ID   LCB5_YEAST              Reviewed;         687 AA.
AC   Q06147;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 58.
DE   RecName: Full=Sphingoid long chain base kinase 5;
DE            Short=LCB kinase 5;
DE            EC=2.7.1.91;
DE   AltName: Full=Sphinganine kinase 5;
GN   Name=LCB5; OrderedLocusNames=YLR260W;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=97313267; PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
RA   Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
RA   Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
RA   Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
RA   Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
RA   Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
RA   Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
RA   Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
RA   Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
RA   Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
RA   Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
RA   Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [2]
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=9677363; DOI=10.1074/jbc.273.31.19437;
RA   Nagiec M.M., Skrzypek M.S., Nagiec E.E., Lester R.L., Dickson R.C.;
RT   "The LCB4 (YOR171c) and LCB5 (YLR260w) genes of Saccharomyces encode
RT   sphingoid long chain base kinases.";
RL   J. Biol. Chem. 273:19437-19442(1998).
RN   [3]
RP   FUNCTION.
RX   PubMed=11102354;
RA   Kim S., Fyrst H., Saba J.D.;
RT   "Accumulation of phosphorylated sphingoid long chain bases results in
RT   cell growth inhibition in Saccharomyces cerevisiae.";
RL   Genetics 156:1519-1529(2000).
RN   [4]
RP   FUNCTION.
RX   PubMed=11056159; DOI=10.1074/jbc.M007425200;
RA   Jenkins G.M., Hannun Y.A.;
RT   "Role for de novo sphingoid base biosynthesis in the heat-induced
RT   transient cell cycle arrest of Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 276:8574-8581(2001).
RN   [5]
RP   FUNCTION.
RX   PubMed=11278643; DOI=10.1074/jbc.M010221200;
RA   Birchwood C.J., Saba J.D., Dickson R.C., Cunningham K.W.;
RT   "Calcium influx and signaling in yeast stimulated by intracellular
RT   sphingosine 1-phosphate accumulation.";
RL   J. Biol. Chem. 276:11712-11718(2001).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12493772; DOI=10.1074/jbc.M209925200;
RA   Funato K., Lombardi R., Vallee B., Riezman H.;
RT   "Lcb4p is a key regulator of ceramide synthesis from exogenous long
RT   chain sphingoid base in Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 278:7325-7334(2003).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, AND MASS
RP   SPECTROMETRY.
RX   PubMed=17563356; DOI=10.1073/pnas.0701622104;
RA   Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
RT   "Proteome-wide identification of in vivo targets of DNA damage
RT   checkpoint kinases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-168; SER-169;
RP   SER-171; SER-201; SER-202 AND SER-204, AND MASS SPECTROMETRY.
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: Catalyzes the phosphorylation of the sphingoid long
CC       chain bases dihydrosphingosine (DHS or sphinganine) and
CC       phytosphingosine (PHS) to form dihydrosphingosine 1-phosphate
CC       (DHS-1P) and phytosphingosine 1-phosphate (PHS-1P) respectively.
CC       Redundant to LCB4, is only responsible for few percent of the
CC       total activity. Involved in the biosynthesis of sphingolipids and
CC       ceramides. Involved in heat-induced transient cell cycle arrest.
CC       Accumulation of phosphorylated sphingoid long chain bases (LCBPs)
CC       stimulates calcium influx and activates calcineurin signaling.
CC       Involved in heat-stress resistance.
CC   -!- CATALYTIC ACTIVITY: ATP + sphinganine = ADP + sphinganine 1-
CC       phosphate.
CC   -!- CATALYTIC ACTIVITY: ATP + phytosphingosine = ADP +
CC       phytosphingosine 1-phosphate.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2 uM for dihydrosphingosine;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral
CC       membrane protein.
CC   -!- MISCELLANEOUS: Present with 1760 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Contains 1 DAGKc domain.
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DR   EMBL; U17244; AAB67377.1; -; Genomic_DNA.
DR   PIR; S51398; S51398.
DR   RefSeq; NP_013361.1; -.
DR   IntAct; Q06147; 3.
DR   PeptideAtlas; Q06147; -.
DR   Ensembl; YLR260W; Saccharomyces cerevisiae.
DR   GeneID; 850964; -.
DR   GenomeReviews; Y13138_GR; YLR260W.
DR   KEGG; sce:YLR260W; -.
DR   NMPDR; fig|4932.3.peg.4375; -.
DR   CYGD; YLR260w; -.
DR   SGD; S000004250; LCB5.
DR   HOGENOM; Q06147; -.
DR   OMA; Q06147; ISRTSFQ.
DR   BRENDA; 2.7.1.91; 250.
DR   NextBio; 967451; -.
DR   ArrayExpress; Q06147; -.
DR   GermOnline; YLR260W; Saccharomyces cerevisiae.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005624; C:membrane fraction; IDA:SGD.
DR   GO; GO:0005625; C:soluble fraction; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0017050; F:D-erythro-sphingosine kinase activity; IDA:SGD.
DR   GO; GO:0004143; F:diacylglycerol kinase activity; IEA:InterPro.
DR   GO; GO:0008481; F:sphinganine kinase activity; IEA:EC.
DR   GO; GO:0007205; P:activation of protein kinase C activity by ...; IEA:InterPro.
DR   GO; GO:0019722; P:calcium-mediated signaling; IMP:SGD.
DR   GO; GO:0006665; P:sphingolipid metabolic process; IDA:SGD.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   ProDom; PD005043; DAGKc; 1.
DR   SMART; SM00046; DAGKc; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Golgi apparatus; Kinase;
KW   Lipid metabolism; Lipoprotein; Membrane; Nucleotide-binding;
KW   Palmitate; Phosphoprotein; Sphingolipid metabolism; Transferase.
FT   CHAIN         1    687       Sphingoid long chain base kinase 5.
FT                                /FTId=PRO_0000255957.
FT   DOMAIN      270    410       DAGKc.
FT   MOD_RES      39     39       Phosphoserine.
FT   MOD_RES      55     55       Phosphoserine.
FT   MOD_RES     168    168       Phosphoserine.
FT   MOD_RES     169    169       Phosphoserine.
FT   MOD_RES     171    171       Phosphoserine.
FT   MOD_RES     201    201       Phosphoserine.
FT   MOD_RES     202    202       Phosphoserine.
FT   MOD_RES     204    204       Phosphoserine.
FT   LIPID        91     91       S-palmitoyl cysteine (By similarity).
FT   LIPID        94     94       S-palmitoyl cysteine (By similarity).
SQ   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
//