Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-559292-00658
Entry Name
UniProt Accession
Theoretical PI
6.03
Molecular Weight
69639.31
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Sphingoid long chain base kinase 4
Protein Synonyms/Alias
LCB kinase 4; 2.7.1.91; Sphinganine kinase 4;
Gene Name
LCB4
Gene Synonyms/Alias
YOR171C; O3615;
Created Date
31-OCT-2006
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
43
Canonical
DSLSLLSCLSCLDDG
[1]
S-Palmitoylation
46
Canonical
SLLSCLSCLDDGTLS
[1]
S-Palmitoylation
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
NCBI Taxa ID
559292
Reference
[1] Kihara A, Kurotsu F, Sano T, Iwaki S, Igarashi Y. Long-chain base kinase Lcb4 Is anchored to the membrane through its palmitoylation by Akr1. Mol Cell Biol.2005 Nov;25(21):9189-97.[PMID:16227572]
Functional Description
Catalyzes the phosphorylation of the sphingoid long chain bases dihydrosphingosine (DHS or sphinganine) and phytosphingosine (PHS) to form dihydrosphingosine 1-phosphate (DHS-1P) and phytosphingosine 1-phosphate (PHS-1P) respectively. Involved in the biosynthesis of sphingolipids and ceramides. Required with LCB3 for an effective incorporation of DHS into ceramides through a phosphorylation-dephosphorylation cycle. Involved in heat-induced transient cell cycle arrest. Accumulation of phosphorylated sphingoid long chain bases (LCBPs) stimulates calcium influx and activates calcineurin signaling. Involved in heat-stress resistance.
Sequence Annotation
Domain: 224 363 DAGKc.
Nucleotide-binding: 234 236 ATP.
Nucleotide-binding: 324 326 ATP.
Nucleotide-binding: 589 591 ATP.
Region: 291 294 Substrate binding.
Active site: 293 293 Proton donor/acceptor.
Binding site: 266 266 ATP.
Binding site: 298 298 ATP.
Binding site: 392 392 ATP.
Binding site: 398 398 ATP.
Modified residue: 111 111 Phosphoserine.
Modified residue: 120 120 Phosphoserine.
Modified residue: 154 154 Phosphoserine.
Modified residue: 160 160 Phosphoserine.
Modified residue: 451 451 Phosphoserine; by PHO85.
Modified residue: 454 454 Phosphoserine.
Modified residue: 455 455 Phosphoserine; by PHO85.
Modified residue: 460 460 Phosphoserine.
Protein Length
624 AA.
Protein Sequence
(Canonical)
MVVQKKLRAI LTDEGVLIKS QSHHMFNKHG QLRSGDSLSL LSCLSCLDDG TLSSDGGSFD  60
EDDSLELLPL NTTIPFNRIL NAKYVNVGQK GFNNGKISSN PFQTENLSSS SENDDVENHS  120
LSNDKAPVSE SQSFPKKDKW DTKTNTVKVS PDDSQDNSPS LGIKDNQQLI ELTFAVPKGH  180
DVIPQKLTLL IDHVSRKSRA NTGEENISSG TVEEILEKSY ENSKRNRSIL VIINPHGGKG  240
TAKNLFLTKA RPILVESGCK IEIAYTKYAR HAIDIAKDLD ISKYDTIACA SGDGIPYEVI  300
NGLYRRPDRV DAFNKLAVTQ LPCGSGNAMS ISCHWTNNPS YAALCLVKSI ETRIDLMCCS  360
QPSYMNEWPR LSFLSQTYGV IAESDINTEF IRWMGPVRFN LGVAFNIIQG KKYPCEVFVK  420
YAAKSKKELK VHFLENKDKN KGCLTFEPNP SPNSSPDLLS KNNINNSTKD ELSPNFLNED  480
NFKLKYPMTE PVPRDWEKMD SELTDNLTIF YTGKMPYIAK DTKFFPAALP ADGTIDLVIT  540
DARIPVTRMT PILLSLDKGS HVLEPEVIHS KILAYKIIPK VESGLFSVDG EKFPLEPLQV  600
EIMPMLCKTL LRNGRYIDTE FESM                                         624
FASTA
(Canonical)
>LipidDB-559292-00658|Q12246
MVVQKKLRAILTDEGVLIKSQSHHMFNKHGQLRSGDSLSLLSCLSCLDDGTLSSDGGSFD
EDDSLELLPLNTTIPFNRILNAKYVNVGQKGFNNGKISSNPFQTENLSSSSENDDVENHS
LSNDKAPVSESQSFPKKDKWDTKTNTVKVSPDDSQDNSPSLGIKDNQQLIELTFAVPKGH
DVIPQKLTLLIDHVSRKSRANTGEENISSGTVEEILEKSYENSKRNRSILVIINPHGGKG
TAKNLFLTKARPILVESGCKIEIAYTKYARHAIDIAKDLDISKYDTIACASGDGIPYEVI
NGLYRRPDRVDAFNKLAVTQLPCGSGNAMSISCHWTNNPSYAALCLVKSIETRIDLMCCS
QPSYMNEWPRLSFLSQTYGVIAESDINTEFIRWMGPVRFNLGVAFNIIQGKKYPCEVFVK
YAAKSKKELKVHFLENKDKNKGCLTFEPNPSPNSSPDLLSKNNINNSTKDELSPNFLNED
NFKLKYPMTEPVPRDWEKMDSELTDNLTIFYTGKMPYIAKDTKFFPAALPADGTIDLVIT
DARIPVTRMTPILLSLDKGSHVLEPEVIHSKILAYKIIPKVESGLFSVDGEKFPLEPLQV
EIMPMLCKTLLRNGRYIDTEFESM
Gene Ontology
GO:0032541; C:cortical endoplasmic reticulum; IDA:SGD
GO:0005783; C:endoplasmic reticulum; IDA:SGD
GO:0005768; C:endosome; IEA:UniProtKB-KW
GO:0005794; C:Golgi apparatus; IDA:SGD
GO:0005886; C:plasma membrane; IDA:SGD
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0017050; F:D-erythro-sphingosine kinase activity; IDA:SGD
GO:0004143; F:diacylglycerol kinase activity; IEA:InterPro
GO:0003951; F:NAD+ kinase activity; IEA:InterPro
GO:0008481; F:sphinganine kinase activity; IEA:UniProtKB-EC
GO:0019722; P:calcium-mediated signaling; IMP:SGD
GO:0007205; P:protein kinase C-activating G-protein coupled receptor signaling pathway; IEA:InterPro
GO:0006665; P:sphingolipid metabolic process; IDA:SGD
Interpro
InterPro; IPR016064; ATP-NAD_kinase_PpnK-typ
InterPro; IPR001206; Diacylglycerol_kinase_cat_dom
Pfam
Pfam; PF00781; DAGK_cat;
SMART
SMART; SM00046; DAGKc;
PROSITE
PROSITE; PS50146; DAGK;
PRINTS