GLN3_YEAST
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 03-AUG-2022, entry version 182.
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}.
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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; 425.
DR DIP; DIP-2353N; -.
DR IntAct; P18494; 11.
DR MINT; P18494; -.
DR STRING; 4932.YER040W; -.
DR iPTMnet; P18494; -.
DR MaxQB; P18494; -.
DR PaxDb; P18494; -.
DR PRIDE; P18494; -.
DR EnsemblFungi; YER040W_mRNA; YER040W; YER040W.
DR GeneID; 856763; -.
DR KEGG; sce:YER040W; -.
DR SGD; S000000842; GLN3.
DR VEuPathDB; FungiDB:YER040W; -.
DR eggNOG; KOG1601; Eukaryota.
DR HOGENOM; CLU_022036_0_0_1; -.
DR InParanoid; P18494; -.
DR OMA; IQCFNCK; -.
DR BioCyc; YEAST:G3O-30221-MON; -.
DR Reactome; R-SCE-9018519; Estrogen-dependent gene expression.
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; IMP:SGD.
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 GO; GO:0036278; P:positive regulation of transcription from RNA polymerase II promoter in response to nitrogen starvation; IMP:SGD.
DR GO; GO:2001159; P:regulation of protein localization by the Cvt pathway; IMP:SGD.
DR CDD; cd00202; ZnF_GATA; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR039355; Transcription_factor_GATA.
DR InterPro; IPR000679; Znf_GATA.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR10071; PTHR10071; 1.
DR Pfam; PF00320; GATA; 1.
DR PRINTS; PR00619; GATAZNFINGER.
DR SMART; SM00401; ZnF_GATA; 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
