Zpr1; 2.
PE   1: Evidence at protein level;
KW   Chaperone; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..486
FT                   /note="Zinc finger chaperone ZPR1"
FT                   /id="PRO_0000119040"
FT   ZN_FING         54..86
FT                   /note="C4-type 1"
FT   ZN_FING         295..327
FT                   /note="C4-type 2"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         23
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         407
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
SQ   SEQUENCE   486 AA;  55072 MW;  F523AF8AB5B8ACA0 CRC64;
     MSEQKEDLFK PVGEAAAEVE DESIAEQNKA NDGVKLTGAQ DAMGHPVQEI ESLCMNCGKN
     GTTRLLLTSI PYFREIIIMS FDCPHCGFKN CEIQPASQIQ EKGSRYVLKV ECREDFNRQV
     IKSETATCKF VELDIEIPAK RGQLTTVEGL LSEMIDDLSQ DQEMRKSIDE ALYKKIDDFI
     QKVKSYINCE PNTIPITFIL DDPAGNSWIE YKPGEPQHKW SHTQYVRTDE QNVQVGIITR
     DQLEQRRQEQ LKQLANRERN PSESVKVGSA NPQFLSDATD IENFNNEVQT FRASCPSCTQ
     ECETHMKPVN IPHFKEVIIM STVCDHCGYK SNEVKTGGAI PDKGRRITLY CDDAADLSRD
     ILKSETCSMV IPELHLDIQE GTLGGRFTTL EGLLRQVYEE LESRIFTQTS DSMDEATKAR
     WVEFFAKLKE AIAGKVKFTV IMEDPLAGSY IQNVYAPDPD PNMTIEDYER TKEQNEDLGL
     SDIKVE
//