LCKB2_ARATH
ID LCKB2_ARATH Reviewed; 364 AA.
AC O82359; Q94EZ0;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Sphingoid long-chain bases kinase 2, mitochondrial;
DE Short=AtLCBK2;
DE Short=LCB kinase 2;
DE EC=2.7.-.-;
DE Flags: Precursor;
GN Name=LCKB2; OrderedLocusNames=At2g46090; ORFNames=T3F17.26;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 SUBCELLULAR LOCATION.
RX PubMed=18643979; DOI=10.1111/j.1365-313x.2008.03596.x;
RA Marion J., Bach L., Bellec Y., Meyer C., Gissot L., Faure J.D.;
RT "Systematic analysis of protein subcellular localization and interaction
RT using high-throughput transient transformation of Arabidopsis seedlings.";
RL Plant J. 56:169-179(2008).
RN [5]
RP FUNCTION.
RX PubMed=22236066; DOI=10.1111/j.1469-8137.2011.04017.x;
RA Dutilleul C., Benhassaine-Kesri G., Demandre C., Reze N., Launay A.,
RA Pelletier S., Renou J.P., Zachowski A., Baudouin E., Guillas I.;
RT "Phytosphingosine-phosphate is a signal for AtMPK6 activation and
RT Arabidopsis response to chilling.";
RL New Phytol. 194:181-191(2012).
CC -!- FUNCTION: Involved in the production of sphingoid long-chain base
CC (LCB). Is required for the cold-induced accumulation of
CC phytosphingosine-phosphate, the regulation of the cold-responsive MPK6
CC and reduction of root growth at moderate low temperature.
CC {ECO:0000269|PubMed:22236066}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18643979}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK62459.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAL66946.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC005397; AAC62895.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10642.1; -; Genomic_DNA.
DR EMBL; AF387014; AAK62459.1; ALT_FRAME; mRNA.
DR EMBL; AY072531; AAL66946.1; ALT_FRAME; mRNA.
DR PIR; F84898; F84898.
DR RefSeq; NP_566064.1; NM_130172.5.
DR AlphaFoldDB; O82359; -.
DR SMR; O82359; -.
DR BioGRID; 4552; 1.
DR STRING; 3702.AT2G46090.1; -.
DR PaxDb; O82359; -.
DR PRIDE; O82359; -.
DR ProteomicsDB; 250727; -.
DR EnsemblPlants; AT2G46090.1; AT2G46090.1; AT2G46090.
DR GeneID; 819217; -.
DR Gramene; AT2G46090.1; AT2G46090.1; AT2G46090.
DR KEGG; ath:AT2G46090; -.
DR Araport; AT2G46090; -.
DR TAIR; locus:2063004; AT2G46090.
DR eggNOG; KOG1116; Eukaryota.
DR HOGENOM; CLU_045532_0_0_1; -.
DR InParanoid; O82359; -.
DR OMA; VNDAYFM; -.
DR OrthoDB; 950150at2759; -.
DR PhylomeDB; O82359; -.
DR PRO; PR:O82359; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82359; baseline and differential.
DR Genevisible; O82359; AT.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0042721; C:TIM22 mitochondrial import inner membrane insertion complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017050; F:D-erythro-sphingosine kinase activity; TAS:TAIR.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006671; P:phytosphingosine metabolic process; IMP:TAIR.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0009409; P:response to cold; IMP:TAIR.
DR Gene3D; 3.40.50.10330; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR005218; Diacylglycerol/lipid_kinase.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR045540; YegS/DAGK_C.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF19279; YegS_C; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
DR TIGRFAMs; TIGR00147; TIGR00147; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Mitochondrion; Nucleotide-binding; Reference proteome;
KW Stress response; Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..364
FT /note="Sphingoid long-chain bases kinase 2, mitochondrial"
FT /id="PRO_0000422118"
FT DOMAIN 49..195
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT ACT_SITE 120
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 59..61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 118..121
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 156..158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 342..344
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
SQ SEQUENCE 364 AA; 39655 MW; 93B755F11A948F0E CRC64;
MLRSTCCTPL CPFTAKQPSF LRKQQRITSD RFTFRGGGGG DAAAVVSSSG LRDLVFVVNP
QGANGRTAKE WKKLLPHLRS RLGKDCNVSE LLTSGPSHAI DITREAIRDG ADAVIAVGGD
GTLHEVVNGF FWEGKPVGYL SGEASRSTAL GLIPLGTGSD FARTFGWNND PCEAVERIAR
GMRSRIDVGV IDKEGKDLHY FINVADVHLS AKAGFYASKY KKFGNLCYVI GALQAFMGHH
NQDMRIRVNG GEWEIYPQVT ALCVGNAKYF GGGMKITPNA IPGNGNLEVV VLQNFKWYDF
VLKLHKLYNG THLSVNNVTS RSVQSIEVEE ITDSGSIYVQ SDGEHLGFLP RKFQVLPGAI
DIIS
