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O54694 (SPTC2_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 89. 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 2

EC=2.3.1.50
Alternative name(s):
Long chain base biosynthesis protein 2
Short name=LCB 2
Long chain base biosynthesis protein 2a
Short name=LCB2a
Serine-palmitoyl-CoA transferase 2
Short name=SPT 2
Gene names
Name:SPTLC2
Synonyms:LCB2
OrganismCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Protein attributes

Sequence length560 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Serine palmitoyltransferase (SPT). The heterodimer formed with LCB1/SPTLC1 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-SPTLC2-SPTSSB complex displays a preference for C18-CoA substrate 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 SPTLC1. Component of the serine palmitoyltransferase (SPT) complex, composed of LCB1/SPTLC1, LCB2 (SPTLC2 or SPTLC3) and ssPT (SPTSSA or SPTSSB) By similarity.

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein 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 – 560560Serine palmitoyltransferase 2
PRO_0000163857

Regions

Transmembrane65 – 8521Helical; Potential

Amino acid modifications

Modified residue3771N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
O54694 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: C835A5E0244878E6

FASTA56062,882
        10         20         30         40         50         60 
MRPEPGGCCC RRPLRANGCV KNGEVRNGYV RSSTATAAAA GQIHHVTENG GLYKRPFNEV 

        70         80         90        100        110        120 
FEETPMLVAV LTYVGYGVLT LFGYLRDFLR HWRIEKCHHA TEREEQKDFV SLYQDFENFY 

       130        140        150        160        170        180 
TRNLYMRIRD NWNRPICSVP GARVDIMERQ SHDYNWSFKY TGNIIKGVIN MGSYNYLGFA 

       190        200        210        220        230        240 
RNTGSCQEAA AEVLKEYGAG VCSTRQEIGN LDKHEELEKL VARFLGVEAA MTYGMGFATN 

       250        260        270        280        290        300 
SMNIPALVGK GCLILSDELN HASLVLGARL SGATIRIFKH NNMQSLEKLL KDAIVYGQPR 

       310        320        330        340        350        360 
TRRPWKKILI LVEGIYSMEG SIVRLPEVIA LKKKYKAYLY LDEAHSIGAL GPSGRGVVDY 

       370        380        390        400        410        420 
FGLDPEDVDV MMGTFTKSFG ASGGYIGGKK ALIDYLRTHS HSAVYATSMS PPVMEQIITS 

       430        440        450        460        470        480 
MKCIMGQDGT SLGKECVQQL AENTKYFRRR LKEMGFIIYG NEDSPVVPLM LYMPAKIGAF 

       490        500        510        520        530        540 
GREMLKRNVG VVVVGFPATP IIESRARFCL SAAHTKEILD TALKEIDEVG DLLQLKYSRR 

       550        560 
RLVPLLDRPF DETTYEETED 

« Hide

References

[1]"A mammalian homolog of the yeast LCB1 encodes a component of serine palmitoyltransferase, the enzyme catalyzing the first step in sphingolipid synthesis."
Hanada K., Hara T., Nishijima M., Kuge O., Dickson R.C., Nagiec M.M.
J. Biol. Chem. 272:32108-32114(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Ovary.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF004830 mRNA. Translation: AAC53504.1.
RefSeqNP_001233609.1. NM_001246680.1.

3D structure databases

ProteinModelPortalO54694.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEO54694.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100689415.
KEGGcge:100689415.

Phylogenomic databases

HOVERGENHBG002230.
KOK00654.

Enzyme and pathway databases

UniPathwayUPA00222.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. 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.
PROSITEPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSPTC2_CRIGR
AccessionPrimary (citable) accession number: O54694
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: February 19, 2014
This is version 89 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