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Protein

Serine palmitoyltransferase 1

Gene

SPTLC1

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

Pathway:isphingolipid metabolism

This protein is involved in the pathway sphingolipid metabolism, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway sphingolipid metabolism and in Lipid metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid metabolism, Sphingolipid metabolism

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

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:SPTLC1
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei16 – 3621HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 473473Serine palmitoyltransferase 1PRO_0000327869Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei164 – 1641Phosphotyrosine; by ABLBy similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000021706.

Structurei

3D structure databases

ProteinModelPortaliQ5R9T5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000216602.
HOVERGENiHBG003992.
InParanoidiQ5R9T5.
KOiK00654.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5R9T5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATATEQWVL VEMVQALYEA PAYHLILEGI LILWIIRLLF SKTYKLQERS
60 70 80 90 100
DLTVKEKEEL IEEWQPEPLV PLVPKDHPAL NYNIVSGPPS HKIVVNGKEC
110 120 130 140 150
INFASFNFLG LLDNPRVKAA ALASLKKYGV GTCGPRGFYG TFDVHLDLED
160 170 180 190 200
RLAKFMKTEE AIIYSYGFAT IASAIPAYSK RGDIVFVDRA ACFAIQKGLQ
210 220 230 240 250
ASRSDIKLFK HNDMADLERL LKEQEIEDQK NPRKARVTRR FIVVEGLYMN
260 270 280 290 300
TGTICPLPEL VKLKYKYKAR IFLEESLSFG VLGEHGRGVT EHYGINIDDI
310 320 330 340 350
DLISANMENA LASIGGFCCG RSFVIDHQRL SGQGYCFSAS LPPLLAAAAI
360 370 380 390 400
EALNIMEENP GIFAVLKEKC RQIHKALQGI SGLKVVGEPL SPAFHLQLEE
410 420 430 440 450
STGSREQDVR LLQEIVDQCM NRSIALTQAR YLEKEEKCLP PPSIRVVVTV
460 470
EQTEEELDRA ASTIKEVAQA VLL
Length:473
Mass (Da):52,867
Last modified:December 21, 2004 - v1
Checksum:i64BCBB758A79B632
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti158 – 1581T → I in CAH92367 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR859297 mRNA. Translation: CAH91475.1.
CR860225 mRNA. Translation: CAH92367.1.
RefSeqiNP_001126393.1. NM_001132921.1.

Genome annotation databases

GeneIDi100173375.
KEGGipon:100173375.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR859297 mRNA. Translation: CAH91475.1.
CR860225 mRNA. Translation: CAH92367.1.
RefSeqiNP_001126393.1. NM_001132921.1.

3D structure databases

ProteinModelPortaliQ5R9T5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000021706.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100173375.
KEGGipon:100173375.

Organism-specific databases

CTDi10558.

Phylogenomic databases

HOGENOMiHOG000216602.
HOVERGENiHBG003992.
InParanoidiQ5R9T5.
KOiK00654.

Enzyme and pathway databases

UniPathwayiUPA00222.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiSPTC1_PONAB
AccessioniPrimary (citable) accession number: Q5R9T5
Secondary accession number(s): Q5R793
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: December 21, 2004
Last modified: June 24, 2015
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.