SPTC1_CAEEL
ID SPTC1_CAEEL Reviewed; 458 AA.
AC P91079; Q5R3Y5;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Serine palmitoyltransferase 1;
DE EC=2.3.1.50;
DE AltName: Full=Long chain base biosynthesis protein 1;
DE Short=LCB 1;
DE AltName: Full=Serine-palmitoyl-CoA transferase 1;
DE Short=SPT 1;
DE Short=SPT1;
GN Name=sptl-1; ORFNames=C23H3.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION.
RX PubMed=21926990; DOI=10.1038/ncb2328;
RA Zhang H., Abraham N., Khan L.A., Hall D.H., Fleming J.T., Gobel V.;
RT "Apicobasal domain identities of expanding tubular membranes depend on
RT glycosphingolipid biosynthesis.";
RL Nat. Cell Biol. 13:1189-1201(2011).
CC -!- FUNCTION: Component of the serine palmitoyltransferase (SPT) that
CC catalyzes the first committed step in sphingolipid biosynthesis, which
CC is the condensation of an acyl-CoA species and L-serine. The catalytic
CC core is composed of a heterodimer of sptl-1 and sptl-2 or sptl-1 and
CC sptl-3 (By similarity). Required for the specification of abicobasal
CC polarity and development of the gut lumen. {ECO:0000250,
CC ECO:0000269|PubMed:21926990}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexadecanoyl-CoA + L-serine = 3-oxosphinganine + CO2 +
CC CoA; Xref=Rhea:RHEA:14761, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:58299; EC=2.3.1.50;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC -!- SUBUNIT: Heterodimer of sptl-1/sptl-2 or sptl-1/sptl-3. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; FO080632; CCD65323.1; -; Genomic_DNA.
DR EMBL; FO080632; CCD65324.1; -; Genomic_DNA.
DR PIR; T25557; T25557.
DR RefSeq; NP_001021978.1; NM_001026807.2.
DR RefSeq; NP_001021979.1; NM_001026808.2.
DR AlphaFoldDB; P91079; -.
DR SMR; P91079; -.
DR BioGRID; 38769; 5.
DR IntAct; P91079; 1.
DR STRING; 6239.C23H3.4a.2; -.
DR SwissLipids; SLP:000000194; -.
DR EPD; P91079; -.
DR PaxDb; P91079; -.
DR PeptideAtlas; P91079; -.
DR EnsemblMetazoa; C23H3.4a.1; C23H3.4a.1; WBGene00016020.
DR EnsemblMetazoa; C23H3.4b.1; C23H3.4b.1; WBGene00016020.
DR GeneID; 173389; -.
DR UCSC; C23H3.4a.2; c. elegans.
DR CTD; 173389; -.
DR WormBase; C23H3.4a; CE08323; WBGene00016020; sptl-1.
DR WormBase; C23H3.4b; CE37749; WBGene00016020; sptl-1.
DR eggNOG; KOG1358; Eukaryota.
DR GeneTree; ENSGT00550000074872; -.
DR InParanoid; P91079; -.
DR OMA; RNTPTFA; -.
DR OrthoDB; 438936at2759; -.
DR PhylomeDB; P91079; -.
DR UniPathway; UPA00222; -.
DR PRO; PR:P91079; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00016020; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; P91079; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004758; F:serine C-palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IMP:UniProtKB.
DR GO; GO:0046512; P:sphingosine biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Lipid metabolism; Pyridoxal phosphate; Reference proteome;
KW Sphingolipid metabolism; Transferase.
FT CHAIN 1..458
FT /note="Serine palmitoyltransferase 1"
FT /id="PRO_0000421271"
SQ SEQUENCE 458 AA; 52085 MW; 2F56AC94DFFABF91 CRC64;
MGFLPDSWHF YIETLLVALL AYVVMRNRSK RQQEKLSKKL TERQKDELIA DWTPEPLVPE
TPQDHPVLNP KYADGKMTKD VSIDGEKYLN MASTNFLSFI GVKRIEDRAK QTIFKYGVGS
CGPRGFYGTV DVHLDLEKEL AKFMGCEEAV LYSYGFATVS SAIPAYAKKG DVIFVDEGVN
FAIQKGLQAS RSRVEYFKHN DMEHLERLLL EQEQRDKKDP KKAKSVRRFI VVEGLYVNYA
DLCPLPKIIE FKWRFKVRVF IDESWSFGVI GKTGRGVTEH FNVPMEDVDM VMASLENALA
STGGFCVGRS YVVGHQRLSG LGYCFSASLP PLLATAASEA ISIIDEEPSR VQKVTEMAIN
GQKKLQDALS GSKFSLQGCP ESPMKHIYYN GEDEEKQLDT FVETVFTKNH LLLTRARYLD
KDELFKIRPS IRVMFQHDLT EEEIQRAVDA IRVVAHKF
