SPHK2_ARATH
ID SPHK2_ARATH Reviewed; 481 AA.
AC F2Y4A3; O65419;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Sphingosine kinase 2;
DE EC=2.7.1.91 {ECO:0000269|PubMed:21330371};
GN Name=SPHK2; OrderedLocusNames=At4g21534; ORFNames=F18E5.160;
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, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21330371; DOI=10.1074/jbc.m110.190892;
RA Guo L., Mishra G., Taylor K., Wang X.;
RT "Phosphatidic acid binds and stimulates Arabidopsis sphingosine kinases.";
RL J. Biol. Chem. 286:13336-13345(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22275366; DOI=10.1074/jbc.m111.274274;
RA Guo L., Mishra G., Markham J.E., Li M., Tawfall A., Welti R., Wang X.;
RT "Connections between sphingosine kinase and phospholipase D in the abscisic
RT acid signaling pathway in Arabidopsis.";
RL J. Biol. Chem. 287:8286-8296(2012).
CC -!- FUNCTION: Involved in the production of sphingolipid metabolites.
CC Phosphorylates sphingosine and various l sphingoid long-chain base
CC (LCB) products, such as phytosphingosine (PHS, 4-hydroxysphinganine),
CC 4-hydroxy-8-sphingenine, 4,8-sphingadienine and D-erythro-
CC dihydrosphingosine, but has a very few activity toward D,L-
CC threo- dihydrosphingosine. Is required for abscisic acid (ABA)
CC signaling that mediates stomatal closure, inhibition of seed
CC germination and root elongation. May function upstream of PLDALPHA1 and
CC phosphatidic acid (PA) in an amplification response to ABA that
CC mediates stomatal closure. {ECO:0000269|PubMed:21330371,
CC ECO:0000269|PubMed:22275366}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sphingoid base + ATP = a sphingoid 1-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:51496, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:76941, ChEBI:CHEBI:84410, ChEBI:CHEBI:456216;
CC EC=2.7.1.91; Evidence={ECO:0000269|PubMed:21330371};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Activated by phosphatidic acid (PA). Binding with
CC PA stimulates the activity by promoting the binding of substrate to the
CC catalytic site.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000305|PubMed:21330371};
CC Peripheral membrane protein {ECO:0000305|PubMed:21330371}.
CC Note=Associated with the tonoplast.
CC -!- TISSUE SPECIFICITY: Highly expressed in flowers and siliques and at
CC lower levels in roots, leaves and stems. {ECO:0000269|PubMed:21330371}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:22275366}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18718.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g21540 has been split into 2 genes: At4g21534 and At4g21540.; Evidence={ECO:0000305};
CC Sequence=CAB81261.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g21540 has been split into 2 genes: At4g21534 and At4g21540.; Evidence={ECO:0000305};
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DR EMBL; HQ825315; ADZ38930.1; -; mRNA.
DR EMBL; AL022603; CAA18718.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161555; CAB81261.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84464.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67721.1; -; Genomic_DNA.
DR PIR; T05162; T05162.
DR RefSeq; NP_001190787.1; NM_001203858.2.
DR RefSeq; NP_001320021.1; NM_001341495.1.
DR AlphaFoldDB; F2Y4A3; -.
DR SMR; F2Y4A3; -.
DR STRING; 3702.AT4G21534.1; -.
DR PaxDb; F2Y4A3; -.
DR PRIDE; F2Y4A3; -.
DR ProteomicsDB; 245193; -.
DR EnsemblPlants; AT4G21534.1; AT4G21534.1; AT4G21534.
DR EnsemblPlants; AT4G21534.2; AT4G21534.2; AT4G21534.
DR GeneID; 10723114; -.
DR Gramene; AT4G21534.1; AT4G21534.1; AT4G21534.
DR Gramene; AT4G21534.2; AT4G21534.2; AT4G21534.
DR KEGG; ath:AT4G21534; -.
DR Araport; AT4G21534; -.
DR TAIR; locus:6530298214; AT4G21534.
DR eggNOG; KOG1116; Eukaryota.
DR HOGENOM; CLU_013399_1_2_1; -.
DR OMA; HYISIDG; -.
DR OrthoDB; 681139at2759; -.
DR PRO; PR:F2Y4A3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F2Y4A3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017050; F:D-erythro-sphingosine kinase activity; IDA:TAIR.
DR GO; GO:0001727; F:lipid kinase activity; IBA:GO_Central.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:TAIR.
DR GO; GO:0008481; F:sphinganine kinase activity; IDA:UniProtKB.
DR GO; GO:0071215; P:cellular response to abscisic acid stimulus; IMP:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0006665; P:sphingolipid metabolic process; IDA:UniProtKB.
DR GO; GO:0046512; P:sphingosine biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.10330; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
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 PROSITE; PS50146; DAGK; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Membrane; Nucleotide-binding; Reference proteome;
KW Stress response; Transferase; Vacuole.
FT CHAIN 1..481
FT /note="Sphingosine kinase 2"
FT /id="PRO_0000422117"
FT DOMAIN 111..253
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT ACT_SITE 180
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 121..123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 178..181
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 210..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 284
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 441..443
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
SQ SEQUENCE 481 AA; 53890 MW; C7A6755F369C28BF CRC64;
MENDQFMCPT DIITGIVFID GELAMLTLTA DGELRWTEYG LRQYLSMKKD VLGFIVEGKQ
IRVKAVVEKE AGGICCGQFG GDFVRKDFVF EPLIDQNGWC YKLRQYLDSL GRPKRLLVFV
NPFGGKKSAR EIFVKEVKPL FEDADVQLEI QETKYQLHAK EFVKSMDVSK YDGIVCVSGD
GILVEVVNGL LERADWRNAL KLPIGMVPAG TGNGMIKSLL DTVGLRCCAN SATISIIRGH
KRSVDVATIA QGNTKFFSVL MLAWGLIADI DIESEKFRWM GSARIDFYAL QRIICLRRYN
GRILFLPAPG FEGYGQPASC SLYQEPHVSD KEVGYQGPET KFEDLEWREM KGPFVTIWLH
NVPWGSENTL TAPAAKFSDG YLDLIVLKNC PKLVLLSLMR QTSSGTHVES PYIVYIKVKA
FVLEPGALVD EPDKEGIIDS DGEVLARGKR TYKCDQKALM SYDKLQVTVD QGLATLFSPE
Y
