LCB4_SCHPO
ID LCB4_SCHPO Reviewed; 458 AA.
AC O14159;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Sphingoid long chain base kinase 4 {ECO:0000250|UniProtKB:Q12246};
DE Short=LCB kinase 4 {ECO:0000250|UniProtKB:Q12246};
DE EC=2.7.1.91 {ECO:0000250|UniProtKB:Q12246};
DE AltName: Full=Sphinganine kinase 4 {ECO:0000305};
GN Name=lcb4; ORFNames=SPAC4A8.07c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Catalyzes the phosphorylation of the sphingoid long chain
CC bases dihydrosphingosine (DHS) and phytosphingosine (PHS) to form
CC dihydrosphingosine 1-phosphate (DHS-1P) and phytosphingosine 1-
CC phosphate (PHS-1P) respectively (By similarity). Involved in the
CC biosynthesis of sphingolipids and ceramides (By similarity). Involved
CC in heat-induced transient cell cycle arrest (By similarity).
CC Accumulation of phosphorylated sphingoid long chain bases (LCBPs)
CC stimulates calcium influx and activates calcineurin signaling. Involved
CC in heat-stress resistance (By similarity).
CC {ECO:0000250|UniProtKB:Q12246}.
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:0000250|UniProtKB:Q12246};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q12246};
CC Peripheral membrane protein {ECO:0000305}. Endoplasmic reticulum
CC membrane {ECO:0000250|UniProtKB:Q12246}; Peripheral membrane protein
CC {ECO:0000305}. Late endosome membrane {ECO:0000250|UniProtKB:Q12246};
CC Peripheral membrane protein {ECO:0000305}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q12246}; Peripheral membrane protein
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB11477.1; -; Genomic_DNA.
DR PIR; T38776; T38776.
DR RefSeq; NP_593818.1; NM_001019248.2.
DR AlphaFoldDB; O14159; -.
DR SMR; O14159; -.
DR STRING; 4896.SPAC4A8.07c.1; -.
DR MaxQB; O14159; -.
DR PaxDb; O14159; -.
DR EnsemblFungi; SPAC4A8.07c.1; SPAC4A8.07c.1:pep; SPAC4A8.07c.
DR GeneID; 2543328; -.
DR KEGG; spo:SPAC4A8.07c; -.
DR PomBase; SPAC4A8.07c; lcb4.
DR VEuPathDB; FungiDB:SPAC4A8.07c; -.
DR eggNOG; KOG1116; Eukaryota.
DR HOGENOM; CLU_013399_0_1_1; -.
DR InParanoid; O14159; -.
DR OMA; AECDLGT; -.
DR PhylomeDB; O14159; -.
DR Reactome; R-SPO-1483206; Glycerophospholipid biosynthesis.
DR Reactome; R-SPO-1660661; Sphingolipid de novo biosynthesis.
DR Reactome; R-SPO-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR Reactome; R-SPO-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-SPO-9009391; Extra-nuclear estrogen signaling.
DR PRO; PR:O14159; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:PomBase.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017050; F:D-erythro-sphingosine kinase activity; ISO:PomBase.
DR GO; GO:0004143; F:diacylglycerol kinase activity; ISM:PomBase.
DR GO; GO:0001727; F:lipid kinase activity; IBA:GO_Central.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0008481; F:sphinganine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0019722; P:calcium-mediated signaling; ISO:PomBase.
DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central.
DR GO; GO:0006665; P:sphingolipid metabolic process; IBA:GO_Central.
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 3: Inferred from homology;
KW ATP-binding; Cell membrane; Endoplasmic reticulum; Endosome;
KW Golgi apparatus; Kinase; Lipid metabolism; Membrane; Nucleotide-binding;
KW Reference proteome; Sphingolipid metabolism; Transferase.
FT CHAIN 1..458
FT /note="Sphingoid long chain base kinase 4"
FT /id="PRO_0000314771"
FT DOMAIN 103..241
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT ACT_SITE 172
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 113..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 170..173
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 202..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 266
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 272
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 426..428
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
SQ SEQUENCE 458 AA; 51289 MW; 9DD4DA333E1CD9DB CRC64;
MDFGLTNNSI KAFEDQKLLH IHQSCVSYPS DTLICSIPVS AKNVDLNIPF KNILWVDKTG
PNSVTLSYVS RSSKVATKCW VDFVENSDQF CEYLLDVAYK GIKRSRRFIV FINPHGGKGK
AKHIWESEAE PVFSSAHSIC EVVLTRRKDH AKSIAKNLDV GSYDGILSVG GDGLFHEVIN
GLGERDDYLE AFKLPVCMIP GGSGNAFSYN ATGQLKPALT ALEILKGRPT SFDLMTFEQK
GKKAYSFLTA NYGIIADCDI GTENWRFMGE NRAYLGFFLR LFQKPDWKCS IEMDVVSSDR
TEIKHMYEKS KNLAPMSESS DSDKTVSTSP ESHLLTFEIN DLSIFCAGLL PYIAPDAKMF
PAASNDDGLI DVVIVYSKQF RKSLLSMFTQ LDNGGFYYSK HLNYYKVRSF RFTPVNTGKR
HYFALDGESY PLEPFECRVA PKLGTTLSPV AGFQLLDI
