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

Q8BG54 (SPTC3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. 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 3

EC=2.3.1.50
Alternative name(s):
Long chain base biosynthesis protein 2b
Short name=LCB2b
Long chain base biosynthesis protein 3
Short name=LCB 3
Serine-palmitoyl-CoA transferase 3
Short name=SPT 3
Gene names
Name:Sptlc3
Synonyms:Sptlc2l
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length563 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-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, while the SPTLC1-SPTLC3-SPTSSB has the ability to use a broader range of acyl-CoAs without apparent preference 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 caution

The sequence AAH94496.1 differs from that shown. Reason: Frameshift at position 420.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 563563Serine palmitoyltransferase 3
PRO_0000304978

Regions

Transmembrane59 – 7921Helical; Potential

Amino acid modifications

Modified residue3711N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8BG54 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: C373554525D2E980

FASTA56363,486
        10         20         30         40         50         60 
MANLNDSAVT NGTLHNPKTQ QGKRQSTGCV KNGISKEAQQ NRKAYAEDKP VFEPYQEAPL 

        70         80         90        100        110        120 
YVYVLTYMGY GIGILFGYLR DFMRNWGIEK CNAAVEREEQ KDFVPLYQDF ENFYKRNLYM 

       130        140        150        160        170        180 
RIRDSWSHTV CSAPEPYMNV MEKVTDDYNW TFRHTGKVIE NIINMASYNY LGLAGKYDDS 

       190        200        210        220        230        240 
MVRVKDTLEK YGVGVASTRN EMGTLDIHKE LEDLMAEFLN VEAVMSFGMG FATNAMNIPV 

       250        260        270        280        290        300 
FVGKGCLILS DEFNHTSVIL GSRLSGAVIR PFKHNNAENL EKLLREAIIR GQPGTGRAWK 

       310        320        330        340        350        360 
KILIVVEGVY SMEGSIVNLA QIVALKKKYK AYLYIDEAHS IGCTGPTGRG VRELFGLDPE 

       370        380        390        400        410        420 
DIDVYMGTFT KSFSGSGGYI GGKKEIVDYL RMQSHSTTYA TSMSPVVAAQ LIRSLKITMG 

       430        440        450        460        470        480 
YEGNIGGMER IQQLKENIKY FRRRLKEMGF IIYGNDFSPV IPVLLYMPAK VSAFSRFLLK 

       490        500        510        520        530        540 
KKISVVVVGF PATSLPEGRA RFSMSSAHTR EMLDTVLEVV DELGDLLNVK YFPLKKSGRA 

       550        560 
ILYNKEGFDN EASFEEMHSE PEA 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryonic head, Eye and Oviduct.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"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].
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK048374 mRNA. Translation: BAC33316.1.
AK054240 mRNA. Translation: BAC35701.1.
AK078679 mRNA. Translation: BAC37356.1.
AK078686 mRNA. Translation: BAC37359.1.
AL928899 Genomic DNA. Translation: CAM21721.1.
BC094496 mRNA. Translation: AAH94496.1. Frameshift.
CCDSCCDS16800.1.
RefSeqNP_780676.1. NM_175467.3.
XP_006499358.1. XM_006499295.1.
UniGeneMm.100450.

3D structure databases

ProteinModelPortalQ8BG54.
SMRQ8BG54. Positions 160-527.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8BG54. 2 interactions.
MINTMINT-7985027.

PTM databases

PhosphoSiteQ8BG54.

Proteomic databases

PRIDEQ8BG54.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000047370; ENSMUSP00000048313; ENSMUSG00000039092.
ENSMUST00000110083; ENSMUSP00000105710; ENSMUSG00000039092.
GeneID228677.
KEGGmmu:228677.
UCSCuc008mpd.1. mouse.

Organism-specific databases

CTD55304.
MGIMGI:2444678. Sptlc3.

Phylogenomic databases

eggNOGCOG0156.
GeneTreeENSGT00550000074678.
HOGENOMHOG000206826.
HOVERGENHBG002230.
InParanoidQ8BG54.
KOK00654.
OMASTRNEMG.
OrthoDBEOG73RBB0.
PhylomeDBQ8BG54.
TreeFamTF300452.

Enzyme and pathway databases

UniPathwayUPA00222.

Gene expression databases

BgeeQ8BG54.
GenevestigatorQ8BG54.

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

NextBio379074.
PROQ8BG54.
SOURCESearch...

Entry information

Entry nameSPTC3_MOUSE
AccessionPrimary (citable) accession number: Q8BG54
Secondary accession number(s): Q505L2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 102 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

MGD cross-references

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