ID   SPHK1_MOUSE             Reviewed;         382 AA.
AC   Q8CI15; O88886; Q3U2E3; Q91ZN3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   05-MAY-2009, entry version 49.
DE   RecName: Full=Sphingosine kinase 1;
DE            Short=SPK 1;
DE            Short=SK 1;
DE            EC=2.7.1.91;
GN   Name=Sphk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   MEDLINE=98395082; PubMed=9726979; DOI=10.1074/jbc.273.37.23722;
RA   Kohama T., Olivera A., Edsall L., Nagiec M.M., Dickson R., Spiegel S.;
RT   "Molecular cloning and functional characterization of murine
RT   sphingosine kinase.";
RL   J. Biol. Chem. 273:23722-23728(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA   Thompson D., Pyne S.;
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RG   The mouse genome sequencing consortium;
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   INTERACTION WITH ACY1.
RX   PubMed=15196915; DOI=10.1016/j.febslet.2004.04.093;
RA   Maceyka M., Nava V.E., Milstien S., Spiegel S.;
RT   "Aminoacylase 1 is a sphingosine kinase 1-interacting protein.";
RL   FEBS Lett. 568:30-34(2004).
CC   -!- FUNCTION: Catalyzes the phosphorylation of sphingosine to form
CC       sphingosine 1-phosphate (SPP), a lipid mediator with both intra-
CC       and extracellular functions. Also acts on D-erythro-sphingosine
CC       and to a lesser extent sphinganine, but not other lipids, such as
CC       D,L-threo-dihydrosphingosine, N,N-dimethylsphingosine,
CC       diacylglycerol, ceramide, or phosphatidylinositol (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + sphinganine = ADP + sphinganine 1-
CC       phosphate.
CC   -!- CATALYTIC ACTIVITY: ATP + sphingosine = ADP + sphingosine 1-
CC       phosphate.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- SUBUNIT: Binds to calmodulin. Interacts with SPHKAP (By
CC       similarity). Interacts with ACY1.
CC   -!- INTERACTION:
CC       O70433:Fhl2; NbExp=1; IntAct=EBI-985291, EBI-299379;
CC       P06241:FYN (xeno); NbExp=1; IntAct=EBI-985291, EBI-515315;
CC       P07948:LYN (xeno); NbExp=1; IntAct=EBI-985291, EBI-79452;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8CI15-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CI15-2; Sequence=VSP_033448;
CC       Name=3;
CC         IsoId=Q8CI15-3; Sequence=VSP_033449;
CC   -!- SIMILARITY: Contains 1 DAGKc domain.
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DR   EMBL; AF068749; AAC61698.1; -; mRNA.
DR   EMBL; AF415213; AAL07499.1; -; mRNA.
DR   EMBL; AK155332; BAE33198.1; -; mRNA.
DR   EMBL; AK160900; BAE36079.1; -; mRNA.
DR   EMBL; AL645851; CAM17116.1; -; Genomic_DNA.
DR   EMBL; AL645851; CAM17117.1; -; Genomic_DNA.
DR   EMBL; BC037710; AAH37710.1; -; mRNA.
DR   IPI; IPI00407664; -.
DR   IPI; IPI00649112; -.
DR   IPI; IPI00762556; -.
DR   RefSeq; NP_079643.2; -.
DR   UniGene; Mm.20944; -.
DR   IntAct; Q8CI15; 3.
DR   PhosphoSite; Q8CI15; -.
DR   PRIDE; Q8CI15; -.
DR   Ensembl; ENSMUSG00000061878; Mus musculus.
DR   GeneID; 20698; -.
DR   MGI; MGI:1316649; Sphk1.
DR   HOVERGEN; Q8CI15; -.
DR   OMA; Q8CI15; AIQKPLC.
DR   NextBio; 299241; -.
DR   Bgee; Q8CI15; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0017050; F:D-erythro-sphingosine kinase activity; ISS:UniProtKB.
DR   GO; GO:0004143; F:diacylglycerol kinase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
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:0001568; P:blood vessel development; IGI:MGI.
DR   GO; GO:0007420; P:brain development; IGI:MGI.
DR   GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IGI:MGI.
DR   GO; GO:0032651; P:regulation of interleukin-1 beta production; IMP:MGI.
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   Alternative splicing; ATP-binding; Calmodulin-binding; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Transferase.
FT   CHAIN         1    382       Sphingosine kinase 1.
FT                                /FTId=PRO_0000333032.
FT   DOMAIN       16    153       DAGKc.
FT   MOD_RES     193    193       Phosphothreonine (By similarity).
FT   VAR_SEQ       1      3       MEP -> MWWCCVLFV (in isoform 2).
FT                                /FTId=VSP_033448.
FT   VAR_SEQ       4      4       Missing (in isoform 3).
FT                                /FTId=VSP_033449.
FT   CONFLICT    146    146       R -> H (in Ref. 1; BAE33198).
SQ   SEQUENCE   382 AA;  42443 MW;  B791FAA58FCE3D29 CRC64;
     MEPVECPRGL LPRPCRVLVL LNPQGGKGKA LQLFQSRVQP FLEEAEITFK LILTERKNHA
     RELVCAEELG HWDALAVMSG DGLMHEVVNG LMERPDWETA IQKPLCSLPG GSGNALAASV
     NHYAGYEQVT NEDLLINCTL LLCRRRLSPM NLLSLHTASG LRLYSVLSLS WGFVADVDLE
     SEKYRRLGEI RFTVGTFFRL ASLRIYQGQL AYLPVGTVAS KRPASTLVQK GPVDTHLVPL
     EEPVPSHWTV VPEQDFVLVL VLLHTHLSSE LFAAPMGRCE AGVMHLFYVR AGVSRAALLR
     LFLAMQKGKH MELDCPYLVH VPVVAFRLEP RSQRGVFSVD GELMVCEAVQ GQVHPNYLWM
     VCGSRDAPSG RDSRRGPPPE EP
//