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Q5R9T5 (SPTC1_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 66. 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
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

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_0000327869

Regions

Transmembrane16 – 3621Helical; Potential

Amino acid modifications

Modified residue1641Phosphotyrosine; by ABL By similarity

Experimental info

Sequence conflict1581T → I in CAH92367. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q5R9T5 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 64BCBB758A79B632

FASTA47352,867
        10         20         30         40         50         60 
MATATEQWVL VEMVQALYEA PAYHLILEGI LILWIIRLLF SKTYKLQERS DLTVKEKEEL 

        70         80         90        100        110        120 
IEEWQPEPLV PLVPKDHPAL NYNIVSGPPS HKIVVNGKEC INFASFNFLG LLDNPRVKAA 

       130        140        150        160        170        180 
ALASLKKYGV GTCGPRGFYG TFDVHLDLED RLAKFMKTEE AIIYSYGFAT IASAIPAYSK 

       190        200        210        220        230        240 
RGDIVFVDRA ACFAIQKGLQ ASRSDIKLFK HNDMADLERL LKEQEIEDQK NPRKARVTRR 

       250        260        270        280        290        300 
FIVVEGLYMN TGTICPLPEL VKLKYKYKAR IFLEESLSFG VLGEHGRGVT EHYGINIDDI 

       310        320        330        340        350        360 
DLISANMENA LASIGGFCCG RSFVIDHQRL SGQGYCFSAS LPPLLAAAAI EALNIMEENP 

       370        380        390        400        410        420 
GIFAVLKEKC RQIHKALQGI SGLKVVGEPL SPAFHLQLEE STGSREQDVR LLQEIVDQCM 

       430        440        450        460        470 
NRSIALTQAR YLEKEEKCLP PPSIRVVVTV EQTEEELDRA ASTIKEVAQA VLL 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Heart and Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR859297 mRNA. Translation: CAH91475.1.
CR860225 mRNA. Translation: CAH92367.1.
RefSeqNP_001126393.1. NM_001132921.1.

3D structure databases

ProteinModelPortalQ5R9T5.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100173375.
KEGGpon:100173375.

Organism-specific databases

CTD10558.

Phylogenomic databases

HOGENOMHOG000216602.
HOVERGENHBG003992.
InParanoidQ5R793.
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_PONAB
AccessionPrimary (citable) accession number: Q5R9T5
Secondary accession number(s): Q5R793
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: December 21, 2004
Last modified: February 19, 2014
This is version 66 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