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Q8BG54

- SPTC3_MOUSE

UniProt

Q8BG54 - SPTC3_MOUSE

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Protein

Serine palmitoyltransferase 3

Gene

Sptlc3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

Pyridoxal phosphate.By similarity

Pathwayi

GO - Molecular functioni

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

GO - Biological processi

  1. sphingoid biosynthetic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid metabolism, Sphingolipid metabolism

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiREACT_198151. Sphingolipid de novo biosynthesis.
UniPathwayiUPA00222.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Sptlc3
Synonyms:Sptlc2l
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:2444678. Sptlc3.

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. serine C-palmitoyltransferase complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 563563Serine palmitoyltransferase 3PRO_0000304978Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei371 – 3711N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PRIDEiQ8BG54.

PTM databases

PhosphoSiteiQ8BG54.

Expressioni

Gene expression databases

BgeeiQ8BG54.
GenevestigatoriQ8BG54.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

IntActiQ8BG54. 2 interactions.
MINTiMINT-7985027.

Structurei

3D structure databases

ProteinModelPortaliQ8BG54.
SMRiQ8BG54. Positions 160-527.
ModBaseiSearch...
MobiDBiSearch...

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei59 – 7921HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0156.
GeneTreeiENSGT00550000074678.
HOGENOMiHOG000206826.
HOVERGENiHBG002230.
InParanoidiQ8BG54.
KOiK00654.
OMAiSTRNEMG.
OrthoDBiEOG73RBB0.
PhylomeDBiQ8BG54.
TreeFamiTF300452.

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.

Q8BG54-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MANLNDSAVT NGTLHNPKTQ QGKRQSTGCV KNGISKEAQQ NRKAYAEDKP
60 70 80 90 100
VFEPYQEAPL YVYVLTYMGY GIGILFGYLR DFMRNWGIEK CNAAVEREEQ
110 120 130 140 150
KDFVPLYQDF ENFYKRNLYM RIRDSWSHTV CSAPEPYMNV MEKVTDDYNW
160 170 180 190 200
TFRHTGKVIE NIINMASYNY LGLAGKYDDS MVRVKDTLEK YGVGVASTRN
210 220 230 240 250
EMGTLDIHKE LEDLMAEFLN VEAVMSFGMG FATNAMNIPV FVGKGCLILS
260 270 280 290 300
DEFNHTSVIL GSRLSGAVIR PFKHNNAENL EKLLREAIIR GQPGTGRAWK
310 320 330 340 350
KILIVVEGVY SMEGSIVNLA QIVALKKKYK AYLYIDEAHS IGCTGPTGRG
360 370 380 390 400
VRELFGLDPE DIDVYMGTFT KSFSGSGGYI GGKKEIVDYL RMQSHSTTYA
410 420 430 440 450
TSMSPVVAAQ LIRSLKITMG YEGNIGGMER IQQLKENIKY FRRRLKEMGF
460 470 480 490 500
IIYGNDFSPV IPVLLYMPAK VSAFSRFLLK KKISVVVVGF PATSLPEGRA
510 520 530 540 550
RFSMSSAHTR EMLDTVLEVV DELGDLLNVK YFPLKKSGRA ILYNKEGFDN
560
EASFEEMHSE PEA
Length:563
Mass (Da):63,486
Last modified:March 1, 2003 - v1
Checksum:iC373554525D2E980
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS16800.1.
RefSeqiNP_780676.1. NM_175467.3.
XP_006499358.1. XM_006499295.1.
UniGeneiMm.100450.

Genome annotation databases

EnsembliENSMUST00000047370; ENSMUSP00000048313; ENSMUSG00000039092.
ENSMUST00000110083; ENSMUSP00000105710; ENSMUSG00000039092.
GeneIDi228677.
KEGGimmu:228677.
UCSCiuc008mpd.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS16800.1.
RefSeqi NP_780676.1. NM_175467.3.
XP_006499358.1. XM_006499295.1.
UniGenei Mm.100450.

3D structure databases

ProteinModelPortali Q8BG54.
SMRi Q8BG54. Positions 160-527.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8BG54. 2 interactions.
MINTi MINT-7985027.

PTM databases

PhosphoSitei Q8BG54.

Proteomic databases

PRIDEi Q8BG54.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000047370 ; ENSMUSP00000048313 ; ENSMUSG00000039092 .
ENSMUST00000110083 ; ENSMUSP00000105710 ; ENSMUSG00000039092 .
GeneIDi 228677.
KEGGi mmu:228677.
UCSCi uc008mpd.1. mouse.

Organism-specific databases

CTDi 55304.
MGIi MGI:2444678. Sptlc3.

Phylogenomic databases

eggNOGi COG0156.
GeneTreei ENSGT00550000074678.
HOGENOMi HOG000206826.
HOVERGENi HBG002230.
InParanoidi Q8BG54.
KOi K00654.
OMAi STRNEMG.
OrthoDBi EOG73RBB0.
PhylomeDBi Q8BG54.
TreeFami TF300452.

Enzyme and pathway databases

UniPathwayi UPA00222 .
Reactomei REACT_198151. Sphingolipid de novo biosynthesis.

Miscellaneous databases

NextBioi 379074.
PROi Q8BG54.
SOURCEi Search...

Gene expression databases

Bgeei Q8BG54.
Genevestigatori Q8BG54.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProi IPR001917. 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 ]
Pfami PF00155. Aminotran_1_2. 1 hit.
[Graphical view ]
SUPFAMi SSF53383. SSF53383. 1 hit.
PROSITEi PS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.
    , 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. 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.

Entry informationi

Entry nameiSPTC3_MOUSE
AccessioniPrimary (citable) accession number: Q8BG54
Secondary accession number(s): Q505L2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: March 1, 2003
Last modified: October 1, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3