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

P97363 (SPTC2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. 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 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 Ref.5.

Tissue specificity

Expressed in a variety of tissues.

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_0000163859

Regions

Transmembrane65 – 8521Helical; Potential

Amino acid modifications

Modified residue3771N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P97363 [UniParc].

Last modified January 1, 1998. Version 2.
Checksum: 6429566979B18D1C

FASTA56062,982
        10         20         30         40         50         60 
MRPEPGGCCC RRPMRANGCV KNGEVRNGYL RSSTATVAAA GQIHHVTENG GLYKRPFNEA 

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

       130        140        150        160        170        180 
TRNLYMRIRD NWNRPICSVP GAKVDIMERK 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 ELIDYLRTHS HSAVYATSMS PPVMEQIITS 

       430        440        450        460        470        480 
MKCIMGQDGT SLGKECIQQL AENTRYFRRR LKEMGFIIYG NEDSPVVPLM LYMPAKIGAF 

       490        500        510        520        530        540 
GREMLKRNIG VVVVGFPATP IIESRARFCL SAAHTKEILD TALKEIDEVG DLLQLKYSRH 

       550        560 
RLVPLLDRPF DETTYEETED 

« Hide

References

« Hide 'large scale' references
[1]"Sphingolipid synthesis: identification and characterization of mammalian cDNAs encoding the Lcb2 subunit of serine palmitoyltransferase."
Nagiec M.M., Lester R.L., Dickson R.C.
Gene 177:237-241(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney and Testis.
[2]Nagiec M.M., Lester R.L., Dickson R.C.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Human and murine serine-palmitoyl-CoA transferase. Cloning, expression and characterization of the key enzyme in sphingolipid synthesis."
Weiss B., Stoffel W.
Eur. J. Biochem. 249:239-247(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Kidney and Liver.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Mammary gland.
[5]"Subcellular localization and membrane topology of serine palmitoyltransferase, 3-dehydrosphinganine reductase, and sphinganine N-acyltransferase in mouse liver."
Mandon E.C., Ehses I., Rother J., van Echten G., Sandhoff K.
J. Biol. Chem. 267:11144-11148(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U27455 mRNA. Translation: AAC53310.1.
X95642 mRNA. Translation: CAA64898.1.
BC003227 mRNA. Translation: AAH03227.1.
CCDSCCDS26076.1.
PIRJC5180.
RefSeqNP_035609.1. NM_011479.3.
UniGeneMm.565.

3D structure databases

ProteinModelPortalP97363.
SMRP97363. Positions 110-533.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP97363. 1 interaction.
MINTMINT-4100293.

PTM databases

PhosphoSiteP97363.

Proteomic databases

MaxQBP97363.
PaxDbP97363.
PRIDEP97363.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021424; ENSMUSP00000021424; ENSMUSG00000021036.
GeneID20773.
KEGGmmu:20773.
UCSCuc007oiw.1. mouse.

Organism-specific databases

CTD9517.
MGIMGI:108074. Sptlc2.

Phylogenomic databases

eggNOGCOG0156.
HOGENOMHOG000206826.
HOVERGENHBG002230.
InParanoidP97363.
KOK00654.
OMAPEPGGCC.
OrthoDBEOG73RBB0.
PhylomeDBP97363.
TreeFamTF300452.

Enzyme and pathway databases

UniPathwayUPA00222.

Gene expression databases

ArrayExpressP97363.
BgeeP97363.
GenevestigatorP97363.

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...

Other

ChiTaRSSPTLC2. mouse.
NextBio299487.
PROP97363.
SOURCESearch...

Entry information

Entry nameSPTC2_MOUSE
AccessionPrimary (citable) accession number: P97363
Secondary accession number(s): P97356
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 121 of the entry and version 2 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot