Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q3MHG1 (SPTC1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 77. 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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

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_0000283042

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
Q3MHG1 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: 13C8315F8B3572F0

FASTA47352,788
        10         20         30         40         50         60 
MATVAEQWVL VEMVQALYEA PAYHLILEGI LILWIIRLLF SKTYKLQERS DLTLKEKEEL 

        70         80         90        100        110        120 
IEEWQPEPLV PPVSKDHPAL NYNIVSGPPS HNIVVNGKEC INFASFNFLG LLDNPRLKAA 

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

       190        200        210        220        230        240 
RGDIVFVDKA ACFAIQKGLQ ASRSDIKVFN HNDMDDLERL LKEQEIEDQK NPRKARVTRR 

       250        260        270        280        290        300 
FIIVEGLYMN TGTVCPLPEL VKLKYKYKAR IFLEESLSFG VLGEHGRGVT EHFGISIDDI 

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

       370        380        390        400        410        420 
GIFAVLKEKC KRIHKALQGI PGLKVVGESI SPALHLQLEE TTGCRERDVK LLQEIVTQCM 

       430        440        450        460        470 
DRGIALTQAR YLEKEEKYLP PPSIRVVVTV EQTEEDLEKA ASTISEVAQT VLL 

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Uterus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC105250 mRNA. Translation: AAI05251.1.
RefSeqNP_001029921.1. NM_001034749.1.
UniGeneBt.109577.

3D structure databases

ProteinModelPortalQ3MHG1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000002872.

Proteomic databases

PRIDEQ3MHG1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000002872; ENSBTAP00000002872; ENSBTAG00000002220.
GeneID614165.
KEGGbta:614165.

Organism-specific databases

CTD10558.

Phylogenomic databases

eggNOGCOG0156.
GeneTreeENSGT00550000074872.
HOGENOMHOG000216602.
HOVERGENHBG003992.
InParanoidQ3MHG1.
KOK00654.
OMARVFMDES.
OrthoDBEOG786H30.
TreeFamTF314877.

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...

Other

NextBio20898974.

Entry information

Entry nameSPTC1_BOVIN
AccessionPrimary (citable) accession number: Q3MHG1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: October 25, 2005
Last modified: May 14, 2014
This is version 77 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