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Sphingoid long chain base kinase 5 (LCB kinase 5) (EC 2.7.1.91) (Sphinganine kinase 5)

 LCB5_YEAST              Reviewed;         687 AA.
Q06147; D6VYQ7;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
23-MAY-2018, entry version 138.
RecName: Full=Sphingoid long chain base kinase 5;
Short=LCB kinase 5;
EC=2.7.1.91 {ECO:0000269|PubMed:9677363};
AltName: Full=Sphinganine kinase 5;
Name=LCB5; OrderedLocusNames=YLR260W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=9677363; DOI=10.1074/jbc.273.31.19437;
Nagiec M.M., Skrzypek M.S., Nagiec E.E., Lester R.L., Dickson R.C.;
"The LCB4 (YOR171c) and LCB5 (YLR260w) genes of Saccharomyces encode
sphingoid long chain base kinases.";
J. Biol. Chem. 273:19437-19442(1998).
[4]
FUNCTION.
PubMed=11102354;
Kim S., Fyrst H., Saba J.D.;
"Accumulation of phosphorylated sphingoid long chain bases results in
cell growth inhibition in Saccharomyces cerevisiae.";
Genetics 156:1519-1529(2000).
[5]
FUNCTION.
PubMed=11056159; DOI=10.1074/jbc.M007425200;
Jenkins G.M., Hannun Y.A.;
"Role for de novo sphingoid base biosynthesis in the heat-induced
transient cell cycle arrest of Saccharomyces cerevisiae.";
J. Biol. Chem. 276:8574-8581(2001).
[6]
FUNCTION.
PubMed=11278643; DOI=10.1074/jbc.M010221200;
Birchwood C.J., Saba J.D., Dickson R.C., Cunningham K.W.;
"Calcium influx and signaling in yeast stimulated by intracellular
sphingosine 1-phosphate accumulation.";
J. Biol. Chem. 276:11712-11718(2001).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12493772; DOI=10.1074/jbc.M209925200;
Funato K., Lombardi R., Vallee B., Riezman H.;
"Lcb4p is a key regulator of ceramide synthesis from exogenous long
chain sphingoid base in Saccharomyces cerevisiae.";
J. Biol. Chem. 278:7325-7334(2003).
[8]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: 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.
Redundant to LCB4, is only responsible for few percent of the
total activity. Involved in the biosynthesis of sphingolipids and
ceramides. 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. {ECO:0000269|PubMed:11056159,
ECO:0000269|PubMed:11102354, ECO:0000269|PubMed:11278643,
ECO:0000269|PubMed:12493772, ECO:0000269|PubMed:9677363}.
-!- CATALYTIC ACTIVITY: ATP + a sphingoid base = ADP + a sphingoid
base 1-phosphate. {ECO:0000269|PubMed:9677363}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2 uM for dihydrosphingosine {ECO:0000269|PubMed:9677363};
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000269|PubMed:12493772}; Peripheral membrane protein
{ECO:0000269|PubMed:12493772}.
-!- MISCELLANEOUS: Present with 1760 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-----------------------------------------------------------------------
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EMBL; U17244; AAB67377.1; -; Genomic_DNA.
EMBL; BK006945; DAA09573.1; -; Genomic_DNA.
PIR; S51398; S51398.
RefSeq; NP_013361.1; NM_001182147.1.
ProteinModelPortal; Q06147; -.
SMR; Q06147; -.
BioGrid; 31528; 165.
IntAct; Q06147; 1.
MINT; Q06147; -.
STRING; 4932.YLR260W; -.
SwissLipids; SLP:000000110; -.
iPTMnet; Q06147; -.
MaxQB; Q06147; -.
PaxDb; Q06147; -.
PRIDE; Q06147; -.
EnsemblFungi; YLR260W; YLR260W; YLR260W.
GeneID; 850964; -.
KEGG; sce:YLR260W; -.
EuPathDB; FungiDB:YLR260W; -.
SGD; S000004250; LCB5.
GeneTree; ENSGT00690000101761; -.
HOGENOM; HOG000207396; -.
InParanoid; Q06147; -.
KO; K04718; -.
OMA; MEPEHAK; -.
OrthoDB; EOG092C1LMZ; -.
BioCyc; MetaCyc:YLR260W-MONOMER; -.
BioCyc; YEAST:YLR260W-MONOMER; -.
Reactome; R-SCE-1483206; Glycerophospholipid biosynthesis.
Reactome; R-SCE-1660661; Sphingolipid de novo biosynthesis.
Reactome; R-SCE-1660662; Glycosphingolipid metabolism.
Reactome; R-SCE-390471; Association of TriC/CCT with target proteins during biosynthesis.
Reactome; R-SCE-5218921; VEGFR2 mediated cell proliferation.
PRO; PR:Q06147; -.
Proteomes; UP000002311; Chromosome XII.
GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0017050; F:D-erythro-sphingosine kinase activity; IDA:SGD.
GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
GO; GO:0008481; F:sphinganine kinase activity; IEA:UniProtKB-EC.
GO; GO:0019722; P:calcium-mediated signaling; IMP:SGD.
GO; GO:0009408; P:response to heat; IDA:SGD.
GO; GO:0006665; P:sphingolipid metabolic process; IDA:SGD.
Gene3D; 3.40.50.10330; -; 1.
InterPro; IPR017438; ATP-NAD_kinase_N.
InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
Pfam; PF00781; DAGK_cat; 1.
SMART; SM00046; DAGKc; 1.
SUPFAM; SSF111331; SSF111331; 2.
PROSITE; PS50146; DAGK; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Golgi apparatus; Kinase;
Lipid metabolism; Lipoprotein; Membrane; Nucleotide-binding;
Palmitate; Reference proteome; Sphingolipid metabolism; Transferase.
CHAIN 1 687 Sphingoid long chain base kinase 5.
/FTId=PRO_0000255957.
DOMAIN 266 405 DAGKc. {ECO:0000255|PROSITE-
ProRule:PRU00783}.
NP_BIND 276 278 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00783}.
NP_BIND 366 368 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00783}.
NP_BIND 652 654 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00783}.
REGION 333 336 Substrate binding. {ECO:0000250}.
ACT_SITE 335 335 Proton donor/acceptor. {ECO:0000250}.
BINDING 308 308 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00783}.
BINDING 340 340 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00783}.
BINDING 434 434 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00783}.
BINDING 440 440 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00783}.
LIPID 91 91 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 94 94 S-palmitoyl cysteine. {ECO:0000250}.
SEQUENCE 687 AA; 77566 MW; 205C32F3570042FA CRC64;
MTLKPSKRRK GRSRHSRKKQ ITSAILTEEG IMIKAKPSSP YTYANRMADK RSRSSIDNIS
RTSFQSNISR TSFQSNSDNN SIFETASLIS CVTCLSDTDT IDRSETSTTD TSKDDLSANP
KLHYPSVNGQ LPANTVIPYG RILDARYIEK EPLHYYDANS SPSSPLSSSM SNISEKCDLD
ELESSQKKER KGNSLSRGSN SSSSLLTSRS PFTKLVEVIF ARPRRHDVVP KRVSLYIDYK
PHSSSHLKEE DDLVEEILKR SYKNTRRNKS IFVIINPFGG KGKAKKLFMT KAKPLLLASR
CSIEVVYTKY PGHAIEIARE MDIDKYDTIA CASGDGIPHE VINGLYQRPD HVKAFNNIAI
TEIPCGSGNA MSVSCHWTNN PSYSTLCLIK SIETRIDLMC CSQPSYAREH PKLSFLSQTY
GLIAETDINT EFIRWMGPAR FELGVAFNII QKKKYPCEIY VKYAAKSKNE LKNHYLEHKN
KGSLEFQHIT MNKDNEDCDN YNYENEYETE NEDEDEDADA DDEDSHLISR DLADSSADQI
KEEDFKIKYP LDEGIPSDWE RLDPNISNNL GIFYTGKMPY VAADTKFFPA ALPSDGTMDM
VITDARTSLT RMAPILLGLD KGSHVLQPEV LHSKILAYKI IPKLGNGLFS VDGEKFPLEP
LQVEIMPRLC KTLLRNGRYV DTDFDSM


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