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Q09925 (LCB2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 110. 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

Short name=SPT 2
EC=2.3.1.50
Alternative name(s):
Long chain base biosynthesis protein 2
Gene names
Name:lcb2
ORF Names:SPAC21E11.08, SPAC2C4.02
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length603 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalytic subunit of serine palmitoyltransferase (SPT), which catalyzes the committed step in the synthesis of sphingolipids, the condensation of serine with palmitoyl CoA to form the long chain base 3-ketosphinganine 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

Lcb1 and lcb2 encode essential subunits of the enzyme and form a heterodimer By similarity.

Subcellular location

Cytoplasm By similarity. Endoplasmic reticulum. Membrane; Single-pass membrane protein Potential Ref.3.

Sequence similarities

Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 603603Serine palmitoyltransferase 2
PRO_0000163861

Regions

Transmembrane90 – 10718Helical; Potential

Amino acid modifications

Modified residue3981N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q09925 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 251A2383CC9B8472

FASTA60367,519
        10         20         30         40         50         60 
MAQADFVSPT SIDVSEKKEV EFHKKVDHVE NPPLSTESAK LEAEEVAAEK LNSEHLLENE 

        70         80         90        100        110        120 
FAPITDPTHR RVSKNPDGAE LFQFEDEPSY YYVVATYLTY LVLIIIGHVR DFFGKRFHKD 

       130        140        150        160        170        180 
DYKYLKDNDG YAPLYNHFDN FYVRRLQHRI NDCFSRPTMG VPGRVIRLMN RYSTDSNSTF 

       190        200        210        220        230        240 
KLTGDTSLAL NVSSYNYLGF AQSHGPCATK VEEAMQKYGL STCSSNAICG TYGLHKEVEE 

       250        260        270        280        290        300 
LTANFVGKPA ALVFSQGFST NATVFSTLMC PGSLIISDEL NHTSIRFGAR LSGANIRVYK 

       310        320        330        340        350        360 
HNDMTDLERV LREVISQGQP RTHRPYSKIL VVIEGLYSME GNFCDLPKVV ELKNRYKFYL 

       370        380        390        400        410        420 
FIDEAHSIGA IGPRGGGICD YFGISTDHVD ILMGTFTKSF GAAGGYISAT PNIINKLRVT 

       430        440        450        460        470        480 
NPGYVYAESM SPAVLAQIKS SFLEIMDNSP TSAGLERIER LAFNSRYIRL GLKRLGFIIF 

       490        500        510        520        530        540 
GNDDSPVVPL LLYNPGKINA FSHEMLKRGI AVVVVGYPAC PLLTSRVRFC FSASHNKADM 

       550        560        570        580        590        600 
DYFLRACDEV GEKLQLKFST GAAGEDVGKT NVEKMKKNQG WFKPPRWKIE DVLKHGVHDA 


LTQ 

« 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 [GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[3]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U15645 Genomic DNA. Translation: AAC49534.1.
CU329670 Genomic DNA. Translation: CAA91967.2.
PIRJC5183.
RefSeqXP_001713103.1. XM_001713051.2.

3D structure databases

ProteinModelPortalQ09925.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid280491. 5 interactions.
MINTMINT-4696465.
STRING4896.SPAC21E11.08-1.

Proteomic databases

MaxQBQ09925.
PRIDEQ09925.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC21E11.08.1; SPAC21E11.08.1:pep; SPAC21E11.08.
GeneID3361415.
KEGGspo:SPAC21E11.08.

Organism-specific databases

PomBaseSPAC21E11.08.

Phylogenomic databases

eggNOGCOG0156.
HOGENOMHOG000206826.
KOK00654.
OMAPMYVAVM.
OrthoDBEOG7XPZG0.
PhylomeDBQ09925.

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...

Other

NextBio20811466.
PROQ09925.

Entry information

Entry nameLCB2_SCHPO
AccessionPrimary (citable) accession number: Q09925
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 14, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways