LOCUS       NP_060797                552 aa            linear   PRI 27-APR-2025
DEFINITION  serine palmitoyltransferase 3 [Homo sapiens].
ACCESSION   NP_060797
VERSION     NP_060797.2
DBSOURCE    REFSEQ: accession NM_018327.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Lone,M.A., Bourquin,F. and Hornemann,T.
  TITLE     Serine Palmitoyltransferase Subunit 3 and Metabolic Diseases
  JOURNAL   Adv Exp Med Biol 1372, 47-56 (2022)
   PUBMED   35503173
  REMARK    GeneRIF: Serine Palmitoyltransferase Subunit 3 and Metabolic
            Diseases.
            Review article
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Luo,C., Liu,H., Wang,X., Xia,L., Huang,H., Peng,X., Xia,C. and
            Liu,L.
  TITLE     The associations between individual plasma SFAs, serine
            palmitoyl-transferase long-chain base subunit 3 gene rs680379
            polymorphism, and type 2 diabetes among Chinese adults
  JOURNAL   Am J Clin Nutr 114 (2), 704-712 (2021)
   PUBMED   33964854
  REMARK    GeneRIF: The associations between individual plasma SFAs, serine
            palmitoyl-transferase long-chain base subunit 3 gene rs680379
            polymorphism, and type 2 diabetes among Chinese adults.
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Wang,Y., Niu,Y., Zhang,Z., Gable,K., Gupta,S.D., Somashekarappa,N.,
            Han,G., Zhao,H., Myasnikov,A.G., Kalathur,R.C., Dunn,T.M. and
            Lee,C.H.
  TITLE     Structural insights into the regulation of human serine
            palmitoyltransferase complexes
  JOURNAL   Nat Struct Mol Biol 28 (3), 240-248 (2021)
   PUBMED   33558761
REFERENCE   4  (residues 1 to 552)
  AUTHORS   Nel,M., Jalali Sefid Dashti,M., Gamieldien,J. and Heckmann,J.M.
  TITLE     Exome sequencing identifies targets in the treatment-resistant
            ophthalmoplegic subphenotype of myasthenia gravis
  JOURNAL   Neuromuscul Disord 27 (9), 816-825 (2017)
   PUBMED   28673556
  REMARK    GeneRIF: This study demonstrated that the association of
            SPTLC3insACAC (p = 0.055) with the treatment-resistant
            ophthalmoplegic subphenotype of myasthenia gravis.
REFERENCE   5  (residues 1 to 552)
  AUTHORS   Zhang,Q.H., Yin,R.X., Gao,H., Huang,F., Wu,J.Z., Pan,S.L., Lin,W.X.
            and Yang,D.Z.
  TITLE     Association of the SPTLC3 rs364585 polymorphism and serum lipid
            profiles in two Chinese ethnic groups
  JOURNAL   Lipids Health Dis 16 (1), 1 (2017)
   PUBMED   28056980
  REMARK    GeneRIF: The association between the SPTLC3 rs364585 SNP and serum
            total cholesterol, high-density lipoprotein cholesterol and
            low-density lipoprotein cholesterol levels in the Han and Jing
            populations
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 552)
  AUTHORS   Hornemann,T., Penno,A., Rutti,M.F., Ernst,D., Kivrak-Pfiffner,F.,
            Rohrer,L. and von Eckardstein,A.
  TITLE     The SPTLC3 subunit of serine palmitoyltransferase generates short
            chain sphingoid bases
  JOURNAL   J Biol Chem 284 (39), 26322-26330 (2009)
   PUBMED   19648650
  REMARK    GeneRIF: Data show that the SPTLC3 subunit generates
            C(16)-sphingoid bases and that sphingolipids with a C(16) backbone
            constitute a significant proportion of plasma sphingolipids.
REFERENCE   7  (residues 1 to 552)
  AUTHORS   Han,G., Gupta,S.D., Gable,K., Niranjanakumari,S., Moitra,P.,
            Eichler,F., Brown,R.H. Jr., Harmon,J.M. and Dunn,T.M.
  TITLE     Identification of small subunits of mammalian serine
            palmitoyltransferase that confer distinct acyl-CoA substrate
            specificities
  JOURNAL   Proc Natl Acad Sci U S A 106 (20), 8186-8191 (2009)
   PUBMED   19416851
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2009 Jun 16;106(24):9931]
REFERENCE   8  (residues 1 to 552)
  AUTHORS   Hornemann,T., Wei,Y. and von Eckardstein,A.
  TITLE     Is the mammalian serine palmitoyltransferase a high-molecular-mass
            complex?
  JOURNAL   Biochem J 405 (1), 157-164 (2007)
   PUBMED   17331073
  REMARK    GeneRIF: Results suggest that functional serine
            palmitoyltransferase is not a dimer, but a higher organized
            complex, composed of three distinct subunits (SPTLC1, SPTLC2 and
            SPTLC3) with a molecular mass of 480 kDa.
REFERENCE   9  (residues 1 to 552)
  AUTHORS   Hornemann,T., Richard,S., Rutti,M.F., Wei,Y. and von Eckardstein,A.
  TITLE     Cloning and initial characterization of a new subunit for mammalian
            serine-palmitoyltransferase
  JOURNAL   J Biol Chem 281 (49), 37275-37281 (2006)
   PUBMED   17023427
  REMARK    GeneRIF: cloning and expression in tissues and cell lines
REFERENCE   10 (residues 1 to 552)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL133331.27, AL445589.6,
            AL109983.2 and AL050320.19.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 8, 2006 this sequence version replaced NP_060797.1.
            
            Summary: This gene encodes a subunit of the serine
            palmitoyltransferase complex which catalyzes the rate-limiting step
            in sphingolipid biosynthesis. This subunit metabolizes lauroyl- and
            myristoyl-CoA and generates C14 and C16-sphingoid bases. [provided
            by RefSeq, Mar 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.20299.1,
                                           SRR1803613.142798.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000399002.7/ ENSP00000381968.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p12.1"
     Protein         1..552
                     /product="serine palmitoyltransferase 3"
                     /EC_number="2.3.1.50"
                     /note="serine palmitoyltransferase, long chain base
                     subunit 2-like (aminotransferase 2); long chain base
                     biosynthesis protein 3; serine-palmitoyl-CoA transferase
                     3; long chain base biosynthesis protein 2b"
                     /calculated_mol_wt=61919
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NUV7.3)"
     Region          57..549
                     /region_name="AAT_I"
                     /note="Aspartate aminotransferase (AAT) superfamily (fold
                     type I) of pyridoxal phosphate (PLP)-dependent enzymes.
                     PLP combines with an alpha-amino acid to form a compound
                     called a Schiff base or aldimine intermediate, which
                     depending on the reaction, is the...; cl18945"
                     /db_xref="CDD:450240"
     Site            59..79
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NUV7.3)"
     Site            order(168,229..231,255,307,311..312,336,338..339,368,371,
                     501)
                     /site_type="active"
                     /note="substrate-cofactor binding pocket [active]"
                     /db_xref="CDD:99747"
     Site            order(229..231,255,307,311,336,338..339,368,371)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99747"
     Site            371
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99747"
     CDS             1..552
                     /gene="SPTLC3"
                     /gene_synonym="C20orf38; dJ718P11; dJ718P11.1; hLCB2b; LCB
                     3; LCB2B; LCB3; SPT 3; SPT3; SPTLC2L"
                     /coded_by="NM_018327.4:297..1955"
                     /db_xref="CCDS:CCDS13115.2"
                     /db_xref="GeneID:55304"
                     /db_xref="HGNC:HGNC:16253"
                     /db_xref="MIM:611120"
ORIGIN      
        1 manpgggavc ngklhnhkkq sngsqsrnct kngivkeaqq ngkphfydkl ivesfeeapl
       61 hvmvftymgy gigtlfgylr dflrnwgiek cnaaverkeq kdfvplyqdf enfytrnlym
      121 rirdnwnrpi csapgplfdl mervsddynw tfrftgrvik dvinmgsynf lglaakydes
      181 mrtikdvlev ygtgvastrh emgtldkhke ledlvakfln veaamvfgmg fatnsmnipa
      241 lvgkgclils delnhtslvl garlsgatir ifkhnntqsl ekllrdaviy gqprtrrawk
      301 kililvegvy smegsivhlp qiialkkkyk aylyideahs igavgptgrg vteffgldph
      361 evdvlmgtft ksfgasggyi agrkdlvdyl rvhshsavya ssmsppiaeq iirslklimg
      421 ldgttqglqr vqqlakntry frqrlqemgf iiygnenasv vplllympgk vaafarhmle
      481 kkigvvvvgf patplaeara rfcvsaahtr emldtvleal demgdllqlk ysrhkksarp
      541 elydetsfel ed
//
