SPTC3_MOUSE
ID SPTC3_MOUSE Reviewed; 563 AA.
AC Q8BG54; Q505L2;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Serine palmitoyltransferase 3 {ECO:0000305};
DE EC=2.3.1.50 {ECO:0000250|UniProtKB:Q9NUV7};
DE AltName: Full=Long chain base biosynthesis protein 2b;
DE Short=LCB2b;
DE AltName: Full=Long chain base biosynthesis protein 3;
DE Short=LCB 3;
DE AltName: Full=Serine-palmityl-CoA transferase 3;
DE Short=SPT 3;
GN Name=Sptlc3 {ECO:0000312|MGI:MGI:2444678}; Synonyms=Sptlc2l;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic head, Eye, and Oviduct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=27818258; DOI=10.1016/j.cmet.2016.10.002;
RA Chaurasia B., Kaddai V.A., Lancaster G.I., Henstridge D.C., Sriram S.,
RA Galam D.L., Gopalan V., Prakash K.N., Velan S.S., Bulchand S., Tsong T.J.,
RA Wang M., Siddique M.M., Yuguang G., Sigmundsson K., Mellet N.A., Weir J.M.,
RA Meikle P.J., Bin M Yassin M.S., Shabbir A., Shayman J.A., Hirabayashi Y.,
RA Shiow S.T., Sugii S., Summers S.A.;
RT "Adipocyte Ceramides Regulate Subcutaneous Adipose Browning, Inflammation,
RT and Metabolism.";
RL Cell Metab. 24:820-834(2016).
CC -!- FUNCTION: Serine palmitoyltransferase (SPT). The heterodimer formed
CC with LCB1/SPTLC1 constitutes the catalytic core. The composition of the
CC serine palmitoyltransferase (SPT) complex determines the substrate
CC preference. SPT complexes containing SPTLC3 generate shorter chain
CC sphingoid bases compared to complexes containing SPTLC2. The SPTLC1-
CC SPTLC3-SPTSSA isozyme uses C12-CoA, C14-CoA and C16-CoA as substrates,
CC with a slight preference for C14-CoA. On the other hand, the SPTLC1-
CC SPTLC3-SPTSSB has the ability to use a broader range of acyl-CoAs
CC without apparent preference. {ECO:0000250|UniProtKB:Q9NUV7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexadecanoyl-CoA + L-serine = 3-oxosphinganine + CO2 +
CC CoA; Xref=Rhea:RHEA:14761, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:58299; EC=2.3.1.50;
CC Evidence={ECO:0000250|UniProtKB:Q9NUV7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14762;
CC Evidence={ECO:0000250|UniProtKB:Q9NUV7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + H(+) + L-serine = 3-oxotetradecasphinganine +
CC CO2 + CoA; Xref=Rhea:RHEA:35679, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57375, ChEBI:CHEBI:71008;
CC Evidence={ECO:0000250|UniProtKB:Q9NUV7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35680;
CC Evidence={ECO:0000250|UniProtKB:Q9NUV7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-serine + tetradecanoyl-CoA = 3-oxohexadecasphinganine
CC + CO2 + CoA; Xref=Rhea:RHEA:35675, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57385, ChEBI:CHEBI:71007;
CC Evidence={ECO:0000250|UniProtKB:Q9NUV7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35676;
CC Evidence={ECO:0000250|UniProtKB:Q9NUV7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-serine + octadecanoyl-CoA = 3-oxoeicosasphinganine +
CC CO2 + CoA; Xref=Rhea:RHEA:33683, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57394, ChEBI:CHEBI:65073;
CC Evidence={ECO:0000250|UniProtKB:Q9NUV7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33684;
CC Evidence={ECO:0000250|UniProtKB:Q9NUV7};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC -!- SUBUNIT: Heterodimer with SPTLC1. Component of the serine
CC palmitoyltransferase (SPT) complex, composed of SPTLC1, either SPTLC2
CC or SPTLC3, and either SPTSSA or SPTSSB. The composition of the complex
CC will define the substrate specificity. {ECO:0000250|UniProtKB:Q9NUV7}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9NUV7}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9NUV7}.
CC -!- TISSUE SPECIFICITY: Expressed in white and brown adipose tissues.
CC {ECO:0000269|PubMed:27818258}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH94496.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK048374; BAC33316.1; -; mRNA.
DR EMBL; AK054240; BAC35701.1; -; mRNA.
DR EMBL; AK078679; BAC37356.1; -; mRNA.
DR EMBL; AK078686; BAC37359.1; -; mRNA.
DR EMBL; AL928899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC094496; AAH94496.1; ALT_FRAME; mRNA.
DR CCDS; CCDS16800.1; -.
DR RefSeq; NP_780676.1; NM_175467.3.
DR RefSeq; XP_006499358.1; XM_006499295.3.
DR AlphaFoldDB; Q8BG54; -.
DR SMR; Q8BG54; -.
DR BioGRID; 230752; 1.
DR IntAct; Q8BG54; 2.
DR MINT; Q8BG54; -.
DR STRING; 10090.ENSMUSP00000048313; -.
DR PhosphoSitePlus; Q8BG54; -.
DR PaxDb; Q8BG54; -.
DR PRIDE; Q8BG54; -.
DR ProteomicsDB; 254551; -.
DR Antibodypedia; 70994; 65 antibodies from 12 providers.
DR DNASU; 228677; -.
DR Ensembl; ENSMUST00000047370; ENSMUSP00000048313; ENSMUSG00000039092.
DR Ensembl; ENSMUST00000110083; ENSMUSP00000105710; ENSMUSG00000039092.
DR GeneID; 228677; -.
DR KEGG; mmu:228677; -.
DR UCSC; uc008mpd.1; mouse.
DR CTD; 55304; -.
DR MGI; MGI:2444678; Sptlc3.
DR VEuPathDB; HostDB:ENSMUSG00000039092; -.
DR eggNOG; KOG1357; Eukaryota.
DR GeneTree; ENSGT00940000158513; -.
DR HOGENOM; CLU_015846_7_1_1; -.
DR InParanoid; Q8BG54; -.
DR OMA; RICENSN; -.
DR OrthoDB; 438936at2759; -.
DR PhylomeDB; Q8BG54; -.
DR TreeFam; TF300452; -.
DR Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
DR UniPathway; UPA00222; -.
DR BioGRID-ORCS; 228677; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q8BG54; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BG54; protein.
DR Bgee; ENSMUSG00000039092; Expressed in urinary bladder urothelium and 81 other tissues.
DR Genevisible; Q8BG54; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0017059; C:serine C-palmitoyltransferase complex; ISO:MGI.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004758; F:serine C-palmitoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR GO; GO:0046520; P:sphingoid biosynthetic process; ISO:MGI.
DR GO; GO:0046512; P:sphingosine biosynthetic process; ISO:MGI.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Endoplasmic reticulum; Lipid metabolism; Membrane;
KW Pyridoxal phosphate; Reference proteome; Sphingolipid metabolism;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..563
FT /note="Serine palmitoyltransferase 3"
FT /id="PRO_0000304978"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 371
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 563 AA; 63486 MW; C373554525D2E980 CRC64;
MANLNDSAVT NGTLHNPKTQ QGKRQSTGCV KNGISKEAQQ NRKAYAEDKP VFEPYQEAPL
YVYVLTYMGY GIGILFGYLR DFMRNWGIEK CNAAVEREEQ KDFVPLYQDF ENFYKRNLYM
RIRDSWSHTV CSAPEPYMNV MEKVTDDYNW TFRHTGKVIE NIINMASYNY LGLAGKYDDS
MVRVKDTLEK YGVGVASTRN EMGTLDIHKE LEDLMAEFLN VEAVMSFGMG FATNAMNIPV
FVGKGCLILS DEFNHTSVIL GSRLSGAVIR PFKHNNAENL EKLLREAIIR GQPGTGRAWK
KILIVVEGVY SMEGSIVNLA QIVALKKKYK AYLYIDEAHS IGCTGPTGRG VRELFGLDPE
DIDVYMGTFT KSFSGSGGYI GGKKEIVDYL RMQSHSTTYA TSMSPVVAAQ LIRSLKITMG
YEGNIGGMER IQQLKENIKY FRRRLKEMGF IIYGNDFSPV IPVLLYMPAK VSAFSRFLLK
KKISVVVVGF PATSLPEGRA RFSMSSAHTR EMLDTVLEVV DELGDLLNVK YFPLKKSGRA
ILYNKEGFDN EASFEEMHSE PEA
