CERK_ARATH
ID CERK_ARATH Reviewed; 608 AA.
AC Q6USK2; Q9LU45;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Ceramide kinase;
DE Short=AtCERK;
DE EC=2.7.1.138;
DE AltName: Full=Protein ACCELERATED CELL DEATH 5;
GN Name=CERK; Synonyms=ACD5; OrderedLocusNames=At5g51290;
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF GLY-412.
RX PubMed=14563678; DOI=10.1101/gad.1140503;
RA Liang H., Yao N., Song J.T., Luo S., Lu H., Greenberg J.T.;
RT "Ceramides modulate programmed cell death in plants.";
RL Genes Dev. 17:2636-2641(2003).
RN [2]
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 [3]
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).
CC -!- FUNCTION: Catalyzes specifically the phosphorylation of ceramide to
CC form ceramide 1-phosphate. Possesses high activity on ceramide analogs
CC (C6, C8 synthetic ceramides) and lower activity on C6 and C8
CC dihydroceramides. Has weak activity on natural ceramides (a mixture of
CC ceramides from bovine brain) and the synthetic substrate C2 ceramide.
CC Has very poor activity on diacylglycerol and sphingosine. Ceramide is a
CC critical sphingolipid metabolite that induces programmed cell death
CC (PCD) in plants and ceramide-1-phosphate has a PCD suppressive effect.
CC Thus, ceramide phosphorylation plays a role in the modulation of PCD
CC and CERK activity is crucial for the maintenance of cell viability.
CC {ECO:0000269|PubMed:14563678}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylsphing-4-enine + ATP = ADP + an N-acylsphing-4-enine
CC 1-phosphate + H(+); Xref=Rhea:RHEA:17929, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:52639, ChEBI:CHEBI:57674,
CC ChEBI:CHEBI:456216; EC=2.7.1.138;
CC Evidence={ECO:0000269|PubMed:14563678};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:14563678};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=24.4 uM for C8 ceramide {ECO:0000269|PubMed:14563678};
CC pH dependence:
CC Optimum pH is 8.2 (at 30 degrees Celsius).
CC {ECO:0000269|PubMed:14563678};
CC -!- INDUCTION: By infection with bacterial pathogen P.syringae.
CC {ECO:0000269|PubMed:14563678}.
CC -!- DISRUPTION PHENOTYPE: Enhanced apoptotic-like cell death late in
CC development. {ECO:0000269|PubMed:14563678}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA97392.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY362552; AAQ62904.1; -; mRNA.
DR EMBL; AB023044; BAA97392.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96062.1; -; Genomic_DNA.
DR RefSeq; NP_568756.2; NM_124508.4.
DR AlphaFoldDB; Q6USK2; -.
DR STRING; 3702.AT5G51290.1; -.
DR PaxDb; Q6USK2; -.
DR PRIDE; Q6USK2; -.
DR ProteomicsDB; 220471; -.
DR EnsemblPlants; AT5G51290.1; AT5G51290.1; AT5G51290.
DR GeneID; 835203; -.
DR Gramene; AT5G51290.1; AT5G51290.1; AT5G51290.
DR KEGG; ath:AT5G51290; -.
DR Araport; AT5G51290; -.
DR TAIR; locus:2176202; AT5G51290.
DR eggNOG; KOG1115; Eukaryota.
DR HOGENOM; CLU_013399_2_2_1; -.
DR InParanoid; Q6USK2; -.
DR OMA; HHKTTAF; -.
DR OrthoDB; 681139at2759; -.
DR PhylomeDB; Q6USK2; -.
DR BioCyc; ARA:AT5G51290-MON; -.
DR BioCyc; MetaCyc:AT5G51290-MON; -.
DR BRENDA; 2.7.1.138; 399.
DR PRO; PR:Q6USK2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q6USK2; baseline and differential.
DR Genevisible; Q6USK2; AT.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0001729; F:ceramide kinase activity; IDA:TAIR.
DR GO; GO:0102773; F:dihydroceramide kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0001727; F:lipid kinase activity; IBA:GO_Central.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0008219; P:cell death; IMP:TAIR.
DR GO; GO:0006672; P:ceramide metabolic process; IDA:TAIR.
DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central.
DR GO; GO:0043067; P:regulation of programmed cell death; IMP:TAIR.
DR GO; GO:0006665; P:sphingolipid metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.10330; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR045363; CERK_C.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR Pfam; PF19280; CERK_C; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Calcium; Kinase; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..608
FT /note="Ceramide kinase"
FT /id="PRO_0000430308"
FT DOMAIN 160..367
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT REGION 254..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 231
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 170..174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 229..232
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 230..236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 329
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT MUTAGEN 412
FT /note="G->R: In acd5; reduces activity 10-fold."
FT /evidence="ECO:0000269|PubMed:14563678"
SQ SEQUENCE 608 AA; 68462 MW; 65EB9353692D9CA6 CRC64;
MEEGRDDEYC SFSNSGDRDG GLSGCFFLDH VGQVLLSRNH DGLSWKCLDS SDCEGTTCLG
IIICENSETE IKFSDIYAVE FVSYGLVHSP KLGLRHAKEC FRERLLNTQE MYRFTVHGFQ
SSPKEPCLWN LAAFTFGHMD LQTCQSWMDQ LNYSLIKEVE RPRNLLVFVH PKSGKGNGSK
VWETVSKIFI RAKVNTKVIV TERAGHAFDV MASIQNKELH TYDGIIAVGG DGFFNEILNG
YLLSRLKVPL PPSPSDSFNS VQSRGSSSVP EPGDEVHETD QKEHYPLLPD SVQEVMNFRT
VNGSCEGIED PDHPFSSERP RFGLIPAGST DAIVMCTTGA RDPVTSALHI ILGRKLFLDA
MQVVRWKTAS TSTIEPYIRY AASFAGYGFY GDVISESEKY RWMGPKRYDY VGTKIFLKHR
SYEAEVMFEE AESENSKASL HTRSKTWPFR NTTRSEKILC RANCKICNSK VGWNSASTTL
NPCPEKTRWC RTKGRFLSIG AAVMSNRNER APDGLVVDAH LSDGFLHLIL IKDCSRPKYL
WHLTELAKRG GEPLNFEFVE YHKTRAFTFT SFGEESVWNL DGEIFEAHQL SAQVLRGLIP
LFASGPEI
