ID   GLN3_YEAST              Reviewed;         730 AA.
AC   P18494; D3DLU0;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   27-MAR-2024, entry version 189.
DE   RecName: Full=Nitrogen regulatory protein GLN3;
GN   Name=GLN3; OrderedLocusNames=YER040W;
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].
RX   PubMed=1682800; DOI=10.1128/mcb.11.12.6216-6228.1991;
RA   Minehart P.L., Magasanik B.;
RT   "Sequence and expression of GLN3, a positive nitrogen regulatory gene of
RT   Saccharomyces cerevisiae encoding a protein with a putative zinc finger
RT   DNA-binding domain.";
RL   Mol. Cell. Biol. 11:6216-6228(1991).
RN   [2]
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   [3]
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   [4]
RP   DOMAIN.
RX   PubMed=17467953; DOI=10.1016/j.ygeno.2007.02.003;
RA   Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P., Piskacek M.;
RT   "Nine-amino-acid transactivation domain: establishment and prediction
RT   utilities.";
RL   Genomics 89:756-768(2007).
RN   [5]
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562, 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-251; SER-469 AND SER-552, 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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267; SER-285; SER-469;
RP   SER-552 AND SER-562, 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: Positive nitrogen regulatory protein. Required for the
CC       activation of transcription of a number of genes (including the
CC       allantoin pathway genes) in response to the replacement of glutamine by
CC       glutamate as source of nitrogen. Binds the nitrogen upstream activation
CC       sequence of GLN1, the gene encoding glutamine synthetase. URE2 may
CC       catalytically inactivate GLN3 in response to an increase in the
CC       intracellular concentration of glutamine.
CC   -!- INTERACTION:
CC       P18494; P23202: URE2; NbExp=2; IntAct=EBI-7657, EBI-20138;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- DOMAIN: the 9aaTAD motif is a transactivation domain present in a large
CC       number of yeast and animal transcription factors.
CC       {ECO:0000269|PubMed:17467953}.
CC   -!- MISCELLANEOUS: Present with 589 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M35267; AAA34645.1; -; Genomic_DNA.
DR   EMBL; U18796; AAB64575.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07694.1; -; Genomic_DNA.
DR   PIR; S50543; S50543.
DR   RefSeq; NP_010958.3; NM_001178931.3.
DR   AlphaFoldDB; P18494; -.
DR   SMR; P18494; -.
DR   BioGRID; 36776; 430.
DR   DIP; DIP-2353N; -.
DR   IntAct; P18494; 11.
DR   MINT; P18494; -.
DR   STRING; 4932.YER040W; -.
DR   GlyGen; P18494; 10 sites, 1 O-linked glycan (10 sites).
DR   iPTMnet; P18494; -.
DR   MaxQB; P18494; -.
DR   PaxDb; 4932-YER040W; -.
DR   PeptideAtlas; P18494; -.
DR   EnsemblFungi; YER040W_mRNA; YER040W; YER040W.
DR   GeneID; 856763; -.
DR   KEGG; sce:YER040W; -.
DR   AGR; SGD:S000000842; -.
DR   SGD; S000000842; GLN3.
DR   VEuPathDB; FungiDB:YER040W; -.
DR   eggNOG; KOG1601; Eukaryota.
DR   HOGENOM; CLU_022036_0_0_1; -.
DR   InParanoid; P18494; -.
DR   OMA; IAQLWDF; -.
DR   OrthoDB; 318925at2759; -.
DR   BioCyc; YEAST:G3O-30221-MONOMER; -.
DR   Reactome; R-SCE-9018519; Estrogen-dependent gene expression.
DR   BioGRID-ORCS; 856763; 0 hits in 13 CRISPR screens.
DR   PRO; PR:P18494; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P18494; Protein.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:SGD.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR   GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   GO; GO:0001080; P:nitrogen catabolite activation of transcription from RNA polymerase II promoter; IMP:SGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR   CDD; cd00202; ZnF_GATA; 1.
DR   Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR   InterPro; IPR039355; Transcription_factor_GATA.
DR   InterPro; IPR000679; Znf_GATA.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   PANTHER; PTHR10071:SF281; GATA-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR10071; TRANSCRIPTION FACTOR GATA FAMILY MEMBER; 1.
DR   Pfam; PF00320; GATA; 1.
DR   PRINTS; PR00619; GATAZNFINGER.
DR   SMART; SM00401; ZnF_GATA; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   PROSITE; PS00344; GATA_ZN_FINGER_1; 1.
DR   PROSITE; PS50114; GATA_ZN_FINGER_2; 1.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Metal-binding; Nitrate assimilation; Nucleus;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..730
FT                   /note="Nitrogen regulatory protein GLN3"
FT                   /id="PRO_0000083477"
FT   ZN_FING         306..330
FT                   /note="GATA-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          187..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          224..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          355..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          593..673
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          696..717
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           129..137
FT                   /note="9aaTAD"
FT   COMPBIAS        31..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..398
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        702..716
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         251
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         267
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         285
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         469
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         552
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         562
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   CONFLICT        474
FT                   /note="P -> G (in Ref. 1; AAA34645)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   730 AA;  79383 MW;  3159E1844469942E CRC64;
     MQDDPENSKL YDLLNSHLDV HGRSNEEPRQ TGDSRSQSSG NTGENEEDIA FASGLNGGTF
     DSMLEALPDD LYFTDFVSPF TAAATTSVTT KTVKDTTPAT NHMDDDIAMF DSLATTQPID
     IAASNQQNGE IAQLWDFNVD QFNMTPSNSS GSATISAPNS FTSDIPQYNH GSLGNSVSKS
     SLFPYNSSTS NSNINQPSIN NNSNTNAQSH HSFNIYKLQN NNSSSSAMNI TNNNNSNNSN
     IQHPFLKKSD SIGLSSSNTT NSVRKNSLIK PMSSTSLANF KRAASVSSSI SNMEPSGQNK
     KPLIQCFNCK TFKTPLWRRS PEGNTLCNAC GLFQKLHGTM RPLSLKSDVI KKRISKKRAK
     QTDPNIAQNT PSAPATASTS VTTTNAKPIR SRKKSLQQNS LSRVIPEEII RDNIGNTNNI
     LNVNRGGYNF NSVPSPVLMN SQSYNSSNAN FNGASNANLN SNNLMRHNSN TVTPNFRRSS
     RRSSTSSNTS SSSKSSSRSV VPILPKPSPN SANSQQFNMN MNLMNTTNNV SAGNSVASSP
     RIISSANFNS NSPLQQNLLS NSFQRQGMNI PRRKMSRNAS YSSSFMAASL QQLHEQQQVD
     VNSNTNTNSN RQNWNSSNSV STNSRSSNFV SQKPNFDIFN TPVDSPSVSR PSSRKSHTSL
     LSQQLQNSES NSFISNHKFN NRLSSDSTSP IKYEADVSAG GKISEDNSTK GSSKESSAIA
     DELDWLKFGI
//