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   27-MAR-2024, entry version 157.
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; 3.
DR   DIP; DIP-26788N; -.
DR   IntAct; Q9XVI6; 1.
DR   STRING; 6239.T22G5.5b.1; -.
DR   EPD; Q9XVI6; -.
DR   PaxDb; 6239-T22G5-5b; -.
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   AGR; WB:WBGene00011932; -.
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; DATYTDH; -.
DR   OrthoDB; 9643at2759; -.
DR   PhylomeDB; Q9XVI6; -.
DR   UniPathway; UPA00222; -.
DR   PRO; PR:Q9XVI6; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00011932; Expressed in larva and 4 other cell types or 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   CDD; cd06454; KBL_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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   PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR   PANTHER; PTHR13693:SF54; SERINE PALMITOYLTRANSFERASE 3; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 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
//