AB1K7_ARATH
ID AB1K7_ARATH Reviewed; 695 AA.
AC B9DGY1; Q8L8V3; Q8RXL3; Q93ZL4; Q9SFD6; Q9SSE3;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Protein ACTIVITY OF BC1 COMPLEX KINASE 7, chloroplastic {ECO:0000303|PubMed:22694836};
DE Short=ABC1-LIKE KINASE 7 {ECO:0000303|PubMed:22694836};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q9MA15};
DE AltName: Full=Salt-induced ABC1 kinase 1, chloroplastic {ECO:0000303|PubMed:24117441};
DE Short=AtSIA1 {ECO:0000303|PubMed:24117441};
DE Flags: Precursor;
GN Name=ABC1K7 {ECO:0000303|PubMed:22694836};
GN Synonyms=SIA1 {ECO:0000303|PubMed:24117441};
GN OrderedLocusNames=At3g07700 {ECO:0000312|Araport:AT3G07700};
GN ORFNames=F17A17.4 {ECO:0000312|EMBL:AAF21180.1},
GN MLP3.15 {ECO:0000312|EMBL:AAF13088.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia; TISSUE=Flower, and Silique;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP SUBCELLULAR LOCATION, 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. Influences
CC responses to reactive oxygen species (ROS) production. Regulates
CC plastoglobules formation in thylakoids. Together with OSA1, regulates
CC iron distribution within the chloroplast and mediates the oxidative
CC stress response (PubMed:24117441). Together with ABC1K8, influences
CC chloroplast lipid synthesis/accumulation and modulates chloroplast
CC membrane composition in response to stress (PubMed:25809944).
CC {ECO:0000269|PubMed:24117441, 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 thylakoid membrane
CC {ECO:0000269|PubMed:24117441}; Multi-pass membrane protein
CC {ECO:0000255}. Plastid, chloroplast, plastoglobule
CC {ECO:0000269|PubMed:22274653, ECO:0000305|PubMed:22694836}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves and flowers, and, to a
CC lower extent, in roots. {ECO:0000269|PubMed:24117441}.
CC -!- INDUCTION: Down-regulated in response to iron deprivation.
CC {ECO:0000269|PubMed:24117441}.
CC -!- DISRUPTION PHENOTYPE: Larger plastoglobules associated with thylakoids
CC characterized by VTE1 accumulation and high tocopherol content. The
CC pale green double mutant atsia1 atosa1 accumulates ferritin and
CC superoxides, exhibits an increased nonphotochemical quenching (NPQ),
CC and have a reduced tolerance to reactive oxygen species (ROS)
CC (PubMed:24117441). Lower levels of the highly unsaturated lipid
CC digalactosyldiacylglycerol (DGDG) and of different forms of
CC monogalactosyldiacylglycerol (MGDG) and kaempferol. The abc1k7 abc1k8
CC double mutant accumulates strong levels of oxylipin-conjugated MGDG and
CC DGDG (PubMed:25809944). {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=AAF13088.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF21180.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC009176; AAF13088.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC013483; AAF21180.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74588.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74589.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65268.1; -; Genomic_DNA.
DR EMBL; AY056806; AAL10497.1; -; mRNA.
DR EMBL; AY080823; AAL87300.1; -; mRNA.
DR EMBL; AK317324; BAH19998.1; -; mRNA.
DR EMBL; AY088788; AAM67100.1; -; mRNA.
DR RefSeq; NP_001319495.1; NM_001337729.1.
DR RefSeq; NP_566315.1; NM_111649.4.
DR RefSeq; NP_850536.1; NM_180205.2.
DR AlphaFoldDB; B9DGY1; -.
DR SMR; B9DGY1; -.
DR STRING; 3702.AT3G07700.3; -.
DR iPTMnet; B9DGY1; -.
DR PRIDE; B9DGY1; -.
DR ProteomicsDB; 245121; -.
DR EnsemblPlants; AT3G07700.1; AT3G07700.1; AT3G07700.
DR EnsemblPlants; AT3G07700.2; AT3G07700.2; AT3G07700.
DR EnsemblPlants; AT3G07700.4; AT3G07700.4; AT3G07700.
DR GeneID; 819961; -.
DR Gramene; AT3G07700.1; AT3G07700.1; AT3G07700.
DR Gramene; AT3G07700.2; AT3G07700.2; AT3G07700.
DR Gramene; AT3G07700.4; AT3G07700.4; AT3G07700.
DR KEGG; ath:AT3G07700; -.
DR Araport; AT3G07700; -.
DR eggNOG; KOG1235; Eukaryota.
DR OMA; VMFDQLF; -.
DR PhylomeDB; B9DGY1; -.
DR PRO; PR:B9DGY1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; B9DGY1; baseline and differential.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0010287; C:plastoglobule; TAS:UniProtKB.
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:0055072; P:iron ion homeostasis; IMP:UniProtKB.
DR GO; GO:0046467; P:membrane lipid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0080177; P:plastoglobule organization; IMP:UniProtKB.
DR GO; GO:1901031; P:regulation of response to reactive oxygen species; 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 1: Evidence at protein level;
KW ATP-binding; Chloroplast; Kinase; Lipid metabolism; Membrane;
KW Nucleotide-binding; Plastid; Reference proteome; Stress response;
KW Thylakoid; Transferase; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..695
FT /note="Protein ACTIVITY OF BC1 COMPLEX KINASE 7,
FT chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000441256"
FT TRANSMEM 633..653
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 659..679
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 259..589
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 421
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 265..273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 287
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 2
FT /note="A -> V (in Ref. 5; AAM67100)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="T -> I (in Ref. 3; AAL10497)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 695 AA; 78279 MW; A701A309F5A500C4 CRC64;
MAALLASQSC CYGGETARVT KAIGFSSSLE NHFTGEATQC YGSKSKRFRI EMRQSELPSK
VGINGRSVKM VPASEVVKRK DGVNGSAGKG VNGASLVSSR NINGAASTLV KAPKKTTESY
LPPPVEGVRV LPSDEGFSWA DENYSSLQRS IDVWSFVISL RIRILFDNSK WAYVGGFTEE
KQKSRRRETA SWLRESVLQL GPTFIKLGQL SSTRSDLFPR EFVDELSKLQ DRVPAFSPEK
AKRFIEAELG APISVMYKEF EEQPIAAASL GQVHRAVLHN GEKVVVKVQR PGLKKLFDID
LRNLKLIAEY FQKSESFGTN DWVGIYEECA LILYQEIDYI NEAKNADRFR RDFRNINWVR
VPLVYWDYSA MKVLTLEYVP GVKINNLDAL AARGFNRSRI ASRAIEAYLI QILKTGFFHA
DPHPGNLAID VDESIIYYDF GMMGEIKTFT RKRLLDLFYS VYEKDAKKVM QNLIDLEALQ
PTGDLSSVRR SVQFFLDNLL SQSPDQQQTL AAIGEDLFAI SQDQPFRFPS TFTFVIRAFS
TLEGIGYILD PEFSFVKVAA PYAQELLDLK QRQRSGTQLV QEIRKQADDA RSSTLSMPYR
VQRIEEFVKE LDSGDLKLRV RVLESERAAR KATILQMATM YTVLGGTLLN IGVTFSNQGS
QLVANGSFIG AGIFMLLVLR SMQRVNKLDK FEKMI
