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O54695 (SPTC1_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine palmitoyltransferase 1

EC=2.3.1.50
Alternative name(s):
Long chain base biosynthesis protein 1
Short name=LCB 1
Serine-palmitoyl-CoA transferase 1
Short name=SPT 1
Short name=SPT1
Gene names
Name:SPTLC1
Synonyms:LCB1
OrganismCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine palmitoyltransferase (SPT). The heterodimer formed with SPTLC2 or SPTLC3 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates. The SPTLC1-SPTLC2-SPTSSB complex displays a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme has the ability to use a broader range of acyl-CoAs By similarity.

Catalytic activity

Palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2.

Cofactor

Pyridoxal phosphate By similarity.

Pathway

Lipid metabolism; sphingolipid metabolism.

Subunit structure

Heterodimer with SPTLC2 or SPTLC3. Component of the serine palmitoyltransferase (SPT) complex, composed of SPTLC1, either SPTLC2 or SPTLC3, and either SPTSSA or SPTSSB. Interacts with SPTSSA and SPTSSB; the interaction is direct. Interacts with ORMDL3 By similarity.

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein Ref.2.

Post-translational modification

Phosphorylation at Tyr-164 inhibits activity and promotes cell survival By similarity.

Sequence similarities

Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 473473Serine palmitoyltransferase 1
PRO_0000163852

Regions

Topological domain1 – 1515Lumenal Potential
Transmembrane16 – 3621Helical; Potential
Topological domain37 – 473437Cytoplasmic Potential

Amino acid modifications

Modified residue1641Phosphotyrosine; by ABL By similarity

Sequences

Sequence LengthMass (Da)Tools
O54695 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 1ABED2B60EC854B4

FASTA47352,520
        10         20         30         40         50         60 
MAMAAEQWVL VEMVQALYEA PAYHLILEGI LILWIIRLVF SKTYKLQERS DLTAKEKEEL 

        70         80         90        100        110        120 
IEEWQPEPLV PPVSKNHPAL NYNIVSGPPT HNIVVNGKEC VNFASFNFLG LLANPRVKAA 

       130        140        150        160        170        180 
ALASLKKYGV GTCGPRGFYG TFDVHLDLEE RLAKFMRTEE AIIYSYGFST IASAIPAYSK 

       190        200        210        220        230        240 
RGDIVFVDSA ACFAIQKGLQ ASRSDIKLFK HNDVADLERL LKEQEIEDQK NPRKARVTRR 

       250        260        270        280        290        300 
FIVVEGLYMN TGTVCPLPEL VKLKYKYKAR IFLEESLSFG VLGEHGRGVT EHYGISIDDI 

       310        320        330        340        350        360 
DLISANMENA LASVGGFCCG RSFVVDHQRL SGQGYCFSAS LPPLLAAAAI EALNIMEENP 

       370        380        390        400        410        420 
GIFAVLKKKC QHIHKSLQGI SGLKVVGESL SPALHLQLEE STGSREKDVQ LLQEMVIHCM 

       430        440        450        460        470 
NEGIALTQAR YLDKEEKCLP PPSIRVVVTV EQTEEELERA ASTIREAAQA VLL 

« Hide

References

[1]"A mammalian homolog of the yeast LCB1 encodes a component of serine palmitoyltransferase, the enzyme catalyzing the first step in sphingolipid synthesis."
Hanada K., Hara T., Nishijima M., Kuge O., Dickson R.C., Nagiec M.M.
J. Biol. Chem. 272:32108-32114(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Ovary.
[2]"Localization, topology, and function of the LCB1 subunit of serine palmitoyltransferase in mammalian cells."
Yasuda S., Nishijima M., Hanada K.
J. Biol. Chem. 278:4176-4183(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF004831 mRNA. Translation: AAC53505.1.
RefSeqNP_001233688.1. NM_001246759.1.

3D structure databases

ProteinModelPortalO54695.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEO54695.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100689326.
KEGGcge:100689326.

Organism-specific databases

CTD10558.

Phylogenomic databases

HOVERGENHBG003992.
KOK00654.

Enzyme and pathway databases

UniPathwayUPA00222.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSPTC1_CRIGR
AccessionPrimary (citable) accession number: O54695
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: April 16, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways