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

P91079 (SPTC1_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:sptl-1
ORF Names:C23H3.4
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length458 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Component of the serine palmitoyltransferase (SPT) that catalyzes the first committed step in sphingolipid biosynthesis, which is the condensation of an acyl-CoA species and L-serine. The catalytic core is composed of a heterodimer of sptl-1 and sptl-2 or sptl-1 and sptl-3 By similarity. Required for the specification of abicobasal polarity and development of the gut lumen. Ref.2

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 of sptl-1/sptl-2 or sptl-1/sptl-3 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 – 458458Serine palmitoyltransferase 1
PRO_0000421271

Sequences

Sequence LengthMass (Da)Tools
P91079 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 2F56AC94DFFABF91

FASTA45852,085
        10         20         30         40         50         60 
MGFLPDSWHF YIETLLVALL AYVVMRNRSK RQQEKLSKKL TERQKDELIA DWTPEPLVPE 

        70         80         90        100        110        120 
TPQDHPVLNP KYADGKMTKD VSIDGEKYLN MASTNFLSFI GVKRIEDRAK QTIFKYGVGS 

       130        140        150        160        170        180 
CGPRGFYGTV DVHLDLEKEL AKFMGCEEAV LYSYGFATVS SAIPAYAKKG DVIFVDEGVN 

       190        200        210        220        230        240 
FAIQKGLQAS RSRVEYFKHN DMEHLERLLL EQEQRDKKDP KKAKSVRRFI VVEGLYVNYA 

       250        260        270        280        290        300 
DLCPLPKIIE FKWRFKVRVF IDESWSFGVI GKTGRGVTEH FNVPMEDVDM VMASLENALA 

       310        320        330        340        350        360 
STGGFCVGRS YVVGHQRLSG LGYCFSASLP PLLATAASEA ISIIDEEPSR VQKVTEMAIN 

       370        380        390        400        410        420 
GQKKLQDALS GSKFSLQGCP ESPMKHIYYN GEDEEKQLDT FVETVFTKNH LLLTRARYLD 

       430        440        450 
KDELFKIRPS IRVMFQHDLT EEEIQRAVDA IRVVAHKF 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
[2]"Apicobasal domain identities of expanding tubular membranes depend on glycosphingolipid biosynthesis."
Zhang H., Abraham N., Khan L.A., Hall D.H., Fleming J.T., Gobel V.
Nat. Cell Biol. 13:1189-1201(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FO080632 Genomic DNA. Translation: CCD65323.1.
FO080632 Genomic DNA. Translation: CCD65324.1.
PIRT25557.
RefSeqNP_001021978.1. NM_001026807.2.
NP_001021979.1. NM_001026808.2.
UniGeneCel.8663.

3D structure databases

ProteinModelPortalP91079.
SMRP91079. Positions 76-449.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP91079. 1 interaction.
MINTMINT-213137.
STRING6239.C23H3.4a.2.

Proteomic databases

PaxDbP91079.
PRIDEP91079.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaC23H3.4a.1; C23H3.4a.1; WBGene00016020.
C23H3.4a.2; C23H3.4a.2; WBGene00016020.
GeneID173389.
KEGGcel:CELE_C23H3.4.
UCSCC23H3.4a.2. c. elegans.

Organism-specific databases

CTD173389.
WormBaseC23H3.4a; CE08323; WBGene00016020; sptl-1.
C23H3.4b; CE37749; WBGene00016020; sptl-1.

Phylogenomic databases

eggNOGCOG0156.
GeneTreeENSGT00550000074872.
HOGENOMHOG000216602.
InParanoidP91079.
OMATEMAING.
PhylomeDBP91079.

Enzyme and pathway databases

UniPathwayUPA00222.

Family and domain databases

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

Other

NextBio879437.
PROP91079.

Entry information

Entry nameSPTC1_CAEEL
AccessionPrimary (citable) accession number: P91079
Secondary accession number(s): Q5R3Y5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: May 1, 1997
Last modified: June 11, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase