SPTC2_CAEEL
ID SPTC2_CAEEL Reviewed; 558 AA.
AC Q20375; Q95ZT7;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Serine palmitoyltransferase 2;
DE EC=2.3.1.50;
DE AltName: Full=Long chain base biosynthesis protein 2;
DE Short=LCB 2;
DE AltName: Full=Serine-palmitoyl-CoA transferase 2;
DE Short=SPT 2;
DE Short=SPT2;
GN Name=sptl-2; ORFNames=F43H9.2;
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-2. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q20375-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q20375-2; Sequence=VSP_045379;
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; FO081377; CCD71173.1; -; Genomic_DNA.
DR EMBL; FO081377; CCD71174.1; -; Genomic_DNA.
DR PIR; T29503; T29503.
DR RefSeq; NP_505064.1; NM_072663.4. [Q20375-2]
DR RefSeq; NP_505065.1; NM_072664.4. [Q20375-1]
DR AlphaFoldDB; Q20375; -.
DR SMR; Q20375; -.
DR BioGRID; 57296; 1.
DR DIP; DIP-26394N; -.
DR STRING; 6239.F43H9.2b; -.
DR EPD; Q20375; -.
DR PaxDb; Q20375; -.
DR PeptideAtlas; Q20375; -.
DR EnsemblMetazoa; F43H9.2a.1; F43H9.2a.1; WBGene00018398. [Q20375-1]
DR EnsemblMetazoa; F43H9.2b.1; F43H9.2b.1; WBGene00018398. [Q20375-2]
DR EnsemblMetazoa; F43H9.2b.2; F43H9.2b.2; WBGene00018398. [Q20375-2]
DR GeneID; 266646; -.
DR KEGG; cel:CELE_F43H9.2; -.
DR UCSC; F43H9.2b; c. elegans.
DR CTD; 266646; -.
DR WormBase; F43H9.2a; CE07246; WBGene00018398; sptl-2. [Q20375-1]
DR WormBase; F43H9.2b; CE27380; WBGene00018398; sptl-2. [Q20375-2]
DR eggNOG; KOG1357; Eukaryota.
DR GeneTree; ENSGT00940000168104; -.
DR HOGENOM; CLU_015846_7_1_1; -.
DR InParanoid; Q20375; -.
DR OMA; IEDEPPY; -.
DR OrthoDB; 438936at2759; -.
DR UniPathway; UPA00222; -.
DR PRO; PR:Q20375; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00018398; Expressed in pharyngeal muscle cell (C elegans) and 3 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..558
FT /note="Serine palmitoyltransferase 2"
FT /id="PRO_0000421272"
FT REGION 33..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 384
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..16
FT /note="MSRRTDSLCLDEYLSS -> MTSEVAKRNSPFRFLHKLPIRLTFTEKKSPLL
FT ISDLAKQREEND (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_045379"
SQ SEQUENCE 558 AA; 62704 MW; 2896A1C20966CB25 CRC64;
MSRRTDSLCL DEYLSSELKK RTHILECAWN QEHDDDEEEE EVKVDQGSEE TTSSHDIYGD
VGKRAPNEFE KIDRLTTIKV YIAWLALFVF AHIREYVTRF GFVKDLSSKE NAKMKDFVPL
FSDFEAFYQR NCYIKVRDVF ERPICSVPGA TVDLVDRVSH DGNWTYEYPG TRTNVINVGS
YNYLGFAQSA GPCAEQSASS IDREGLSCCT TVHERGRSVS QAKLEKLVAE FLGVEDAICF
SMGFATNSMN APCLVDKHSL IISDKYNHAS LILGCRLSGA STKVFEHNDM ESLERILRDA
IAYGNPKTHR PYKKILIIVE GIYSMEGSIC NLPGIIALKK KYQAYLYLDE AHSIGAMGKT
GKGVVEYWGC DPKDVDILMG TFTKSFGAAG GYIAGSKRTV DHLRAASPTG YYSSPMSPPI
AQQIYTSMSI IMGKDGTKDG AQRIERLARN SHYFRMKLKQ NGFIVYGSND SPVVPMLIYF
PTMCGFYGRE MLARNIGCVV VSFPATHMTE GRVRFCISAA HTKEQLDEVL ETVNLLGSMS
RSKFSKRSHL YKNQKIEW
