SCKL2_ARATH
ID SCKL2_ARATH Reviewed; 614 AA.
AC F4I0K2; Q9C978; Q9LQA2;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Fructokinase-like 2, chloroplastic {ECO:0000303|PubMed:20511297};
DE AltName: Full=pfkB-type carbohydrate kinase family protein 1 {ECO:0000303|PubMed:16326926};
DE Flags: Precursor;
GN Name=FLN2 {ECO:0000303|PubMed:20511297};
GN Synonyms=PFKB1 {ECO:0000303|PubMed:16326926};
GN OrderedLocusNames=At1g69200 {ECO:0000312|Araport:AT1G69200};
GN ORFNames=F23O10.21 {ECO:0000312|EMBL:AAG52502.1},
GN F4N2.16 {ECO:0000312|EMBL:AAF27059.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16326926; DOI=10.1105/tpc.105.036392;
RA Pfalz J., Liere K., Kandlbinder A., Dietz K.-J., Oelmueller R.;
RT "pTAC2, -6, and -12 are components of the transcriptionally active plastid
RT chromosome that are required for plastid gene expression.";
RL Plant Cell 18:176-197(2006).
RN [4]
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 [5]
RP FUNCTION, INTERACTION WITH CITRX, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP CYS-208; CYS-209 AND 208-CYS-CYS-209.
RX PubMed=20511297; DOI=10.1105/tpc.109.071001;
RA Arsova B., Hoja U., Wimmelbacher M., Greiner E., Ustun S., Melzer M.,
RA Petersen K., Lein W., Bornke F.;
RT "Plastidial thioredoxin z interacts with two fructokinase-like proteins in
RT a thiol-dependent manner: evidence for an essential role in chloroplast
RT development in Arabidopsis and Nicotiana benthamiana.";
RL Plant Cell 22:1498-1515(2010).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=22770232; DOI=10.1186/1471-2229-12-102;
RA Gilkerson J., Perez-Ruiz J.M., Chory J., Callis J.;
RT "The plastid-localized pfkB-type carbohydrate kinases FRUCTOKINASE-LIKE 1
RT and 2 are essential for growth and development of Arabidopsis thaliana.";
RL BMC Plant Biol. 12:102-102(2012).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH FLN1 AND PTAC5.
RC STRAIN=cv. Columbia;
RX PubMed=24019900; DOI=10.1371/journal.pone.0073092;
RA Huang C., Yu Q.-B., Lv R.-H., Yin Q.-Q., Chen G.-Y., Xu L., Yang Z.-N.;
RT "The reduced plastid-encoded polymerase-dependent plastid gene expression
RT leads to the delayed greening of the Arabidopsis fln2 mutant.";
RL PLoS ONE 8:E73092-E73092(2013).
CC -!- FUNCTION: Required for proper chloroplast development, most likely
CC through regulating plastid-encoded polymerase (PEP) dependent
CC chloroplast transcription. Acts as a component of the transcriptionally
CC active plastid chromosome that is required for plastid gene expression.
CC {ECO:0000269|PubMed:16326926, ECO:0000269|PubMed:20511297,
CC ECO:0000269|PubMed:22770232, ECO:0000269|PubMed:24019900}.
CC -!- SUBUNIT: Interacts with CITRX/TRXz (PubMed:20511297). Binds to FLN1 and
CC PTAC5. Associates with the plastid-encoded RNA polymerase (PEP) complex
CC (PubMed:24019900). {ECO:0000269|PubMed:20511297,
CC ECO:0000269|PubMed:24019900}.
CC -!- INTERACTION:
CC F4I0K2; Q9M7X9: CITRX; NbExp=3; IntAct=EBI-9823671, EBI-9823626;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:20511297}.
CC -!- DISRUPTION PHENOTYPE: Plants display chlorosis prior to leaf expansion,
CC but exhibit slow greening, remain autotrophic, can grow to maturity,
CC and set viable seed (PubMed:22770232). Albino phenotype of seedlings
CC grown on sucrose-free medium associated with reduced plastid-encoded
CC RNA polymerase (PEP)-dependent gene expression and altered chloroplast
CC development. Delayed greening of seedlings grown on sucrose-containing
CC medium (PubMed:24019900). {ECO:0000269|PubMed:22770232,
CC ECO:0000269|PubMed:24019900}.
CC -!- MISCELLANEOUS: RNAi plants display abnormal plastids lacking internal
CC membrane structures. {ECO:0000269|PubMed:20511297}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF27059.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC008262; AAF27059.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC018364; AAG52502.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34893.2; -; Genomic_DNA.
DR PIR; A96716; A96716.
DR RefSeq; NP_177080.3; NM_105587.6.
DR AlphaFoldDB; F4I0K2; -.
DR SMR; F4I0K2; -.
DR BioGRID; 28472; 12.
DR IntAct; F4I0K2; 1.
DR STRING; 3702.AT1G69200.1; -.
DR iPTMnet; F4I0K2; -.
DR PaxDb; F4I0K2; -.
DR PRIDE; F4I0K2; -.
DR ProteomicsDB; 232692; -.
DR EnsemblPlants; AT1G69200.1; AT1G69200.1; AT1G69200.
DR GeneID; 843251; -.
DR Gramene; AT1G69200.1; AT1G69200.1; AT1G69200.
DR KEGG; ath:AT1G69200; -.
DR Araport; AT1G69200; -.
DR TAIR; locus:2026465; AT1G69200.
DR eggNOG; KOG2855; Eukaryota.
DR HOGENOM; CLU_023435_0_0_1; -.
DR InParanoid; F4I0K2; -.
DR OMA; DDEYGQA; -.
DR OrthoDB; 918144at2759; -.
DR PhylomeDB; F4I0K2; -.
DR PRO; PR:F4I0K2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I0K2; baseline and differential.
DR Genevisible; F4I0K2; AT.
DR GO; GO:0042644; C:chloroplast nucleoid; IDA:TAIR.
DR GO; GO:0000427; C:plastid-encoded plastid RNA polymerase complex; IMP:UniProtKB.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0009658; P:chloroplast organization; IMP:UniProtKB.
DR GO; GO:0009662; P:etioplast organization; IMP:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0042793; P:plastid transcription; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
DR Pfam; PF00294; PfkB; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Kinase; Plastid; Reference proteome; Transcription;
KW Transcription regulation; Transferase; Transit peptide.
FT TRANSIT 1..44
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 45..614
FT /note="Fructokinase-like 2, chloroplastic"
FT /id="PRO_0000430870"
FT REGION 47..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..563
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 208..209
FT /note="CC->AA: Abolishes interaction with CITRX."
FT /evidence="ECO:0000269|PubMed:20511297"
FT MUTAGEN 208
FT /note="C->A: Strongly reduces the interaction with CITRX."
FT /evidence="ECO:0000269|PubMed:20511297"
FT MUTAGEN 209
FT /note="C->A: Strongly reduces the interaction with CITRX."
FT /evidence="ECO:0000269|PubMed:20511297"
SQ SEQUENCE 614 AA; 68980 MW; D5A1F341886042C3 CRC64;
MASLSFTQFL SFPRCNADVP CLLQSHGFVK FRGERWNGKQ SFSMAAGRRK LSESAPLEEE
GNDGNGAVVG KKPSKSVKRT TKKKVVVKDE PLEEISEFLV DNDDVLDKES IVSALKPKKT
RTRKKAAAAS SDVEEVKTEK KVRRKRTVKK DKDVEDDLAT IMDAEVSDVE EALAVESTDT
ESEEEEIDLS KHEGEDISHT YGWPPLVCCF GSAQHAFVPS GRPANRLLDY ELHERMRDAK
WAPEKYIRAP GGCAGGVAIA LASLGGKVAF MGKLGADDYG QAMLYYLNVC KVQTRSVKID
GKRVTACSTM KISKRGRLKS TCIKPCAEDS LSKSEINVDV LKEAKMFYFS THSLLDKKMM
STTIQAIKIS KQLGNVIFYD LNLPLPLWHS SEETKSFIQE VWNLADVIEI TKQELEFLCG
IEPTEEFDTE NNDISKFVHY PPETVEQLWH ENLKVLFVTN GTSKIHYYTK EHNGAVSGME
DVPITPFTRD MSASGDGIVA GLIRMLTVQP DLMNNKGYLE RTARYAIECG IIDQWLLAQT
RGYPPKDDME EEEDDEEEDE VESDPNGIRS ITEKEYRTSK PYDEPDGPYV MKPVEEREYK
KLELVGSMFE DGSL
