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SIGF_ARATH
ID   SIGF_ARATH              Reviewed;         547 AA.
AC   Q9LD95; Q9SJK8; Q9SMV8;
DT   11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=RNA polymerase sigma factor sigF, chloroplastic;
DE            Short=Sigma factor F;
DE            Short=Sigma-F;
DE   AltName: Full=Protein SINGLET OXYGEN-LINKED DEATH ACTIVATOR 8;
DE   AltName: Full=RNA polymerase sigma factor sig6;
DE            Short=Atsig6;
DE            Short=Sigma factor 6;
DE   Flags: Precursor;
GN   Name=SIGF; Synonyms=SIG6, SOLDAT8; OrderedLocusNames=At2g36990;
GN   ORFNames=T1J8;
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 [MRNA], AND SUBCELLULAR LOCATION.
RX   PubMed=10984613; DOI=10.1016/s0014-5793(00)01965-7;
RA   Fujiwara M., Nagashima A., Kanamaru K., Tanaka K., Takahashi H.;
RT   "Three new nuclear genes, sigD, sigE and sigF, encoding putative plastid
RT   RNA polymerase sigma factors in Aarabidopsis thaliana.";
RL   FEBS Lett. 481:47-52(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RA   Hoffmann M., Binder S.;
RT   "Arabidopsis thaliana gene for sigma factor-like protein.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
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   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 61-547.
RC   STRAIN=cv. C24;
RX   PubMed=10734058; DOI=10.1074/jbc.275.13.9215;
RA   Hakimi M.-A., Privat I., Valay J.-G., Lerbs-Mache S.;
RT   "Evolutionary conservation of C-terminal domains of primary sigma(70)-type
RT   transcription factors between plants and bacteria.";
RL   J. Biol. Chem. 275:9215-9221(2000).
RN   [7]
RP   GENE FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. Columbia; TISSUE=Seedling hypocotyl;
RX   PubMed=10946105; DOI=10.1016/s0300-9084(00)00611-8;
RA   Allison L.A.;
RT   "The role of sigma factors in plastid transcription.";
RL   Biochimie 82:537-548(2000).
RN   [8]
RP   INDUCTION BY BLUE LIGHT.
RC   STRAIN=cv. Columbia;
RX   PubMed=11959137; DOI=10.1016/s0014-5793(02)02538-3;
RA   Tsunoyama Y., Morikawa K., Shiina T., Toyoshima Y.;
RT   "Blue light specific and differential expression of a plastid sigma factor,
RT   Sig5 in Arabidopsis thaliana.";
RL   FEBS Lett. 516:225-228(2002).
RN   [9]
RP   FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION BY LIGHT.
RC   STRAIN=cv. Columbia;
RX   PubMed=15807777; DOI=10.1111/j.1365-313x.2005.02362.x;
RA   Ishizaki Y., Tsunoyama Y., Hatano K., Ando K., Kato K., Shinmyo A.,
RA   Kobori M., Takeba G., Nakahira Y., Shiina T.;
RT   "A nuclear-encoded sigma factor, Arabidopsis SIG6, recognizes sigma-70 type
RT   chloroplast promoters and regulates early chloroplast development in
RT   cotyledons.";
RL   Plant J. 42:133-144(2005).
RN   [10]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=17118361; DOI=10.1016/j.febslet.2006.11.010;
RA   Schweer J., Loschelder H., Link G.;
RT   "A promoter switch that can rescue a plant sigma factor mutant.";
RL   FEBS Lett. 580:6617-6622(2006).
RN   [11]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16905663; DOI=10.1104/pp.106.085878;
RA   Loschelder H., Schweer J., Link B., Link G.;
RT   "Dual temporal role of plastid sigma factor 6 in Arabidopsis development.";
RL   Plant Physiol. 142:642-650(2006).
RN   [12]
RP   INDUCTION BY LIGHT.
RX   PubMed=18532976; DOI=10.1111/j.1365-313x.2008.03567.x;
RA   Onda Y., Yagi Y., Saito Y., Takenaka N., Toyoshima Y.;
RT   "Light induction of Arabidopsis SIG1 and SIG5 transcripts in mature leaves:
RT   differential roles of cryptochrome 1 and cryptochrome 2 and dual function
RT   of SIG5 in the recognition of plastid promoters.";
RL   Plant J. 55:968-978(2008).
RN   [13]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19273469; DOI=10.1093/pcp/pcp036;
RA   Coll N.S., Danon A., Meurer J., Cho W.K., Apel K.;
RT   "Characterization of soldat8, a suppressor of singlet oxygen-induced cell
RT   death in Arabidopsis seedlings.";
RL   Plant Cell Physiol. 50:707-718(2009).
RN   [14]
RP   PHOSPHORYLATION AT SER-94; SER-95; SER-174; SER-176; SER-177; SER-180 AND
RP   THR-249 BY CK2, AND MUTAGENESIS OF SER-94; SER-95; 94-SER-SER-95; SER-174;
RP   SER-176; SER-177; SER-180 AND THR-249.
RX   PubMed=20088902; DOI=10.1111/j.1365-313x.2010.04138.x;
RA   Schweer J., Tuerkeri H., Link B., Link G.;
RT   "AtSIG6, a plastid sigma factor from Arabidopsis, reveals functional impact
RT   of cpCK2 phosphorylation.";
RL   Plant J. 62:192-202(2010).
RN   [15]
RP   FUNCTION, AND INTERACTION WITH DG1.
RX   PubMed=20626654; DOI=10.1111/j.1365-313x.2010.04304.x;
RA   Chi W., Mao J., Li Q., Ji D., Zou M., Lu C., Zhang L.;
RT   "Interaction of the pentatricopeptide-repeat protein DELAYED GREENING 1
RT   with sigma factor SIG6 in the regulation of chloroplast gene expression in
RT   Arabidopsis cotyledons.";
RL   Plant J. 64:14-25(2010).
CC   -!- FUNCTION: Sigma factors are initiation factors that promote the
CC       attachment of plastid-encoded RNA polymerase (PEP) to specific
CC       initiation sites and are then released. Regulates transcription in
CC       chloroplast in a DG1-dependent manner. Involved in light-dependent
CC       chloroplast development. Required during early plant development and
CC       primary leaf formation. {ECO:0000269|PubMed:15807777,
CC       ECO:0000269|PubMed:16905663, ECO:0000269|PubMed:17118361,
CC       ECO:0000269|PubMed:19273469, ECO:0000269|PubMed:20626654}.
CC   -!- SUBUNIT: Interacts (via N-terminus) with DG1 (via C-terminus).
CC       {ECO:0000269|PubMed:20626654}.
CC   -!- INTERACTION:
CC       Q9LD95; Q9LQT8: GAI; NbExp=4; IntAct=EBI-4455937, EBI-963606;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:10984613}.
CC   -!- TISSUE SPECIFICITY: Expressed in seedling, accumulating progressively.
CC       Present in leaves but not in roots. {ECO:0000269|PubMed:15807777}.
CC   -!- INDUCTION: Induced by red light. Slightly induced by blue light.
CC       {ECO:0000269|PubMed:11959137, ECO:0000269|PubMed:15807777,
CC       ECO:0000269|PubMed:18532976}.
CC   -!- PTM: Phosphorylated to acquire sigma activity; site-specific
CC       phosphorylation regulates promoter affinity. Phosphorylation at Ser-174
CC       by chloroplastic CK2 requires prior phosphorylation at Ser-177.
CC       Phosphorylation at either Ser-94, Ser-95 or Ser-174 is required for
CC       sigma activation. {ECO:0000269|PubMed:20088902}.
CC   -!- DISRUPTION PHENOTYPE: Chlorophyll-defective seedlings with reduced
CC       levels of chloroplast-encoded transcripts (e.g. atpB, atpE and rbcL).
CC       Delayed light-dependent chloroplast development. Constitutive
CC       acclimation to light stress. Suppressor of FLU disruption phenotype;
CC       seedlings missing both FLU and SIGF do not bleach when grown under non-
CC       permissive dark/light conditions. {ECO:0000269|PubMed:15807777,
CC       ECO:0000269|PubMed:16905663, ECO:0000269|PubMed:17118361,
CC       ECO:0000269|PubMed:19273469}.
CC   -!- SIMILARITY: Belongs to the sigma-70 factor family. {ECO:0000305}.
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DR   EMBL; AB029916; BAA92288.1; -; mRNA.
DR   EMBL; AJ277389; CAB89775.1; -; mRNA.
DR   EMBL; AC006922; AAD31584.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09332.1; -; Genomic_DNA.
DR   EMBL; AY059768; AAL24116.1; -; mRNA.
DR   EMBL; AY091182; AAM14121.1; -; mRNA.
DR   EMBL; AJ250812; CAB60192.1; -; mRNA.
DR   PIR; B84787; B84787.
DR   PIR; T52653; T52653.
DR   RefSeq; NP_565856.1; NM_129255.3.
DR   AlphaFoldDB; Q9LD95; -.
DR   SMR; Q9LD95; -.
DR   BioGRID; 3617; 7.
DR   IntAct; Q9LD95; 7.
DR   MINT; Q9LD95; -.
DR   STRING; 3702.AT2G36990.1; -.
DR   iPTMnet; Q9LD95; -.
DR   PaxDb; Q9LD95; -.
DR   PRIDE; Q9LD95; -.
DR   ProteomicsDB; 234579; -.
DR   EnsemblPlants; AT2G36990.1; AT2G36990.1; AT2G36990.
DR   GeneID; 818273; -.
DR   Gramene; AT2G36990.1; AT2G36990.1; AT2G36990.
DR   KEGG; ath:AT2G36990; -.
DR   Araport; AT2G36990; -.
DR   TAIR; locus:2057996; AT2G36990.
DR   eggNOG; ENOG502QVXR; Eukaryota.
DR   HOGENOM; CLU_014793_11_1_1; -.
DR   InParanoid; Q9LD95; -.
DR   OMA; IYANFRL; -.
DR   OrthoDB; 1191135at2759; -.
DR   PhylomeDB; Q9LD95; -.
DR   PRO; PR:Q9LD95; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9LD95; baseline and differential.
DR   Genevisible; Q9LD95; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009536; C:plastid; IDA:TAIR.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016987; F:sigma factor activity; IDA:TAIR.
DR   GO; GO:0071483; P:cellular response to blue light; IEP:UniProtKB.
DR   GO; GO:0071482; P:cellular response to light stimulus; IMP:UniProtKB.
DR   GO; GO:0006352; P:DNA-templated transcription, initiation; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:TAIR.
DR   GO; GO:0090351; P:seedling development; IMP:TAIR.
DR   Gene3D; 1.10.10.10; -; 2.
DR   InterPro; IPR014284; RNA_pol_sigma-70_dom.
DR   InterPro; IPR000943; RNA_pol_sigma70.
DR   InterPro; IPR007627; RNA_pol_sigma70_r2.
DR   InterPro; IPR007624; RNA_pol_sigma70_r3.
DR   InterPro; IPR007630; RNA_pol_sigma70_r4.
DR   InterPro; IPR013325; RNA_pol_sigma_r2.
DR   InterPro; IPR013324; RNA_pol_sigma_r3/r4-like.
DR   InterPro; IPR016262; RNA_pol_sigma_SigB/C/D/F.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF04542; Sigma70_r2; 1.
DR   Pfam; PF04539; Sigma70_r3; 1.
DR   Pfam; PF04545; Sigma70_r4; 1.
DR   PIRSF; PIRSF000767; RNA_pol_sigma_SigB/C/D; 1.
DR   PRINTS; PR00046; SIGMA70FCT.
DR   SUPFAM; SSF88659; SSF88659; 2.
DR   SUPFAM; SSF88946; SSF88946; 1.
DR   TIGRFAMs; TIGR02937; sigma70-ECF; 1.
DR   PROSITE; PS00715; SIGMA70_1; 1.
DR   PROSITE; PS00716; SIGMA70_2; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; DNA-binding; Phosphoprotein; Plastid; Reference proteome;
KW   Sigma factor; Transcription; Transcription regulation; Transit peptide.
FT   TRANSIT         1..55
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           56..547
FT                   /note="RNA polymerase sigma factor sigF, chloroplastic"
FT                   /id="PRO_0000418097"
FT   DNA_BIND        505..524
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          54..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          163..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           335..348
FT                   /note="Polymerase core binding"
FT   COMPBIAS        65..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..226
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         94
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000269|PubMed:20088902"
FT   MOD_RES         95
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000269|PubMed:20088902"
FT   MOD_RES         174
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000269|PubMed:20088902"
FT   MOD_RES         176
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000269|PubMed:20088902"
FT   MOD_RES         177
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000269|PubMed:20088902"
FT   MOD_RES         180
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000269|PubMed:20088902"
FT   MOD_RES         249
FT                   /note="Phosphothreonine; by CK2"
FT                   /evidence="ECO:0000269|PubMed:20088902"
FT   MUTAGEN         94..95
FT                   /note="SS->AA: Chlorophyll-defective seedlings."
FT                   /evidence="ECO:0000269|PubMed:20088902"
FT   MUTAGEN         94
FT                   /note="S->A: Loss of sigma factor activity but green
FT                   seedlings."
FT                   /evidence="ECO:0000269|PubMed:20088902"
FT   MUTAGEN         95
FT                   /note="S->A: Loss of sigma factor activity but green
FT                   seedlings."
FT                   /evidence="ECO:0000269|PubMed:20088902"
FT   MUTAGEN         174
FT                   /note="S->A: Loss of sigma factor activity and chlorophyll-
FT                   defective seedlings."
FT                   /evidence="ECO:0000269|PubMed:20088902"
FT   MUTAGEN         174
FT                   /note="S->Q: Chlorophyll-defective seedlings."
FT                   /evidence="ECO:0000269|PubMed:20088902"
FT   MUTAGEN         176
FT                   /note="S->A: Normal sigma factor activity upon
FT                   phosphorylation but green seedlings."
FT                   /evidence="ECO:0000269|PubMed:20088902"
FT   MUTAGEN         177
FT                   /note="S->A,D: Chlorophyll-defective seedlings."
FT                   /evidence="ECO:0000269|PubMed:20088902"
FT   MUTAGEN         180
FT                   /note="S->A: Loss of sigma factor activity but green
FT                   seedlings."
FT                   /evidence="ECO:0000269|PubMed:20088902"
FT   MUTAGEN         249
FT                   /note="T->A: Reduced sigma factor activity upon
FT                   phosphorylation but green seedlings."
FT                   /evidence="ECO:0000269|PubMed:20088902"
SQ   SEQUENCE   547 AA;  61797 MW;  DA75EC67B4542CB6 CRC64;
     MEATRNLVSS SPSFQTKTHL KSSYSSPSSV VMLHDQTTTP VVNSRHLNSL SRHFPASVLS
     QEPREESRPL SHALRDDRTS QLTLERRQFD ELVSSREDEK FEQQLLHSTG LWNLLISPLT
     SETKLPAVVS PLADAELCDV VALAQKALSA SKQAALLVDD TEANPSDNIK DSLSTSSSMS
     LPEKGNIVRS KRQLERRAKN RRAPKSNDVD DEGYVPQKTS AKKKYKQGAD NDDALQLFLW
     GPETKQLLTA KEEAELISHI QHLLKLEKVK TKLESQNGCE PTIGEWAEAM GISSPVLKSD
     IHRGRSSREK LITANLRLVV HIAKQYQNRG LNFQDLLQEG SMGLMKSVEK FKPQSGCRFA
     TYAYWWIRQS IRKSIFQNSR TIRLPENVYM LLGKVSEARK TCVQEGNYRP SKEELAGHVG
     VSTEKLDKLL YNTRTPLSMQ QPIWSDQDTT FQEITPDSGI ETPTMSVGKQ LMRNHVRNLL
     NVLSPKERRI IKLRFGIDGG KQRSLSEIGE IYGLSKERVR QLESRALYRL KQNMNSHGLH
     AYADLLV
 
 
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