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O35704

- SPTC1_MOUSE

UniProt

O35704 - SPTC1_MOUSE

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Protein

Serine palmitoyltransferase 1

Gene

Sptlc1

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

Functioni

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).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. transferase activity, transferring acyl groups Source: UniProtKB-KW

GO - Biological processi

  1. ceramide biosynthetic process Source: MGI
  2. sphinganine biosynthetic process Source: MGI
  3. sphingomyelin biosynthetic process Source: MGI
  4. sphingosine biosynthetic process Source: MGI
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 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 namesi
Name:Sptlc1
Synonyms:Lcb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:1099431. Sptlc1.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Single-pass membrane protein 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 473473Serine palmitoyltransferase 1PRO_0000163855Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei164 – 1641Phosphotyrosine; by ABLBy similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO35704.
PaxDbiO35704.
PRIDEiO35704.

PTM databases

PhosphoSiteiO35704.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiO35704.
ExpressionAtlasiO35704. baseline and differential.
GenevestigatoriO35704.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi234529. 2 interactions.
IntActiO35704. 1 interaction.
MINTiMINT-4100281.
STRINGi10090.ENSMUSP00000021920.

Structurei

3D structure databases

ProteinModelPortaliO35704.
SMRiO35704. Positions 93-471.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1515LumenalSequence AnalysisAdd
BLAST
Topological domaini37 – 473437CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei16 – 3621HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0156.
GeneTreeiENSGT00550000074872.
HOGENOMiHOG000216602.
HOVERGENiHBG003992.
InParanoidiO35704.
KOiK00654.
OMAiVNHQRIN.
OrthoDBiEOG786H30.
TreeFamiTF314877.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. 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.

Sequencei

Sequence statusi: Complete.

O35704 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATVAEQWVL VEMVQALYEA PAYHLILEGI LILWIIRLVF SKTYKLQERS
60 70 80 90 100
DLTAKEKEEL IEEWQPEPLV PPVSKNHPAL NYNIVSGPPT HNIVVNGKEC
110 120 130 140 150
VNFASFNFLG LLANPRVKAT AFSSLKKYGV GTCGPRGFYG TFDVHLDLEE
160 170 180 190 200
RLAKFMKTEE AIIYSYGFST IASAIPAYSK RGDIIFVDSA ACFAIQKGLQ
210 220 230 240 250
ASRSDIKLFK HNDVADLERL LKEQEIEDQK NPRKARVTRR FIVVEGLYMN
260 270 280 290 300
TGTICPLPEL VKLKYKYKAR IFLEESLSFG VLGEHGRGVT EHYGISIDDI
310 320 330 340 350
DLISANMENA LASVGGFCCG RSFVVDHQRL SGQGYCFSAS LPPLLAAAAI
360 370 380 390 400
EALNIMEENP DIFAVLKKKC QNIHKSLQGV SGLKVVGESL SPALHLQLEE
410 420 430 440 450
STGSREKDVK LLQAIVDQCM DKGIALTQAR YLDKEEKCLP PPSIRVVVTV
460 470
EQTEEELQRA ASTIREAAQA VLL
Length:473
Mass (Da):52,535
Last modified:July 27, 2011 - v2
Checksum:i5B037E344DDEB4A7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 72EQ → DE in AAC02264. (PubMed:9405408)Curated
Sequence conflicti85 – 851V → E in AAC02264. (PubMed:9405408)Curated
Sequence conflicti120 – 1201T → A in CAA64897. (PubMed:9363775)Curated
Sequence conflicti120 – 1201T → A in AAC02264. (PubMed:9405408)Curated
Sequence conflicti165 – 1651S → T in AAC02264. (PubMed:9405408)Curated
Sequence conflicti171 – 1711I → V in CAA64897. (PubMed:9363775)Curated
Sequence conflicti171 – 1711I → V in AAC02264. (PubMed:9405408)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS26521.1.
RefSeqiNP_033295.2. NM_009269.2.
UniGeneiMm.240336.

Genome annotation databases

EnsembliENSMUST00000021920; ENSMUSP00000021920; ENSMUSG00000021468.
GeneIDi268656.
KEGGimmu:268656.
UCSCiuc007qnk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS26521.1.
RefSeqi NP_033295.2. NM_009269.2.
UniGenei Mm.240336.

3D structure databases

ProteinModelPortali O35704.
SMRi O35704. Positions 93-471.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 234529. 2 interactions.
IntActi O35704. 1 interaction.
MINTi MINT-4100281.
STRINGi 10090.ENSMUSP00000021920.

PTM databases

PhosphoSitei O35704.

Proteomic databases

MaxQBi O35704.
PaxDbi O35704.
PRIDEi O35704.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000021920 ; ENSMUSP00000021920 ; ENSMUSG00000021468 .
GeneIDi 268656.
KEGGi mmu:268656.
UCSCi uc007qnk.2. mouse.

Organism-specific databases

CTDi 10558.
MGIi MGI:1099431. Sptlc1.

Phylogenomic databases

eggNOGi COG0156.
GeneTreei ENSGT00550000074872.
HOGENOMi HOG000216602.
HOVERGENi HBG003992.
InParanoidi O35704.
KOi K00654.
OMAi VNHQRIN.
OrthoDBi EOG786H30.
TreeFami TF314877.

Enzyme and pathway databases

UniPathwayi UPA00222 .
Reactomei REACT_198151. Sphingolipid de novo biosynthesis.

Miscellaneous databases

NextBioi 392410.
PROi O35704.
SOURCEi Search...

Gene expression databases

Bgeei O35704.
ExpressionAtlasi O35704. baseline and differential.
Genevestigatori O35704.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProi 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.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiSPTC1_MOUSE
AccessioniPrimary (citable) accession number: O35704
Secondary accession number(s): O54813, Q8BH11
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 121 of the entry and version 2 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