GUN4C_ARATH
ID GUN4C_ARATH Reviewed; 265 AA.
AC Q9LX31; Q8VZR4;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Tetrapyrrole-binding protein, chloroplastic;
DE AltName: Full=Genomes uncoupled 4;
DE Flags: Precursor;
GN Name=GUN4; OrderedLocusNames=At3g59400; ORFNames=F25L23_260;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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 [3]
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CHLH, AND MUTANT GUN4-1.
RX PubMed=12574634; DOI=10.1126/science.1079978;
RA Larkin R.M., Alonso J.M., Ecker J.R., Chory J.;
RT "GUN4, a regulator of chlorophyll synthesis and intracellular signaling.";
RL Science 299:902-906(2003).
RN [5]
RP INDUCTION BY LIGHT.
RX PubMed=18846290; DOI=10.1039/b802596g;
RA Stephenson P.G., Terry M.J.;
RT "Light signalling pathways regulating the Mg-chelatase branchpoint of
RT chlorophyll synthesis during de-etiolation in Arabidopsis thaliana.";
RL Photochem. Photobiol. Sci. 7:1243-1252(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP FUNCTION.
RX PubMed=23011401; DOI=10.1007/s11103-012-9965-3;
RA Du S.Y., Zhang X.F., Lu Z., Xin Q., Wu Z., Jiang T., Lu Y., Wang X.F.,
RA Zhang D.P.;
RT "Roles of the different components of magnesium chelatase in abscisic acid
RT signal transduction.";
RL Plant Mol. Biol. 80:519-537(2012).
CC -!- FUNCTION: Regulates chlorophyll synthesis and plastid-to-nucleus signal
CC transduction by binding both the product and the substrate of Mg-
CC chelatase, an enzyme that produces magnesium-protoporphyrin IX (Mg-
CC Proto). Activates also Mg-chelatase. Neither binds abscisic acid (ABA)
CC nor is involved in ABA signaling. {ECO:0000269|PubMed:12574634,
CC ECO:0000269|PubMed:23011401}.
CC -!- SUBUNIT: Interacts with CHLH, the protoporphyrin IX-binding subunit of
CC Mg-chelatase. Monomer or extremely compact dimer.
CC {ECO:0000269|PubMed:12574634}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:12574634}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12574634}. Note=Might be bound to membranes by
CC specific protein-protein interactions.
CC -!- INDUCTION: Up-regulated by light. {ECO:0000269|PubMed:18846290}.
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DR EMBL; AL356014; CAB91610.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79917.1; -; Genomic_DNA.
DR EMBL; AY063918; AAL36274.1; -; mRNA.
DR EMBL; AY150510; AAN13026.1; -; mRNA.
DR PIR; T49008; T49008.
DR RefSeq; NP_191499.1; NM_115802.4.
DR PDB; 7E2R; X-ray; 2.30 A; A/B=70-265.
DR PDBsum; 7E2R; -.
DR AlphaFoldDB; Q9LX31; -.
DR SMR; Q9LX31; -.
DR BioGRID; 10424; 1.
DR STRING; 3702.AT3G59400.1; -.
DR iPTMnet; Q9LX31; -.
DR PaxDb; Q9LX31; -.
DR PRIDE; Q9LX31; -.
DR ProteomicsDB; 230175; -.
DR EnsemblPlants; AT3G59400.1; AT3G59400.1; AT3G59400.
DR GeneID; 825109; -.
DR Gramene; AT3G59400.1; AT3G59400.1; AT3G59400.
DR KEGG; ath:AT3G59400; -.
DR Araport; AT3G59400; -.
DR TAIR; locus:2081207; AT3G59400.
DR eggNOG; ENOG502QWGS; Eukaryota.
DR HOGENOM; CLU_067449_0_0_1; -.
DR InParanoid; Q9LX31; -.
DR OMA; LINQDFR; -.
DR PhylomeDB; Q9LX31; -.
DR PRO; PR:Q9LX31; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LX31; baseline and differential.
DR Genevisible; Q9LX31; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019899; F:enzyme binding; IPI:TAIR.
DR GO; GO:0046906; F:tetrapyrrole binding; IDA:TAIR.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; TAS:TAIR.
DR GO; GO:0010019; P:chloroplast-nucleus signaling pathway; IMP:TAIR.
DR GO; GO:0043085; P:positive regulation of catalytic activity; TAS:TAIR.
DR CDD; cd16383; GUN4; 1.
DR InterPro; IPR008629; GUN4-like.
DR InterPro; IPR037215; GUN4-like_sf.
DR PANTHER; PTHR34800; PTHR34800; 1.
DR Pfam; PF05419; GUN4; 1.
DR SUPFAM; SSF140869; SSF140869; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chlorophyll biosynthesis; Chloroplast; Membrane; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..69
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 70..265
FT /note="Tetrapyrrole-binding protein, chloroplastic"
FT /id="PRO_0000021389"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 88
FT /note="L->F: In gun4-1; decreases the protein stability."
FT CONFLICT 251
FT /note="G -> E (in Ref. 3; AAL36274)"
FT /evidence="ECO:0000305"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:7E2R"
FT HELIX 93..106
FT /evidence="ECO:0007829|PDB:7E2R"
FT HELIX 110..115
FT /evidence="ECO:0007829|PDB:7E2R"
FT HELIX 120..125
FT /evidence="ECO:0007829|PDB:7E2R"
FT HELIX 128..140
FT /evidence="ECO:0007829|PDB:7E2R"
FT TURN 141..144
FT /evidence="ECO:0007829|PDB:7E2R"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:7E2R"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:7E2R"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:7E2R"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:7E2R"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:7E2R"
FT HELIX 214..220
FT /evidence="ECO:0007829|PDB:7E2R"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:7E2R"
SQ SEQUENCE 265 AA; 29665 MW; 80C321C78CDE0255 CRC64;
MATTNSLHHH HHSSPSYTHH RNNLHCQSHF GPTSLSLKQP TSAATFSLIC SASSTSSSTT
AVSAVSTTNA SATTAETATI FDVLENHLVN QNFRQADEET RRLLIQISGE AAVKRGYVFF
SEVKTISPED LQAIDNLWIK HSDGRFGYSV QRKIWLKVKK DFTRFFVKVE WMKLLDTEVV
QYNYRAFPDE FKWELNDETP LGHLPLTNAL RGTQLLKCVL SHPAFATADD NSGETEDELN
RGVAVAKEQA GVGADKRVFK TNYSF
