AB1K8_ARATH
ID AB1K8_ARATH Reviewed; 761 AA.
AC Q93Y08; Q0WLU3; Q9ASU3; Q9LV84;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Protein ACTIVITY OF BC1 COMPLEX KINASE 8, chloroplastic {ECO:0000303|PubMed:22694836};
DE Short=ABC1-LIKE KINASE 8 {ECO:0000303|PubMed:22694836};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q9MA15};
DE AltName: Full=ABC2 homolog protein 13 {ECO:0000303|PubMed:11346655};
DE Short=AtATH13 {ECO:0000303|PubMed:11346655};
DE AltName: Full=Oxidative stress-related ABC1-like protein 1, chloroplastic {ECO:0000303|PubMed:18390807};
DE Short=AtOSA1 {ECO:0000303|PubMed:18390807};
DE Flags: Precursor;
GN Name=ABC1K8 {ECO:0000303|PubMed:22694836};
GN Synonyms=ATH13 {ECO:0000303|PubMed:11346655},
GN OSA1 {ECO:0000303|PubMed:18390807};
GN OrderedLocusNames=At5g64940 {ECO:0000312|Araport:AT5G64940};
GN ORFNames=MXK3.17 {ECO:0000312|EMBL:BAA97306.1};
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 312-761.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NOMENCLATURE.
RX PubMed=11346655; DOI=10.1074/jbc.m103104200;
RA Sanchez-Fernandez R., Davies T.G., Coleman J.O., Rea P.A.;
RT "The Arabidopsis thaliana ABC protein superfamily, a complete inventory.";
RL J. Biol. Chem. 276:30231-30244(2001).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY CADMIUM, TISSUE SPECIFICITY,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=18390807; DOI=10.1104/pp.107.110247;
RA Jasinski M., Sudre D., Schansker G., Schellenberg M., Constant S.,
RA Martinoia E., Bovet L.;
RT "AtOSA1, a member of the Abc1-like family, as a new factor in cadmium and
RT oxidative stress response.";
RL Plant Physiol. 147:719-731(2008).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=22694836; DOI=10.1016/j.tplants.2012.05.010;
RA Lundquist P.K., Davis J.I., van Wijk K.J.;
RT "ABC1K atypical kinases in plants: filling the organellar kinase void.";
RL Trends Plant Sci. 17:546-555(2012).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND RESPONSE TO IRON DEPRIVATION.
RC STRAIN=cv. Columbia;
RX PubMed=24117441; DOI=10.1111/nph.12533;
RA Manara A., DalCorso G., Leister D., Jahns P., Baldan B., Furini A.;
RT "AtSIA1 AND AtOSA1: two Abc1 proteins involved in oxidative stress
RT responses and iron distribution within chloroplasts.";
RL New Phytol. 201:452-465(2014).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=25809944; DOI=10.1093/pcp/pcv046;
RA Manara A., DalCorso G., Guzzo F., Furini A.;
RT "Loss of the atypical kinases ABC1K7 and ABC1K8 changes the lipid
RT composition of the chloroplast membrane.";
RL Plant Cell Physiol. 56:1193-1204(2015).
CC -!- FUNCTION: Involved in resistance to oxidative stress (e.g. hydrogen
CC peroxide H(2)O(2)), high light and heavy metals (e.g. cadmium ions
CC Cd(2+)) (PubMed:18390807, PubMed:24117441). Influences responses to
CC reactive oxygen species (ROS) production. Together with SIA1, regulates
CC iron distribution within the chloroplast and mediates the oxidative
CC stress response (PubMed:24117441). Together with ABC1K7, influences
CC chloroplast lipid synthesis/accumulation and modulates chloroplast
CC membrane composition in response to stress (PubMed:25809944).
CC {ECO:0000269|PubMed:18390807, ECO:0000269|PubMed:24117441,
CC ECO:0000269|PubMed:25809944}.
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:0000250|UniProtKB:Q9MA15};
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:0000250|UniProtKB:Q9MA15};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast envelope
CC {ECO:0000269|PubMed:18390807, ECO:0000269|PubMed:24117441}. Plastid,
CC chloroplast membrane {ECO:0000269|PubMed:18390807,
CC ECO:0000269|PubMed:24117441}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves and flowers, and, to a
CC lower extent, in stems, siliques and roots.
CC {ECO:0000269|PubMed:18390807, ECO:0000269|PubMed:24117441}.
CC -!- INDUCTION: By cadmium ions Cd(2+). Progressively repressed in senescent
CC leaves. Levels follow a circadian rhythm, with lower levels during the
CC night (PubMed:18390807). Down-regulated in response to iron deprivation
CC (PubMed:24117441). {ECO:0000269|PubMed:18390807,
CC ECO:0000269|PubMed:24117441}.
CC -!- DISRUPTION PHENOTYPE: Increased sensitivity toward oxidative stress
CC (e.g. hydrogen peroxide H(2)O(2)), high light and cadmium ions Cd(2+).
CC Higher superoxide dismutase activities in chloroplast and disturbed
CC expression of genes involved in the antioxidant pathway
CC (PubMed:18390807). Pale green plants. The pale green double mutant
CC atsia1 atosa1 accumulates ferritin and superoxides, exhibits an
CC increased nonphotochemical quenching (NPQ), and have a reduced
CC tolerance to reactive oxygen species (ROS) (PubMed:24117441). Lower
CC levels of the highly unsaturated lipid digalactosyldiacylglycerol
CC (DGDG) and of different forms of monogalactosyldiacylglycerol (MGDG)
CC and kaempferol. Higher levels of oxylipin-conjugated DGDG and
CC sinapates. The abc1k7 abc1k8 double mutant accumulates strong levels of
CC oxylipin-conjugated MGDG and DGDG (PubMed:25809944).
CC {ECO:0000269|PubMed:18390807, ECO:0000269|PubMed:24117441,
CC ECO:0000269|PubMed:25809944}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA97306.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB019236; BAA97306.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97972.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97973.1; -; Genomic_DNA.
DR EMBL; AF361830; AAK32842.1; -; mRNA.
DR EMBL; AY059877; AAL24359.1; -; mRNA.
DR EMBL; AY064044; AAL36400.1; -; mRNA.
DR EMBL; AY096382; AAM20023.1; -; mRNA.
DR EMBL; AK230095; BAF01914.1; -; mRNA.
DR RefSeq; NP_201299.2; NM_125893.5.
DR RefSeq; NP_851271.1; NM_180940.2.
DR AlphaFoldDB; Q93Y08; -.
DR SMR; Q93Y08; -.
DR STRING; 3702.AT5G64940.1; -.
DR iPTMnet; Q93Y08; -.
DR PaxDb; Q93Y08; -.
DR PRIDE; Q93Y08; -.
DR ProteomicsDB; 243300; -.
DR EnsemblPlants; AT5G64940.1; AT5G64940.1; AT5G64940.
DR EnsemblPlants; AT5G64940.2; AT5G64940.2; AT5G64940.
DR GeneID; 836618; -.
DR Gramene; AT5G64940.1; AT5G64940.1; AT5G64940.
DR Gramene; AT5G64940.2; AT5G64940.2; AT5G64940.
DR KEGG; ath:AT5G64940; -.
DR Araport; AT5G64940; -.
DR TAIR; locus:2177719; AT5G64940.
DR eggNOG; KOG1235; Eukaryota.
DR HOGENOM; CLU_006533_0_3_1; -.
DR InParanoid; Q93Y08; -.
DR OMA; WVAIFDE; -.
DR OrthoDB; 790106at2759; -.
DR PhylomeDB; Q93Y08; -.
DR PRO; PR:Q93Y08; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q93Y08; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; IDA:UniProtKB.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
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:0034599; P:cellular response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0055072; P:iron ion homeostasis; IMP:UniProtKB.
DR GO; GO:0010150; P:leaf senescence; IEP:UniProtKB.
DR GO; GO:0046467; P:membrane lipid biosynthetic process; IMP:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:1901031; P:regulation of response to reactive oxygen species; IMP:UniProtKB.
DR GO; GO:0046686; P:response to cadmium ion; IMP:UniProtKB.
DR GO; GO:0009644; P:response to high light intensity; IMP:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IMP:UniProtKB.
DR GO; GO:1990641; P:response to iron ion starvation; IEP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
DR InterPro; IPR004147; ABC1_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR Pfam; PF03109; ABC1; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cadmium resistance; Chloroplast; Kinase; Lipid metabolism;
KW Membrane; Nucleotide-binding; Plastid; Reference proteome; Stress response;
KW Transferase; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..57
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 58..761
FT /note="Protein ACTIVITY OF BC1 COMPLEX KINASE 8,
FT chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000441257"
FT TRANSMEM 725..745
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 288..648
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 452
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 294..302
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 315
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 680
FT /note="L -> P (in Ref. 4; BAF01914)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 761 AA; 86023 MW; 10B73693572F52E4 CRC64;
MATSSSSSSS LLLPNINFNS RQSPTITRSV SIAGIFLPRN RLSYNHNLRI RTRLIRASKD
DNVAVEDRDN AVKINGDYNG SARLNGNGSA RKSVNGDFNG SARLNGNGSL VKYVNGSVTV
ETEEVTKKRK EEVRKKRVED IGQEDAWFKN NTQQKQVEVS VTPGGRWNRF KTYSTIQRTL
EIWGFVVQFI FRTWLSNKKF SYKGGMTEEK KVLRRKVLAK WLKENILRLG PTFIKIGQQF
STRVDILPQE YVDQLSELQD QVPPFPSATA LSIVEEELGG SVEDIFDRFD YEPIAAASLG
QVHRARLKGQ EVVLKVQRPG LKDLFDIDLK NLRVIAEYLQ KVDPKSDGAK RDWVAIYDEC
ASVLYQEIDY TKEAANSELF ANNFKDLEYV KVPSIYWEYT TPQVLTMEYV PGIKINKIQA
LDQLGVDRKR LGRYAVESYL EQILSHGFFH ADPHPGNIAV DDVNGGRLIF YDFGMMGSIS
PNIREGLLEA FYGVYEKDPD KVLQAMVQMG VLVPTGDLTA VRRTALFFLN SFEERLAAQR
KEKEEIAAAE ELGFKKPLSK EEKQEKKKQR LAAIGEDLLA IAADQPFRFP ATFTFVVRAF
SVLDGIGKGL DPRFDITEIA KPYALELLRF REAGVEVVVK DLRKRWDRQS QAFYNLFRQA
DRVEKLAVVI ERLEQGDLKL RVRALESERA FQRVAAVQKT VGSAVAAGSL VNLATILYLN
SIKTPATIAY TVCAFFSLQV LIGIIKVKKF DQREKLITGT A
