SPTC3_CAEEL
ID SPTC3_CAEEL Reviewed; 512 AA.
AC Q9XVI6; H9G307;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Serine palmitoyltransferase 3;
DE EC=2.3.1.50;
DE AltName: Full=Long chain base biosynthesis protein 3;
DE Short=LCB 3;
DE AltName: Full=Serine-palmitoyl-CoA transferase 3;
DE Short=SPT 3;
DE Short=SPT3;
GN Name=sptl-3; ORFNames=T22G5.5;
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], AND ALTERNATIVE SPLICING.
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-3. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q9XVI6-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q9XVI6-2; Sequence=VSP_045380;
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; Z81127; CAB03390.2; -; Genomic_DNA.
DR EMBL; Z81127; CCG28222.1; -; Genomic_DNA.
DR PIR; T25126; T25126.
DR RefSeq; NP_001256547.1; NM_001269618.1. [Q9XVI6-2]
DR RefSeq; NP_001256548.1; NM_001269619.1. [Q9XVI6-1]
DR AlphaFoldDB; Q9XVI6; -.
DR SMR; Q9XVI6; -.
DR BioGRID; 44898; 2.
DR DIP; DIP-26788N; -.
DR IntAct; Q9XVI6; 1.
DR STRING; 6239.T22G5.5b; -.
DR EPD; Q9XVI6; -.
DR PaxDb; Q9XVI6; -.
DR PeptideAtlas; Q9XVI6; -.
DR EnsemblMetazoa; T22G5.5a.1; T22G5.5a.1; WBGene00011932. [Q9XVI6-1]
DR EnsemblMetazoa; T22G5.5b.1; T22G5.5b.1; WBGene00011932. [Q9XVI6-2]
DR GeneID; 179884; -.
DR KEGG; cel:CELE_T22G5.5; -.
DR UCSC; T22G5.5.1; c. elegans. [Q9XVI6-1]
DR CTD; 179884; -.
DR WormBase; T22G5.5a; CE31996; WBGene00011932; sptl-3. [Q9XVI6-1]
DR WormBase; T22G5.5b; CE47328; WBGene00011932; sptl-3. [Q9XVI6-2]
DR eggNOG; KOG1357; Eukaryota.
DR HOGENOM; CLU_015846_7_2_1; -.
DR InParanoid; Q9XVI6; -.
DR OMA; GTDIGRQ; -.
DR OrthoDB; 438936at2759; -.
DR PhylomeDB; Q9XVI6; -.
DR UniPathway; UPA00222; -.
DR PRO; PR:Q9XVI6; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00011932; Expressed in larva and 4 other tissues.
DR GO; GO:0017059; C:serine C-palmitoyltransferase complex; 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:0046512; P:sphingosine biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
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.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Alternative splicing; Lipid metabolism;
KW Pyridoxal phosphate; Reference proteome; Sphingolipid metabolism;
KW Transferase.
FT CHAIN 1..512
FT /note="Serine palmitoyltransferase 3"
FT /id="PRO_0000421273"
FT MOD_RES 345
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1
FT /note="M -> MSSCFVFYNM (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_045380"
SQ SEQUENCE 512 AA; 56334 MW; 3F68835D2961C4D0 CRC64;
MGGTQNGKAV ANGKAKNGNI TEKVIKLDPC PKPAFYVFWL VQLNITMMLV GAMVATLFDK
WGIVKTKRSK GDPRMESFQP LGNSFDATYT DHIYRQSTDV VNRPISGVPG AIVRLKDRYT
DDHGWTQKYT GTESEVINLG SYNYLGFSHR SGVCAEAAAA HIDKYGINCG GSRQEIGNHV
AHKSVESTIA QYLNVEDAIV FPMGFATNSM NIPSLVDKGS LILSDRLNHA SLVTGCRLSG
AHTVVFRHND ASDCERKLRD ALCGVSPKTG EKYNKVLIII EGIYSMEGTI VNLPAFIAVK
KKYNCYLFLD EAHSIGAVGP SGRGVAEYWG CNPRDIDIMM GTLTKSFASA GGYMGGSKKV
IDHIRRYSAG TCYGVTMSPP LIAQVERAVL IMSGKDGTDI GRQKAIQLLE NSRYFRKELR
KRGFLVYGNN DSPVVPLMTF YITKVVEFSR RMLKHNIGIV AVGYPATPLL EARVRFCLSA
DHTKEHLDYI LEAVEQVGME TGTFYGTKIV DE
