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O35704 (SPTC1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. 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 1

EC=2.3.1.50
Alternative name(s):
Long chain base biosynthesis protein 1
Short name=LCB 1
Serine-palmitoyl-CoA transferase 1
Short name=SPT 1
Short name=SPT1
Gene names
Name:Sptlc1
Synonyms:Lcb1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Serine palmitoyltransferase (SPT). The heterodimer formed with SPTLC2 or SPTLC3 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-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates. The SPTLC1-SPTLC2-SPTSSB complex displays a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme has the ability to use a broader range of acyl-CoAs 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 SPTLC2 or SPTLC3. Component of the serine palmitoyltransferase (SPT) complex, composed of SPTLC1, either SPTLC2 or SPTLC3, and either SPTSSA or SPTSSB. Interacts with SPTSSA and SPTSSB; the interaction is direct. Interacts with ORMDL3 By similarity.

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein Ref.5.

Tissue specificity

Expressed in a variety of tissues. Highest expression in brain, kidney and liver.

Post-translational modification

Phosphorylation at Tyr-164 inhibits activity and promotes cell survival By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 473473Serine palmitoyltransferase 1
PRO_0000163855

Regions

Topological domain1 – 1515Lumenal Potential
Transmembrane16 – 3621Helical; Potential
Topological domain37 – 473437Cytoplasmic Potential

Amino acid modifications

Modified residue1641Phosphotyrosine; by ABL By similarity

Experimental info

Sequence conflict6 – 72EQ → DE in AAC02264. Ref.2
Sequence conflict851V → E in AAC02264. Ref.2
Sequence conflict1201T → A in CAA64897. Ref.1
Sequence conflict1201T → A in AAC02264. Ref.2
Sequence conflict1651S → T in AAC02264. Ref.2
Sequence conflict1711I → V in CAA64897. Ref.1
Sequence conflict1711I → V in AAC02264. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O35704 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 5B037E344DDEB4A7

FASTA47352,535
        10         20         30         40         50         60 
MATVAEQWVL VEMVQALYEA PAYHLILEGI LILWIIRLVF SKTYKLQERS DLTAKEKEEL 

        70         80         90        100        110        120 
IEEWQPEPLV PPVSKNHPAL NYNIVSGPPT HNIVVNGKEC VNFASFNFLG LLANPRVKAT 

       130        140        150        160        170        180 
AFSSLKKYGV GTCGPRGFYG TFDVHLDLEE RLAKFMKTEE AIIYSYGFST IASAIPAYSK 

       190        200        210        220        230        240 
RGDIIFVDSA ACFAIQKGLQ ASRSDIKLFK HNDVADLERL LKEQEIEDQK NPRKARVTRR 

       250        260        270        280        290        300 
FIVVEGLYMN TGTICPLPEL VKLKYKYKAR IFLEESLSFG VLGEHGRGVT EHYGISIDDI 

       310        320        330        340        350        360 
DLISANMENA LASVGGFCCG RSFVVDHQRL SGQGYCFSAS LPPLLAAAAI EALNIMEENP 

       370        380        390        400        410        420 
DIFAVLKKKC QNIHKSLQGV SGLKVVGESL SPALHLQLEE STGSREKDVK LLQAIVDQCM 

       430        440        450        460        470 
DKGIALTQAR YLDKEEKCLP PPSIRVVVTV EQTEEELQRA ASTIREAAQA VLL 

« Hide

References

« Hide 'large scale' references
[1]"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.
[2]"A mammalian homolog of the yeast LCB1 encodes a component of serine palmitoyltransferase, the enzyme catalyzing the first step in sphingolipid synthesis."
Hanada K., Hara T., Nishijima M., Kuge O., Dickson R.C., Nagiec M.M.
J. Biol. Chem. 272:32108-32114(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney and Testis.
[3]"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: Eye, Hypothalamus and Lung.
[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].
Tissue: Olfactory epithelium.
[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
X95641 mRNA. Translation: CAA64897.1.
AF003823 mRNA. Translation: AAC02264.1.
AK053207 mRNA. Translation: BAC35310.1.
AK079578 mRNA. Translation: BAC37690.1.
AK084391 mRNA. Translation: BAC39172.1.
AK084445 mRNA. Translation: BAC39185.1.
BC046323 mRNA. Translation: AAH46323.1.
CCDSCCDS26521.1.
RefSeqNP_033295.2. NM_009269.2.
UniGeneMm.240336.

3D structure databases

ProteinModelPortalO35704.
SMRO35704. Positions 93-471.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid234529. 2 interactions.
IntActO35704. 1 interaction.
MINTMINT-4100281.
STRING10090.ENSMUSP00000021920.

PTM databases

PhosphoSiteO35704.

Proteomic databases

MaxQBO35704.
PaxDbO35704.
PRIDEO35704.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021920; ENSMUSP00000021920; ENSMUSG00000021468.
GeneID268656.
KEGGmmu:268656.
UCSCuc007qnk.2. mouse.

Organism-specific databases

CTD10558.
MGIMGI:1099431. Sptlc1.

Phylogenomic databases

eggNOGCOG0156.
GeneTreeENSGT00550000074872.
HOGENOMHOG000216602.
HOVERGENHBG003992.
InParanoidQ8BH11.
KOK00654.
OMAVNHQRIN.
OrthoDBEOG786H30.
TreeFamTF314877.

Enzyme and pathway databases

UniPathwayUPA00222.

Gene expression databases

ArrayExpressO35704.
BgeeO35704.
GenevestigatorO35704.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR004839. 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.
ProtoNetSearch...

Other

NextBio392410.
PROO35704.
SOURCESearch...

Entry information

Entry nameSPTC1_MOUSE
AccessionPrimary (citable) accession number: O35704
Secondary accession number(s): O54813, Q8BH11
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 118 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