SCKL1_ARATH
ID SCKL1_ARATH Reviewed; 471 AA.
AC Q9M394;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Fructokinase-like 1, chloroplastic {ECO:0000312|EMBL:AEE79187.1};
DE AltName: Full=PEP-associated protein 6 {ECO:0000303|PubMed:21949211};
DE AltName: Full=pfkB-type carbohydrate kinase family protein 2 {ECO:0000303|PubMed:16326926};
DE Flags: Precursor;
GN Name=FLN1 {ECO:0000312|EMBL:AEE79187.1};
GN Synonyms=PAP6 {ECO:0000303|PubMed:21949211},
GN PFKB2 {ECO:0000303|PubMed:16326926};
GN OrderedLocusNames=At3g54090 {ECO:0000312|Araport:AT3G54090};
GN ORFNames=F24B22.50 {ECO:0000312|EMBL:CAB70983.1};
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=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, 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 [5]
RP FUNCTION, INTERACTION WITH CITRX, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP CYS-105; CYS-106 AND 105-CYS-CYS-106.
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 FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND DISRUPTION PHENOTYPE.
RX PubMed=21949211; DOI=10.1104/pp.111.184515;
RA Steiner S., Schroeter Y., Pfalz J., Pfannschmidt T.;
RT "Identification of essential subunits in the plastid-encoded RNA polymerase
RT complex reveals building blocks for proper plastid development.";
RL Plant Physiol. 157:1043-1055(2011).
RN [7]
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 [8]
RP INTERACTION WITH PTAC7.
RX PubMed=23082802; DOI=10.1111/j.1399-3054.2012.01718.x;
RA Yu Q.-B., Lu Y., Ma Q., Zhao T.-T., Huang C., Zhao H.-F., Zhang X.-L.,
RA Lv R.-H., Yang Z.-N.;
RT "TAC7, an essential component of the plastid transcriptionally active
RT chromosome complex, interacts with FLN1, TAC10, TAC12 and TAC14 to regulate
RT chloroplast gene expression in Arabidopsis thaliana.";
RL Physiol. Plantarum 148:408-421(2013).
RN [9]
RP INTERACTION WITH FLN2, AND HOMODIMERIZATION.
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:21949211, ECO:0000269|PubMed:22770232}.
CC -!- SUBUNIT: Interacts with CITRX/TRXz (PubMed:20511297). Interacts with
CC PTAC7 (PubMed:23082802). Self-interacts. Binds to FLN2. Associates with
CC the plastid-encoded RNA polymerase (PEP) complex (PubMed:24019900).
CC {ECO:0000269|PubMed:20511297, ECO:0000269|PubMed:23082802,
CC ECO:0000269|PubMed:24019900}.
CC -!- INTERACTION:
CC Q9M394; Q9M7X9: CITRX; NbExp=3; IntAct=EBI-9823647, EBI-9823626;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:20511297}.
CC -!- DISRUPTION PHENOTYPE: Albino seedlings leading to lethality.
CC {ECO:0000269|PubMed:21949211, ECO:0000269|PubMed:22770232}.
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}.
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DR EMBL; AL132957; CAB70983.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79187.1; -; Genomic_DNA.
DR EMBL; AY093161; AAM13160.1; -; mRNA.
DR EMBL; AY128817; AAM91217.1; -; mRNA.
DR PIR; T47568; T47568.
DR RefSeq; NP_190977.1; NM_115269.4.
DR AlphaFoldDB; Q9M394; -.
DR SMR; Q9M394; -.
DR BioGRID; 9893; 3.
DR IntAct; Q9M394; 1.
DR STRING; 3702.AT3G54090.1; -.
DR PaxDb; Q9M394; -.
DR PRIDE; Q9M394; -.
DR ProteomicsDB; 232800; -.
DR EnsemblPlants; AT3G54090.1; AT3G54090.1; AT3G54090.
DR GeneID; 824576; -.
DR Gramene; AT3G54090.1; AT3G54090.1; AT3G54090.
DR KEGG; ath:AT3G54090; -.
DR Araport; AT3G54090; -.
DR TAIR; locus:2080270; AT3G54090.
DR eggNOG; KOG2855; Eukaryota.
DR HOGENOM; CLU_023435_1_0_1; -.
DR InParanoid; Q9M394; -.
DR OMA; DDGIDFP; -.
DR OrthoDB; 918144at2759; -.
DR PhylomeDB; Q9M394; -.
DR BioCyc; ARA:AT3G54090-MON; -.
DR PRO; PR:Q9M394; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M394; baseline and differential.
DR Genevisible; Q9M394; AT.
DR GO; GO:0042644; C:chloroplast nucleoid; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0042793; P:plastid transcription; IMP:TAIR.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
DR Pfam; PF00294; PfkB; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR PROSITE; PS00583; PFKB_KINASES_1; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Kinase; Plastid; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..38
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 39..471
FT /note="Fructokinase-like 1, chloroplastic"
FT /id="PRO_0000430869"
FT REGION 36..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 105..106
FT /note="CC->AA: Abolishes interaction with CITRX."
FT /evidence="ECO:0000269|PubMed:20511297"
FT MUTAGEN 105
FT /note="C->A: Does not affect the interaction with CITRX."
FT /evidence="ECO:0000269|PubMed:20511297"
FT MUTAGEN 106
FT /note="C->A: Strongly reduces the interaction with CITRX."
FT /evidence="ECO:0000269|PubMed:20511297"
SQ SEQUENCE 471 AA; 53781 MW; 0433E3D43830ADA2 CRC64;
MASLLIFPHL HHFDSSLDRR EVLVVRHSQA SRRFLTPKAS INGSGITNGA AAETTSKPSR
KGRKKKQTST VIEKDNTETD PELNPELADY DDGIEFPYDD PPLVCCFGAV QKEFVPVVRV
HDNPMHPDMY SQWKMLQWDP PEFGRAPGGP PSNVAISHVR LGGRAAFMGK VGEDDFGDEL
VLMMNQERVQ TRAVKFDENS KTACTRVKIK FKDGKMMAET VKEPPEDSLF ASELNLAVLK
EARIFHFNSE VLTSPTMQST LFTAIQWSKK FGGLIFFDLN LPLPLWRSRN ETRKLIKKAW
NEANIIEVSQ QELEFLLDED YYERRRNYTP QYFAEDFDQT KNRRDYYHYT PEEIKSLWHD
KLKLLVVTDG TLRLHYYTPT FDGVVIGTED VLITPFTCDR TGSGDAVVAG IMRKLTTCPE
MFEDQDVMER QLRFAVAAGI IAQWTIGAVR GFPTESATQN LKEQVYVPSM W
