AB1K3_ARATH
ID AB1K3_ARATH Reviewed; 711 AA.
AC Q9MA15; Q94BV0;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Protein ACTIVITY OF BC1 COMPLEX KINASE 3, chloroplastic {ECO:0000303|PubMed:23673981};
DE Short=ABC1-LIKE KINASE 3 {ECO:0000303|PubMed:23673981};
DE EC=2.7.-.- {ECO:0000255|PROSITE-ProRule:PRU00159};
DE EC=2.7.11.1 {ECO:0000269|PubMed:23632854};
DE AltName: Full=Protein REPRESSOR OF BDR1 {ECO:0000303|PubMed:25882344};
DE Flags: Precursor;
GN Name=ABC1K3 {ECO:0000303|PubMed:23673981};
GN Synonyms=RBD1 {ECO:0000303|PubMed:25882344};
GN OrderedLocusNames=At1g79600 {ECO:0000312|Araport:AT1G79600};
GN ORFNames=F20B17.3 {ECO:0000312|EMBL:AAF68128.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=16461379; DOI=10.1104/pp.105.076083;
RA Ytterberg A.J., Peltier J.-B., van Wijk K.J.;
RT "Protein profiling of plastoglobules in chloroplasts and chromoplasts. A
RT surprising site for differential accumulation of metabolic enzymes.";
RL Plant Physiol. 140:984-997(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=22274653; DOI=10.1104/pp.111.193144;
RA Lundquist P.K., Poliakov A., Bhuiyan N.H., Zybailov B., Sun Q.,
RA van Wijk K.J.;
RT "The functional network of the Arabidopsis plastoglobule proteome based on
RT quantitative proteomics and genome-wide coexpression analysis.";
RL Plant Physiol. 158:1172-1192(2012).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH ABC1K1.
RC STRAIN=cv. Columbia;
RX PubMed=23673981; DOI=10.1105/tpc.113.111120;
RA Lundquist P.K., Poliakov A., Giacomelli L., Friso G., Appel M.,
RA McQuinn R.P., Krasnoff S.B., Rowland E., Ponnala L., Sun Q., van Wijk K.J.;
RT "Loss of plastoglobule kinases ABC1K1 and ABC1K3 causes conditional
RT degreening, modified prenyl-lipids, and recruitment of the jasmonic acid
RT pathway.";
RL Plant Cell 25:1818-1839(2013).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=23632854; DOI=10.1104/pp.113.218644;
RA Martinis J., Glauser G., Valimareanu S., Kessler F.;
RT "A chloroplast ABC1-like kinase regulates vitamin E metabolism in
RT Arabidopsis.";
RL Plant Physiol. 162:652-662(2013).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ALA-82; GLY-167; ALA-243;
RP ALA-301; PRO-320; GLY-362; GLY-399 AND PRO-405, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=25882344; DOI=10.1016/j.molp.2015.04.003;
RA Huang H., Yang M., Su Y., Qu L., Deng X.W.;
RT "Arabidopsis atypical kinases ABC1K1 and ABC1K3 act oppositely to cope with
RT photodamage under red light.";
RL Mol. Plant 8:1122-1124(2015).
RN [9]
RP INTERACTION WITH PGM48.
RX PubMed=27895226; DOI=10.1105/tpc.16.00745;
RA Bhuiyan N.H., Friso G., Rowland E., Majsec K., van Wijk K.J.;
RT "The plastoglobule-localized metallopeptidase PGM48 is a positive regulator
RT of senescence in Arabidopsis thaliana.";
RL Plant Cell 28:3020-3037(2016).
CC -!- FUNCTION: Kinase that can phosphorylate the tocopherol cyclase VTE1, a
CC key enzyme of tocopherol (vitamin E) metabolism and involved in the
CC recycling of oxidated alpha-tocopherol quinone, possibly stabilizing it
CC at plastoglobules. Regulates also membrane prenylquinone composition
CC (PubMed:23632854). Required for photooxidative stress responses to
CC prevent photosystem II core and chlorophyll degradations. Together with
CC ABC1K1, contributes to plastoglobule (PG) function in prenyl-lipid
CC metabolism, stress response, and thylakoid remodeling (PubMed:23673981,
CC PubMed:23632854). Promotes photodamage of chloroplasts under continuous
CC red light, thus working in opposition to ABC1K1 (PubMed:25882344).
CC {ECO:0000269|PubMed:23632854, ECO:0000269|PubMed:23673981,
CC ECO:0000269|PubMed:25882344}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:23632854};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:23632854};
CC -!- SUBUNIT: Interacts with ABC1K1 in plastoglobules (PG)
CC (PubMed:23673981). Interacts with PGM48 (PubMed:27895226).
CC {ECO:0000269|PubMed:23673981, ECO:0000269|PubMed:27895226}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast, plastoglobule
CC {ECO:0000269|PubMed:16461379, ECO:0000269|PubMed:22274653}. Plastid,
CC chloroplast {ECO:0000269|PubMed:25882344}. Note=Colocalizes with the
CC chlorophyll autofluorescence of mature chloroplasts. In cotyledons of
CC seedlings grown in continuous red light, only observed in the
CC chloroplasts losing chlorophyll autofluorescence.
CC {ECO:0000269|PubMed:25882344}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9MA15-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9MA15-2; Sequence=VSP_025067;
CC -!- DISRUPTION PHENOTYPE: Suppression of the bleaching and dwarf phenotypes
CC of plants lacking ABC1K1 in red light, associated with the rescue of
CC chlorophylls and carotenoid contents as well as D1 protein level,
CC product of psbA, one of the four core subunits of the photosystem II
CC (PSII) (PubMed:25882344). Slight reduction of nonphotochemical
CC quenching after high light intensity treatment. Abnormal chloroplast
CC ultrastructure with slightly scattered thylakoid grana and reduced
CC starch granules accumulation in normal light. In high light (HL),
CC stronger phenotype with large scattered grana and extensive vacuolation
CC as well as an increase in plastoglobule size and higher number of
CC plastoglobule clusters, but no starch granule (PubMed:23632854).
CC Impaired for the production of plastochromanol-8 (a plastoquinone-
CC derived lipid antioxidant) and the redox recycling of alpha-tocopherol,
CC but normal tocopherol. Increased accumulation of VTE1 and PAP1/FBN1a
CC transcripts, but reduced levels of proteins fibrillin-1a (PAP1/FBN1a)
CC and tocopherol cyclase (VTE1) due to protein instability and leading to
CC abnormal accumulation of the alpha-tocopherol (alpha-T)
CC oxidative- derivate alpha-tocopherol quinone (alpha-TQ)
CC (PubMed:23632854). Conditional light stress phenotype in the double
CC mutant abc1k1 abc1k3 that displays rapid chlorosis upon high light
CC stress and slower, but irreversible, senescence-like phenotype during
CC moderate light stress, drought or nitrogen limitation, but not cold
CC stress. This senescence-like phenotype is associated with the
CC degradation of the photosystem II core and up-regulation of chlorophyll
CC degradation. During light stress, modified prenyl-lipid composition in
CC plastoglobules (PG) probably due to reduced VTE1 activity and loss of
CC CCD4, as well as abnormal recruitment of plastid jasmonate biosynthesis
CC enzymes in PG (PubMed:23673981). {ECO:0000269|PubMed:23632854,
CC ECO:0000269|PubMed:23673981, ECO:0000269|PubMed:25882344}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC kinase family. {ECO:0000305}.
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DR EMBL; AC010793; AAF68128.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36271.1; -; Genomic_DNA.
DR EMBL; AY141992; AAM98256.1; -; mRNA.
DR EMBL; AY064971; AAL57626.1; -; mRNA.
DR EMBL; AY039869; AAK63973.1; -; mRNA.
DR RefSeq; NP_565214.1; NM_106608.4. [Q9MA15-1]
DR AlphaFoldDB; Q9MA15; -.
DR SMR; Q9MA15; -.
DR STRING; 3702.AT1G79600.1; -.
DR PaxDb; Q9MA15; -.
DR PRIDE; Q9MA15; -.
DR ProteomicsDB; 243299; -. [Q9MA15-1]
DR EnsemblPlants; AT1G79600.1; AT1G79600.1; AT1G79600. [Q9MA15-1]
DR GeneID; 844298; -.
DR Gramene; AT1G79600.1; AT1G79600.1; AT1G79600. [Q9MA15-1]
DR KEGG; ath:AT1G79600; -.
DR Araport; AT1G79600; -.
DR TAIR; locus:2019838; AT1G79600.
DR eggNOG; KOG1235; Eukaryota.
DR HOGENOM; CLU_006533_4_1_1; -.
DR InParanoid; Q9MA15; -.
DR OMA; AYPYFAR; -.
DR PhylomeDB; Q9MA15; -.
DR PRO; PR:Q9MA15; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9MA15; baseline and differential.
DR Genevisible; Q9MA15; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0010287; C:plastoglobule; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IMP:UniProtKB.
DR GO; GO:0009658; P:chloroplast organization; IMP:UniProtKB.
DR GO; GO:0080177; P:plastoglobule organization; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0050821; P:protein stabilization; IMP:TAIR.
DR GO; GO:1902171; P:regulation of tocopherol cyclase activity; IMP:TAIR.
DR GO; GO:0009644; P:response to high light intensity; IMP:UniProtKB.
DR GO; GO:0080183; P:response to photooxidative stress; IMP:UniProtKB.
DR GO; GO:0010114; P:response to red light; IMP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IMP:UniProtKB.
DR InterPro; IPR004147; ABC1_dom.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF03109; ABC1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Chloroplast; Kinase; Nucleotide-binding;
KW Plastid; Reference proteome; Stress response; Transferase; Transit peptide.
FT TRANSIT 1..42
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 43..711
FT /note="Protein ACTIVITY OF BC1 COMPLEX KINASE 3,
FT chloroplastic"
FT /id="PRO_0000286522"
FT DOMAIN 216..546
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 379
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 222..230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..142
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_025067"
FT MUTAGEN 82
FT /note="A->S: In rbd1-5; suppression of bdr1-1 and bdr1-2
FT bleaching and dwarf phenotypes."
FT /evidence="ECO:0000269|PubMed:25882344"
FT MUTAGEN 167
FT /note="G->D: In rbd1-6; suppression of bdr1-1 and bdr1-2
FT bleaching and dwarf phenotypes."
FT /evidence="ECO:0000269|PubMed:25882344"
FT MUTAGEN 243
FT /note="A->T: In rbd1-8; suppression of bdr1-1 and bdr1-2
FT bleaching and dwarf phenotypes."
FT /evidence="ECO:0000269|PubMed:25882344"
FT MUTAGEN 301
FT /note="A->V: In rbd1-3; suppression of bdr1-1 and bdr1-2
FT bleaching and dwarf phenotypes."
FT /evidence="ECO:0000269|PubMed:25882344"
FT MUTAGEN 320
FT /note="P->L: In rbd1-9; suppression of bdr1-1 and bdr1-2
FT bleaching and dwarf phenotypes."
FT /evidence="ECO:0000269|PubMed:25882344"
FT MUTAGEN 362
FT /note="G->E: In rbd1-11; suppression of bdr1-1 and bdr1-2
FT bleaching and dwarf phenotypes."
FT /evidence="ECO:0000269|PubMed:25882344"
FT MUTAGEN 399
FT /note="G->D: In rbd1-1; suppression of bdr1-1 and bdr1-2
FT bleaching and dwarf phenotypes."
FT /evidence="ECO:0000269|PubMed:25882344"
FT MUTAGEN 405
FT /note="P->S: In rbd1-12; suppression of bdr1-1 and bdr1-2
FT bleaching and dwarf phenotypes."
FT /evidence="ECO:0000269|PubMed:25882344"
SQ SEQUENCE 711 AA; 79022 MW; 3F1C53BBC64764CC CRC64;
MSLVVGQSLG LTLVGDGLSL RNSKINVGKS KFFSVNRRRL ARAALVQARP KEDGAAASPS
PSSRPASVVQ YRRADLADDL QAEARALGRA IDASIYSPEL IARKHGSQPF KALRRSLEIL
GALGGFALKL GIDQKQGNLE KNMKKRAIEL RRIFTRLGPT FVKLGQGLST RPDLCPPDYL
EELAELQDAL PTFPDAEAFA CIERELDLSL ETIFSSVSPE PIAAASLGQV YKAQLRYSGQ
VVAVKVQRPG IEEAIGLDFY LIRGVGKLIN KYVDFITTDV LTLIDEFACR VYQELNYVQE
AQNARRFKKL YADKADVLVP DIFWDYTSRK VLTMEWVEGT KLNEQLAIES QGLKVLDLVN
TGIQCSLRQL LEYGFFHADP HPGNLLATPD GKLAFLDFGM MSETPEEARF AIIGHVVHLV
NRDYEAMARD YYALKFLSPD VDVTPIIPAL RDFFDDALNY TVSELNFKTL VDGLGAVFYQ
YPFNVPPYYA LILRSLTVLE GLALYADPNF KVLAASYPYF AKRLLTDPNP YLRDALIELL
FKDGKFRWNR LENLLQQGSK DRDFSAKDAL QPVLKLLLDP NGEELRLLVI KEAVRVSEAI
ALGTVVDTYN SLPEFLRSLV FNGNGNGPLT MSTAELQSTL ELRDQVSRIW GLLQSSESFD
PAILQPILQV LQQPEARRLG GRVAGGVGQR LAARFLQQLL RATTPSSAPS P
