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P91079

- SPTC1_CAEEL

UniProt

P91079 - SPTC1_CAEEL

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Protein
Serine palmitoyltransferase 1
Gene
sptl-1, C23H3.4
Organism
Caenorhabditis elegans
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

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.1 Publication

Catalytic activityi

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

Cofactori

Pyridoxal phosphate By similarity.

Pathwayi

GO - Molecular functioni

  1. pyridoxal phosphate binding Source: InterPro
  2. serine C-palmitoyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. biosynthetic process Source: InterPro
  2. establishment or maintenance of epithelial cell apical/basal polarity Source: UniProtKB
  3. sphingolipid metabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid metabolism, Sphingolipid metabolism

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiREACT_183003. Sphingolipid de novo biosynthesis.
UniPathwayiUPA00222.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:sptl-1
ORF Names:C23H3.4
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940: Chromosome II

Organism-specific databases

WormBaseiC23H3.4a; CE08323; WBGene00016020; sptl-1.
C23H3.4b; CE37749; WBGene00016020; sptl-1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 458458Serine palmitoyltransferase 1
PRO_0000421271Add
BLAST

Proteomic databases

PaxDbiP91079.
PRIDEiP91079.

Interactioni

Subunit structurei

Heterodimer of sptl-1/sptl-2 or sptl-1/sptl-3 By similarity.

Protein-protein interaction databases

IntActiP91079. 1 interaction.
MINTiMINT-213137.
STRINGi6239.C23H3.4a.2.

Structurei

3D structure databases

ProteinModelPortaliP91079.
SMRiP91079. Positions 76-449.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0156.
GeneTreeiENSGT00550000074872.
HOGENOMiHOG000216602.
InParanoidiP91079.
OMAiTEMAING.
PhylomeDBiP91079.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequencei

Sequence statusi: Complete.

P91079-1 [UniParc]FASTAAdd to Basket

« Hide

MGFLPDSWHF YIETLLVALL AYVVMRNRSK RQQEKLSKKL TERQKDELIA    50
DWTPEPLVPE TPQDHPVLNP KYADGKMTKD VSIDGEKYLN MASTNFLSFI 100
GVKRIEDRAK QTIFKYGVGS CGPRGFYGTV DVHLDLEKEL AKFMGCEEAV 150
LYSYGFATVS SAIPAYAKKG DVIFVDEGVN FAIQKGLQAS RSRVEYFKHN 200
DMEHLERLLL EQEQRDKKDP KKAKSVRRFI VVEGLYVNYA DLCPLPKIIE 250
FKWRFKVRVF IDESWSFGVI GKTGRGVTEH FNVPMEDVDM VMASLENALA 300
STGGFCVGRS YVVGHQRLSG LGYCFSASLP PLLATAASEA ISIIDEEPSR 350
VQKVTEMAIN GQKKLQDALS GSKFSLQGCP ESPMKHIYYN GEDEEKQLDT 400
FVETVFTKNH LLLTRARYLD KDELFKIRPS IRVMFQHDLT EEEIQRAVDA 450
IRVVAHKF 458
Length:458
Mass (Da):52,085
Last modified:May 1, 1997 - v1
Checksum:i2F56AC94DFFABF91
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FO080632 Genomic DNA. Translation: CCD65323.1.
FO080632 Genomic DNA. Translation: CCD65324.1.
PIRiT25557.
RefSeqiNP_001021978.1. NM_001026807.2.
NP_001021979.1. NM_001026808.2.
UniGeneiCel.8663.

Genome annotation databases

EnsemblMetazoaiC23H3.4a.1; C23H3.4a.1; WBGene00016020.
C23H3.4a.2; C23H3.4a.2; WBGene00016020.
GeneIDi173389.
KEGGicel:CELE_C23H3.4.
UCSCiC23H3.4a.2. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FO080632 Genomic DNA. Translation: CCD65323.1 .
FO080632 Genomic DNA. Translation: CCD65324.1 .
PIRi T25557.
RefSeqi NP_001021978.1. NM_001026807.2.
NP_001021979.1. NM_001026808.2.
UniGenei Cel.8663.

3D structure databases

ProteinModelPortali P91079.
SMRi P91079. Positions 76-449.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P91079. 1 interaction.
MINTi MINT-213137.
STRINGi 6239.C23H3.4a.2.

Proteomic databases

PaxDbi P91079.
PRIDEi P91079.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai C23H3.4a.1 ; C23H3.4a.1 ; WBGene00016020 .
C23H3.4a.2 ; C23H3.4a.2 ; WBGene00016020 .
GeneIDi 173389.
KEGGi cel:CELE_C23H3.4.
UCSCi C23H3.4a.2. c. elegans.

Organism-specific databases

CTDi 173389.
WormBasei C23H3.4a ; CE08323 ; WBGene00016020 ; sptl-1.
C23H3.4b ; CE37749 ; WBGene00016020 ; sptl-1.

Phylogenomic databases

eggNOGi COG0156.
GeneTreei ENSGT00550000074872.
HOGENOMi HOG000216602.
InParanoidi P91079.
OMAi TEMAING.
PhylomeDBi P91079.

Enzyme and pathway databases

UniPathwayi UPA00222 .
Reactomei REACT_183003. Sphingolipid de novo biosynthesis.

Miscellaneous databases

NextBioi 879437.
PROi P91079.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
InterProi IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view ]
Pfami PF00155. Aminotran_1_2. 1 hit.
[Graphical view ]
SUPFAMi SSF53383. SSF53383. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiSPTC1_CAEEL
AccessioniPrimary (citable) accession number: P91079
Secondary accession number(s): Q5R3Y5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: May 1, 1997
Last modified: September 3, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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