GLNB_ARATH
ID GLNB_ARATH Reviewed; 196 AA.
AC Q9ZST4;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Nitrogen regulatory protein P-II homolog;
DE AltName: Full=Protein PII-like;
DE Flags: Precursor;
GN Name=GLB1; Synonyms=GLNB1; OrderedLocusNames=At4g01900; ORFNames=T7B11.16;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP AND INDUCTION.
RX PubMed=9811909; DOI=10.1073/pnas.95.23.13965;
RA Hsieh M.H., Lam H.M., van de Loo F.J., Coruzzi G.;
RT "A PII-like protein in Arabidopsis: putative role in nitrogen sensing.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:13965-13970(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16133214; DOI=10.1007/s00425-005-0063-5;
RA Ferrario-Mery S., Bouvet M., Leleu O., Savino G., Hodges M., Meyer C.;
RT "Physiological characterisation of Arabidopsis mutants affected in the
RT expression of the putative regulatory protein PII.";
RL Planta 223:28-39(2005).
RN [7]
RP INTERACTION WITH NAGK, AND SUBCELLULAR LOCATION.
RX PubMed=16377628; DOI=10.1074/jbc.m510945200;
RA Chen Y.M., Ferrar T.S., Lohmeier-Vogel E.M., Lohmeir-Vogel E., Morrice N.,
RA Mizuno Y., Berenger B., Ng K.K., Muench D.G., Moorhead G.B.;
RT "The PII signal transduction protein of Arabidopsis thaliana forms an
RT arginine-regulated complex with plastid N-acetyl glutamate kinase.";
RL J. Biol. Chem. 281:5726-5733(2006).
RN [8]
RP FUNCTION.
RX PubMed=18325336; DOI=10.1016/j.febslet.2008.02.056;
RA Ferrario-Mery S., Meyer C., Hodges M.;
RT "Chloroplast nitrite uptake is enhanced in Arabidopsis PII mutants.";
RL FEBS Lett. 582:1061-1066(2008).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 63-196.
RX PubMed=17279613; DOI=10.1021/bi062149e;
RA Mizuno Y., Berenger B., Moorhead G.B., Ng K.K.;
RT "Crystal structure of Arabidopsis PII reveals novel structural elements
RT unique to plants.";
RL Biochemistry 46:1477-1483(2007).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 63-196 IN COMPLEX WITH ADP AND
RP MAGNESIUM, AND SUBUNIT.
RX PubMed=17913711; DOI=10.1074/jbc.m707127200;
RA Mizuno Y., Moorhead G.B., Ng K.K.;
RT "Structural basis for the regulation of N-acetylglutamate kinase by PII in
RT Arabidopsis thaliana.";
RL J. Biol. Chem. 282:35733-35740(2007).
CC -!- FUNCTION: Participates in sensing carbon and organic nitrogen status
CC and regulates some steps of primary carbon and nitrogen metabolism.
CC Required for nitrite uptake in chloroplasts and regulates arginine
CC biosynthesis through interaction with acetylglutamate kinase (NAGK) in
CC chloroplasts. Regulates fatty acids synthesis in chloroplasts by
CC interacting with the acetyl-CoA carboxylase complex and inhibiting
CC acetyl-CoA carboxylase (ACCase) activity. {ECO:0000269|PubMed:16133214,
CC ECO:0000269|PubMed:18325336, ECO:0000269|PubMed:9811909}.
CC -!- SUBUNIT: Homodimer. Interacts with NAGK. Interaction with NAGK is
CC dependent of MgATP and inhibited by 2-oxoglutarate, arginine,
CC glutamate, citrate, and oxaloacetate. {ECO:0000269|PubMed:16377628,
CC ECO:0000269|PubMed:17913711}.
CC -!- INTERACTION:
CC Q9ZST4; Q9LLC1: BCCP2; NbExp=2; IntAct=EBI-701245, EBI-15823091;
CC Q9ZST4; Q9SCL7: NAGK; NbExp=5; IntAct=EBI-701245, EBI-701276;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|PROSITE-
CC ProRule:PRU00675, ECO:0000269|PubMed:16377628,
CC ECO:0000269|PubMed:9811909}.
CC -!- INDUCTION: By light and sucrose. Down-regulated by treatment with amino
CC acids. {ECO:0000269|PubMed:9811909}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC condition, but increased sensitivity to elevated levels of nitrite.
CC {ECO:0000269|PubMed:16133214}.
CC -!- SIMILARITY: Belongs to the P(II) protein family. {ECO:0000255|PROSITE-
CC ProRule:PRU00675}.
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DR EMBL; AF095455; AAC78333.1; -; mRNA.
DR EMBL; AC007138; AAD22652.1; -; Genomic_DNA.
DR EMBL; AL161493; CAB80683.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82094.1; -; Genomic_DNA.
DR EMBL; BT005209; AAO63273.1; -; mRNA.
DR EMBL; AK228189; BAF00143.1; -; mRNA.
DR PIR; D85024; D85024.
DR RefSeq; NP_192099.1; NM_116421.4.
DR PDB; 2O66; X-ray; 1.90 A; A/B/C=63-196.
DR PDB; 2O67; X-ray; 2.50 A; A/B/C=63-196.
DR PDB; 2RD5; X-ray; 2.51 A; C/D=63-196.
DR PDBsum; 2O66; -.
DR PDBsum; 2O67; -.
DR PDBsum; 2RD5; -.
DR AlphaFoldDB; Q9ZST4; -.
DR SMR; Q9ZST4; -.
DR BioGRID; 13502; 7.
DR DIP; DIP-35001N; -.
DR IntAct; Q9ZST4; 13.
DR STRING; 3702.AT4G01900.1; -.
DR MetOSite; Q9ZST4; -.
DR PaxDb; Q9ZST4; -.
DR PRIDE; Q9ZST4; -.
DR ProteomicsDB; 247133; -.
DR EnsemblPlants; AT4G01900.1; AT4G01900.1; AT4G01900.
DR GeneID; 828213; -.
DR Gramene; AT4G01900.1; AT4G01900.1; AT4G01900.
DR KEGG; ath:AT4G01900; -.
DR Araport; AT4G01900; -.
DR TAIR; locus:2141355; AT4G01900.
DR eggNOG; ENOG502RUKA; Eukaryota.
DR HOGENOM; CLU_082268_1_1_1; -.
DR InParanoid; Q9ZST4; -.
DR OMA; NTRVSHL; -.
DR OrthoDB; 1537660at2759; -.
DR PhylomeDB; Q9ZST4; -.
DR SABIO-RK; Q9ZST4; -.
DR EvolutionaryTrace; Q9ZST4; -.
DR PRO; PR:Q9ZST4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZST4; baseline and differential.
DR Genevisible; Q9ZST4; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009536; C:plastid; IDA:TAIR.
DR GO; GO:0010307; F:acetylglutamate kinase regulator activity; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0009718; P:anthocyanin-containing compound biosynthetic process; IMP:TAIR.
DR GO; GO:0006807; P:nitrogen compound metabolic process; ISS:TAIR.
DR GO; GO:2000013; P:regulation of arginine biosynthetic process via ornithine; TAS:TAIR.
DR GO; GO:0042304; P:regulation of fatty acid biosynthetic process; IMP:TAIR.
DR GO; GO:0006808; P:regulation of nitrogen utilization; IBA:GO_Central.
DR GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
DR GO; GO:0009744; P:response to sucrose; IEP:TAIR.
DR Gene3D; 3.30.70.120; -; 1.
DR InterPro; IPR002187; N-reg_PII.
DR InterPro; IPR011322; N-reg_PII-like_a/b.
DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR InterPro; IPR017918; N-reg_PII_CS.
DR PANTHER; PTHR30115; PTHR30115; 1.
DR Pfam; PF00543; P-II; 1.
DR PRINTS; PR00340; PIIGLNB.
DR SMART; SM00938; P-II; 1.
DR SUPFAM; SSF54913; SSF54913; 1.
DR PROSITE; PS00638; PII_GLNB_CTER; 1.
DR PROSITE; PS51343; PII_GLNB_DOM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chloroplast; Magnesium; Metal-binding;
KW Nucleotide-binding; Plastid; Reference proteome; Transcription;
KW Transcription regulation; Transit peptide.
FT TRANSIT 1..61
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 62..196
FT /note="Nitrogen regulatory protein P-II homolog"
FT /id="PRO_0000401368"
FT BINDING 108..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 110
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:17913711"
FT BINDING 161..164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT STRAND 73..81
FT /evidence="ECO:0007829|PDB:2O66"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:2O66"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:2O66"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:2O66"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:2RD5"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:2RD5"
FT STRAND 130..140
FT /evidence="ECO:0007829|PDB:2O66"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:2O66"
FT HELIX 144..155
FT /evidence="ECO:0007829|PDB:2O66"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:2O66"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:2O66"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:2O66"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:2O66"
SQ SEQUENCE 196 AA; 21275 MW; FE740EA66776F157 CRC64;
MAASMTKPIS ITSLGFYSDR KNIAFSDCIS ICSGFRHSRP SCLDLVTKSP SNNSRVLPVV
SAQISSDYIP DSKFYKVEAI VRPWRIQQVS SALLKIGIRG VTVSDVRGFG AQGGSTERHG
GSEFSEDKFV AKVKMEIVVK KDQVESVINT IIEGARTGEI GDGKIFVLPV SDVIRVRTGE
RGEKAEKMTG DMLSPS
