SPTC1_BOVIN
ID SPTC1_BOVIN Reviewed; 473 AA.
AC Q3MHG1;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Serine palmitoyltransferase 1;
DE EC=2.3.1.50 {ECO:0000250|UniProtKB:O15269};
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=SPTLC1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Serine palmitoyltransferase (SPT). The heterodimer formed
CC with SPTLC2 or SPTLC3 constitutes the catalytic core. The composition
CC of the serine palmitoyltransferase (SPT) complex determines the
CC substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong
CC preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA
CC isozyme uses both C14-CoA and C16-CoA as substrates, with a slight
CC preference for C14-CoA. The SPTLC1-SPTLC2-SPTSSB complex shows a strong
CC preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB
CC isozyme displays an ability to use a broader range of acyl-CoAs,
CC without apparent preference (By similarity). Required for adipocyte
CC cell viability and metabolic homeostasis (By similarity).
CC {ECO:0000250|UniProtKB:O15269, ECO:0000250|UniProtKB:O35704}.
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 Evidence={ECO:0000250|UniProtKB:O15269};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14762;
CC Evidence={ECO:0000250|UniProtKB:O15269};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-serine + octadecanoyl-CoA = 3-oxoeicosasphinganine +
CC CO2 + CoA; Xref=Rhea:RHEA:33683, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57394, ChEBI:CHEBI:65073;
CC Evidence={ECO:0000250|UniProtKB:O15269};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33684;
CC Evidence={ECO:0000250|UniProtKB:O15269};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-serine + tetradecanoyl-CoA = 3-oxohexadecasphinganine
CC + CO2 + CoA; Xref=Rhea:RHEA:35675, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57385, ChEBI:CHEBI:71007;
CC Evidence={ECO:0000250|UniProtKB:O15269};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35676;
CC Evidence={ECO:0000250|UniProtKB:O15269};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + H(+) + L-serine = 3-oxotetradecasphinganine +
CC CO2 + CoA; Xref=Rhea:RHEA:35679, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57375, ChEBI:CHEBI:71008;
CC Evidence={ECO:0000250|UniProtKB:O15269};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35680;
CC Evidence={ECO:0000250|UniProtKB:O15269};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC -!- SUBUNIT: Heterodimer with SPTLC2 or SPTLC3. Component of the serine
CC palmitoyltransferase (SPT) complex, composed of SPTLC1, either SPTLC2
CC or SPTLC3, and either SPTSSA or SPTSSB. The composition of the complex
CC will define the substrate specificity. Interacts with SPTSSA and
CC SPTSSB; the interaction is direct. Interacts with ORMDL3 (By
CC similarity). Interacts with RTN4 (isoform B) (By similarity).
CC {ECO:0000250|UniProtKB:O15269, ECO:0000250|UniProtKB:O35704}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O35704}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:O35704}.
CC -!- PTM: Phosphorylation at Tyr-164 inhibits activity and promotes cell
CC survival. {ECO:0000250|UniProtKB:O15269}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; BC105250; AAI05251.1; -; mRNA.
DR RefSeq; NP_001029921.1; NM_001034749.1.
DR AlphaFoldDB; Q3MHG1; -.
DR SMR; Q3MHG1; -.
DR STRING; 9913.ENSBTAP00000002872; -.
DR PaxDb; Q3MHG1; -.
DR PRIDE; Q3MHG1; -.
DR Ensembl; ENSBTAT00000002872; ENSBTAP00000002872; ENSBTAG00000002220.
DR GeneID; 614165; -.
DR KEGG; bta:614165; -.
DR CTD; 10558; -.
DR VEuPathDB; HostDB:ENSBTAG00000002220; -.
DR VGNC; VGNC:35256; SPTLC1.
DR eggNOG; KOG1358; Eukaryota.
DR GeneTree; ENSGT00550000074872; -.
DR HOGENOM; CLU_015846_0_1_1; -.
DR InParanoid; Q3MHG1; -.
DR OMA; RNTPTFA; -.
DR OrthoDB; 438936at2759; -.
DR TreeFam; TF314877; -.
DR Reactome; R-BTA-1660661; Sphingolipid de novo biosynthesis.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000002220; Expressed in parenchyma of mammary gland and 104 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0035339; C:SPOTS complex; ISS:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004758; F:serine C-palmitoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR GO; GO:1904504; P:positive regulation of lipophagy; IEA:Ensembl.
DR GO; GO:1904649; P:regulation of fat cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0006665; P:sphingolipid metabolic process; ISS: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 2: Evidence at transcript level;
KW Acyltransferase; Endoplasmic reticulum; Lipid metabolism; Membrane;
KW Phosphoprotein; Pyridoxal phosphate; Reference proteome;
KW Sphingolipid metabolism; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..473
FT /note="Serine palmitoyltransferase 1"
FT /id="PRO_0000283042"
FT TOPO_DOM 1..15
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 164
FT /note="Phosphotyrosine; by ABL"
FT /evidence="ECO:0000250|UniProtKB:O15269"
SQ SEQUENCE 473 AA; 52788 MW; 13C8315F8B3572F0 CRC64;
MATVAEQWVL VEMVQALYEA PAYHLILEGI LILWIIRLLF SKTYKLQERS DLTLKEKEEL
IEEWQPEPLV PPVSKDHPAL NYNIVSGPPS HNIVVNGKEC INFASFNFLG LLDNPRLKAA
ALASLKKYGV GTCGPRGFYG TFDVHLDLED RLAKFMKTEE AIIYSYGFAT IASAIPAYSK
RGDIVFVDKA ACFAIQKGLQ ASRSDIKVFN HNDMDDLERL LKEQEIEDQK NPRKARVTRR
FIIVEGLYMN TGTVCPLPEL VKLKYKYKAR IFLEESLSFG VLGEHGRGVT EHFGISIDDI
DLISANMENS LASIGGFCCG RSFVIDHQRL SGQGYCFSAS LPPLLAAAAI EALNIMEENP
GIFAVLKEKC KRIHKALQGI PGLKVVGESI SPALHLQLEE TTGCRERDVK LLQEIVTQCM
DRGIALTQAR YLEKEEKYLP PPSIRVVVTV EQTEEDLEKA ASTISEVAQT VLL
