Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Serine palmitoyltransferase 2

Gene

lcb2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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 activityi

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

Cofactori

Pathwayi

GO - Molecular functioni

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

GO - Biological processi

  1. sphingolipid biosynthetic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid metabolism, Sphingolipid metabolism

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiREACT_335433. Sphingolipid de novo biosynthesis.
UniPathwayiUPA00222.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine palmitoyltransferase 2 (EC:2.3.1.50)
Short name:
SPT 2
Alternative name(s):
Long chain base biosynthesis protein 2
Gene namesi
Name:lcb2
ORF Names:SPAC21E11.08, SPAC2C4.02
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

PomBaseiSPAC21E11.08.

Subcellular locationi

Cytoplasm By similarity. Endoplasmic reticulum 1 Publication. Membrane Curated; Single-pass membrane protein Curated

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei90 – 10718HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: PomBase
  2. integral component of membrane Source: UniProtKB-KW
  3. serine C-palmitoyltransferase complex Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 603603Serine palmitoyltransferase 2PRO_0000163861Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei398 – 3981N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

MaxQBiQ09925.
PRIDEiQ09925.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi280491. 5 interactions.
MINTiMINT-4696465.
STRINGi4896.SPAC21E11.08-1.

Structurei

3D structure databases

ProteinModelPortaliQ09925.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0156.
HOGENOMiHOG000206826.
InParanoidiQ09925.
KOiK00654.
OMAiINAFSHE.
OrthoDBiEOG7XPZG0.
PhylomeDBiQ09925.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR001917. 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]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q09925-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQADFVSPT SIDVSEKKEV EFHKKVDHVE NPPLSTESAK LEAEEVAAEK
60 70 80 90 100
LNSEHLLENE FAPITDPTHR RVSKNPDGAE LFQFEDEPSY YYVVATYLTY
110 120 130 140 150
LVLIIIGHVR DFFGKRFHKD DYKYLKDNDG YAPLYNHFDN FYVRRLQHRI
160 170 180 190 200
NDCFSRPTMG VPGRVIRLMN RYSTDSNSTF KLTGDTSLAL NVSSYNYLGF
210 220 230 240 250
AQSHGPCATK VEEAMQKYGL STCSSNAICG TYGLHKEVEE LTANFVGKPA
260 270 280 290 300
ALVFSQGFST NATVFSTLMC PGSLIISDEL NHTSIRFGAR LSGANIRVYK
310 320 330 340 350
HNDMTDLERV LREVISQGQP RTHRPYSKIL VVIEGLYSME GNFCDLPKVV
360 370 380 390 400
ELKNRYKFYL FIDEAHSIGA IGPRGGGICD YFGISTDHVD ILMGTFTKSF
410 420 430 440 450
GAAGGYISAT PNIINKLRVT NPGYVYAESM SPAVLAQIKS SFLEIMDNSP
460 470 480 490 500
TSAGLERIER LAFNSRYIRL GLKRLGFIIF GNDDSPVVPL LLYNPGKINA
510 520 530 540 550
FSHEMLKRGI AVVVVGYPAC PLLTSRVRFC FSASHNKADM DYFLRACDEV
560 570 580 590 600
GEKLQLKFST GAAGEDVGKT NVEKMKKNQG WFKPPRWKIE DVLKHGVHDA

LTQ
Length:603
Mass (Da):67,519
Last modified:January 31, 1996 - v1
Checksum:i251A2383CC9B8472
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15645 Genomic DNA. Translation: AAC49534.1.
CU329670 Genomic DNA. Translation: CAA91967.2.
PIRiJC5183.
RefSeqiXP_001713103.1. XM_001713051.2.

Genome annotation databases

EnsemblFungiiSPAC21E11.08.1; SPAC21E11.08.1:pep; SPAC21E11.08.
GeneIDi3361415.
KEGGispo:SPAC21E11.08.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15645 Genomic DNA. Translation: AAC49534.1.
CU329670 Genomic DNA. Translation: CAA91967.2.
PIRiJC5183.
RefSeqiXP_001713103.1. XM_001713051.2.

3D structure databases

ProteinModelPortaliQ09925.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi280491. 5 interactions.
MINTiMINT-4696465.
STRINGi4896.SPAC21E11.08-1.

Proteomic databases

MaxQBiQ09925.
PRIDEiQ09925.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC21E11.08.1; SPAC21E11.08.1:pep; SPAC21E11.08.
GeneIDi3361415.
KEGGispo:SPAC21E11.08.

Organism-specific databases

PomBaseiSPAC21E11.08.

Phylogenomic databases

eggNOGiCOG0156.
HOGENOMiHOG000206826.
InParanoidiQ09925.
KOiK00654.
OMAiINAFSHE.
OrthoDBiEOG7XPZG0.
PhylomeDBiQ09925.

Enzyme and pathway databases

UniPathwayiUPA00222.
ReactomeiREACT_335433. Sphingolipid de novo biosynthesis.

Miscellaneous databases

NextBioi20811466.
PROiQ09925.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR001917. 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]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1995) [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.
    , 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(2001) [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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiLCB2_SCHPO
AccessioniPrimary (citable) accession number: Q09925
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 1996
Last sequence update: January 31, 1996
Last modified: March 31, 2015
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. 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.