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PP178_ARATH
ID   PP178_ARATH             Reviewed;         918 AA.
AC   Q9SIC9;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Pentatricopeptide repeat-containing protein GUN1, chloroplastic {ECO:0000305};
DE   AltName: Full=Pentatricopeptide repeat-containing protein At2g31400 {ECO:0000305};
DE   AltName: Full=Protein GENOMES UNCOUPLED 1 {ECO:0000303|PubMed:17395793};
DE   Flags: Precursor;
GN   Name=GUN1 {ECO:0000303|PubMed:17395793};
GN   OrderedLocusNames=At2g31400 {ECO:0000312|Araport:AT2G31400};
GN   ORFNames=T28P16.11 {ECO:0000312|EMBL:AAD26479.1};
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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] OF 544-918.
RC   STRAIN=cv. Columbia;
RX   PubMed=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
RN   [4]
RP   GENE FAMILY.
RX   PubMed=15269332; DOI=10.1105/tpc.104.022236;
RA   Lurin C., Andres C., Aubourg S., Bellaoui M., Bitton F., Bruyere C.,
RA   Caboche M., Debast C., Gualberto J., Hoffmann B., Lecharny A., Le Ret M.,
RA   Martin-Magniette M.-L., Mireau H., Peeters N., Renou J.-P., Szurek B.,
RA   Taconnat L., Small I.;
RT   "Genome-wide analysis of Arabidopsis pentatricopeptide repeat proteins
RT   reveals their essential role in organelle biogenesis.";
RL   Plant Cell 16:2089-2103(2004).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=17395793; DOI=10.1126/science. 1140516;
RA   Koussevitzky S., Nott A., Mockler T.C., Hong F., Sachetto-Martins G.,
RA   Surpin M., Lim J., Mittler R., Chory J.;
RT   "Signals from chloroplasts converge to regulate nuclear gene expression.";
RL   Science 316:715-719(2007).
RN   [6]
RP   FUNCTION.
RX   PubMed=19140931; DOI=10.1111/j.1469-8137.2008.02729.x;
RA   Ruckle M.E., Larkin R.M.;
RT   "Plastid signals that affect photomorphogenesis in Arabidopsis thaliana are
RT   dependent on GENOMES UNCOUPLED 1 and cryptochrome 1.";
RL   New Phytol. 182:367-379(2009).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20605896; DOI=10.1093/jxb/erq186;
RA   Cottage A., Mott E.K., Kempster J.A., Gray J.C.;
RT   "The Arabidopsis plastid-signalling mutant gun1 (genomes uncoupled1) shows
RT   altered sensitivity to sucrose and abscisic acid and alterations in early
RT   seedling development.";
RL   J. Exp. Bot. 61:3773-3786(2010).
RN   [8]
RP   FUNCTION.
RX   PubMed=21673514; DOI=10.4161/psb.6.4.14900;
RA   Cottage A., Gray J.C.;
RT   "Timing the switch to phototrophic growth: a possible role of GUN1.";
RL   Plant Signal. Behav. 6:578-582(2011).
CC   -!- FUNCTION: Involved in nuclear gene expression via the retrograde
CC       plastid-to-nucleus signaling (PubMed:17395793, PubMed:19140931,
CC       PubMed:20605896, PubMed:21673514). Plastid signals that depend on GUN1
CC       can affect photomorphogenesis developments, such as cotyledon opening
CC       and expansion, anthocyanin biosynthesis, and hypocotyl elongation
CC       (PubMed:19140931, PubMed:21673514). {ECO:0000269|PubMed:17395793,
CC       ECO:0000269|PubMed:19140931, ECO:0000269|PubMed:20605896,
CC       ECO:0000269|PubMed:21673514}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:17395793}.
CC   -!- DISRUPTION PHENOTYPE: Defective in retrograde plastid-to-nucleus
CC       signaling. {ECO:0000269|PubMed:20605896}.
CC   -!- SIMILARITY: Belongs to the PPR family. P subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Pentatricopeptide repeat proteins;
CC       URL="https://ppr.plantenergy.uwa.edu.au";
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DR   EMBL; AC007169; AAD26479.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08542.1; -; Genomic_DNA.
DR   EMBL; BX819946; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; C84720; C84720.
DR   RefSeq; NP_180698.1; NM_128697.3.
DR   AlphaFoldDB; Q9SIC9; -.
DR   SMR; Q9SIC9; -.
DR   STRING; 3702.AT2G31400.1; -.
DR   PaxDb; Q9SIC9; -.
DR   PRIDE; Q9SIC9; -.
DR   ProteomicsDB; 249147; -.
DR   EnsemblPlants; AT2G31400.1; AT2G31400.1; AT2G31400.
DR   GeneID; 817698; -.
DR   Gramene; AT2G31400.1; AT2G31400.1; AT2G31400.
DR   KEGG; ath:AT2G31400; -.
DR   Araport; AT2G31400; -.
DR   TAIR; locus:2061310; AT2G31400.
DR   eggNOG; KOG4197; Eukaryota.
DR   HOGENOM; CLU_002706_49_5_1; -.
DR   InParanoid; Q9SIC9; -.
DR   OrthoDB; 1344243at2759; -.
DR   PhylomeDB; Q9SIC9; -.
DR   PRO; PR:Q9SIC9; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SIC9; baseline and differential.
DR   Genevisible; Q9SIC9; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR   GO; GO:0010019; P:chloroplast-nucleus signaling pathway; IMP:UniProtKB.
DR   GO; GO:0031930; P:mitochondria-nucleus signaling pathway; IMP:TAIR.
DR   Gene3D; 1.25.40.10; -; 5.
DR   Gene3D; 3.30.1370.110; -; 1.
DR   InterPro; IPR002885; Pentatricopeptide_repeat.
DR   InterPro; IPR002625; Smr_dom.
DR   InterPro; IPR036063; Smr_dom_sf.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   Pfam; PF01535; PPR; 2.
DR   Pfam; PF13041; PPR_2; 4.
DR   Pfam; PF13812; PPR_3; 1.
DR   SMART; SM00463; SMR; 1.
DR   SUPFAM; SSF160443; SSF160443; 1.
DR   TIGRFAMs; TIGR00756; PPR; 9.
DR   PROSITE; PS51375; PPR; 12.
DR   PROSITE; PS50828; SMR; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Plastid; Reference proteome; Repeat; Transit peptide.
FT   TRANSIT         1..41
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           42..918
FT                   /note="Pentatricopeptide repeat-containing protein GUN1,
FT                   chloroplastic"
FT                   /id="PRO_0000356037"
FT   REPEAT          232..266
FT                   /note="PPR 1"
FT   REPEAT          267..301
FT                   /note="PPR 2"
FT   REPEAT          302..337
FT                   /note="PPR 3"
FT   REPEAT          338..372
FT                   /note="PPR 4"
FT   REPEAT          373..407
FT                   /note="PPR 5"
FT   REPEAT          408..442
FT                   /note="PPR 6"
FT   REPEAT          443..477
FT                   /note="PPR 7"
FT   REPEAT          478..512
FT                   /note="PPR 8"
FT   REPEAT          513..547
FT                   /note="PPR 9"
FT   REPEAT          548..582
FT                   /note="PPR 10"
FT   REPEAT          583..619
FT                   /note="PPR 11"
FT   DOMAIN          781..873
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00321"
FT   REGION          1..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   918 AA;  101624 MW;  15627FA285D37D8B CRC64;
     MASTPPHWVT TTNNHRPWLP QRPRPGRSVT SAPPSSSASV SSAHLSQTTP NFSPLQTPKS
     DFSGRQSTRF VSPATNNHRQ TRQNPNYNHR PYGASSSPRG SAPPPSSVAT VAPAQLSQPP
     NFSPLQTPKS DLSSDFSGRR STRFVSKMHF GRQKTTMATR HSSAAEDALQ NAIDFSGDDE
     MFHSLMLSFE SKLCGSDDCT YIIRELGNRN ECDKAVGFYE FAVKRERRKN EQGKLASAMI
     STLGRYGKVT IAKRIFETAF AGGYGNTVYA FSALISAYGR SGLHEEAISV FNSMKEYGLR
     PNLVTYNAVI DACGKGGMEF KQVAKFFDEM QRNGVQPDRI TFNSLLAVCS RGGLWEAARN
     LFDEMTNRRI EQDVFSYNTL LDAICKGGQM DLAFEILAQM PVKRIMPNVV SYSTVIDGFA
     KAGRFDEALN LFGEMRYLGI ALDRVSYNTL LSIYTKVGRS EEALDILREM ASVGIKKDVV
     TYNALLGGYG KQGKYDEVKK VFTEMKREHV LPNLLTYSTL IDGYSKGGLY KEAMEIFREF
     KSAGLRADVV LYSALIDALC KNGLVGSAVS LIDEMTKEGI SPNVVTYNSI IDAFGRSATM
     DRSADYSNGG SLPFSSSALS ALTETEGNRV IQLFGQLTTE SNNRTTKDCE EGMQELSCIL
     EVFRKMHQLE IKPNVVTFSA ILNACSRCNS FEDASMLLEE LRLFDNKVYG VVHGLLMGQR
     ENVWLQAQSL FDKVNEMDGS TASAFYNALT DMLWHFGQKR GAELVALEGR SRQVWENVWS
     DSCLDLHLMS SGAARAMVHA WLLNIRSIVY EGHELPKVLS ILTGWGKHSK VVGDGALRRA
     VEVLLRGMDA PFHLSKCNMG RFTSSGSVVA TWLRESATLK LLILHDHITT ATATTTTMKS
     TDQQQRKQTS FALQPLLL
 
 
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