LOCUS       NM_018946               1179 bp    mRNA    linear   PRI 16-FEB-2025
DEFINITION  Homo sapiens N-acetylneuraminate synthase (NANS), mRNA.
ACCESSION   NM_018946
VERSION     NM_018946.4
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  (bases 1 to 1179)
  AUTHORS   Bu,Q., Dai,Y., Zhang,H., Li,M., Liu,H., Huang,Y., Zeng,A., Qin,F.,
            Jiang,L., Wang,L., Chen,Y., Li,H., Wang,X., Zhao,Y., Qin,M.,
            Zhao,Y., Zhang,N., Kuang,W., Zhao,Y. and Cen,X.
  TITLE     Neurodevelopmental defects in human cortical organoids with
            N-acetylneuraminic acid synthase mutation
  JOURNAL   Sci Adv 9 (47), eadf2772 (2023)
   PUBMED   38000033
  REMARK    GeneRIF: Neurodevelopmental defects in human cortical organoids
            with N-acetylneuraminic acid synthase mutation.
REFERENCE   2  (bases 1 to 1179)
  AUTHORS   Willems,A.P., Sun,L., Schulz,M.A., Tian,W., Ashikov,A., van
            Scherpenzeel,M., Hermans,E., Clausen,H., Yang,Z. and Lefeber,D.J.
  TITLE     Activity of N-acylneuraminate-9-phosphatase (NANP) is not essential
            for de novo sialic acid biosynthesis
  JOURNAL   Biochim Biophys Acta Gen Subj 1863 (10), 1471-1479 (2019)
   PUBMED   31121216
REFERENCE   3  (bases 1 to 1179)
  AUTHORS   van Karnebeek,C.D., Bonafe,L., Wen,X.Y., Tarailo-Graovac,M.,
            Balzano,S., Royer-Bertrand,B., Ashikov,A., Garavelli,L., Mammi,I.,
            Turolla,L., Breen,C., Donnai,D., Cormier-Daire,V., Heron,D.,
            Nishimura,G., Uchikawa,S., Campos-Xavier,B., Rossi,A., Hennet,T.,
            Brand-Arzamendi,K., Rozmus,J., Harshman,K., Stevenson,B.J.,
            Girardi,E., Superti-Furga,G., Dewan,T., Collingridge,A.,
            Halparin,J., Ross,C.J., Van Allen,M.I., Rossi,A., Engelke,U.F.,
            Kluijtmans,L.A., van der Heeft,E., Renkema,H., de Brouwer,A.,
            Huijben,K., Zijlstra,F., Heise,T., Boltje,T., Wasserman,W.W.,
            Rivolta,C., Unger,S., Lefeber,D.J., Wevers,R.A. and
            Superti-Furga,A.
  TITLE     NANS-mediated synthesis of sialic acid is required for brain and
            skeletal development
  JOURNAL   Nat Genet 48 (7), 777-784 (2016)
   PUBMED   27213289
  REMARK    GeneRIF: NANS deficiency is associated with defect in brain and
            skeletal development.
            Erratum:[Nat Genet. 2017 May 26;49(6):969. doi:
            10.1038/ng0617-969a.. PMID: 28546570]
REFERENCE   4  (bases 1 to 1179)
  AUTHORS   Flachsbart,F., Franke,A., Kleindorp,R., Caliebe,A., Blanche,H.,
            Schreiber,S. and Nebel,A.
  TITLE     Investigation of genetic susceptibility factors for human longevity
            - a targeted nonsynonymous SNP study
  JOURNAL   Mutat Res 694 (1-2), 13-19 (2010)
   PUBMED   20800603
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (bases 1 to 1179)
  AUTHORS   Hamada,T., Ito,Y., Abe,T., Hayashi,F., Guntert,P., Inoue,M.,
            Kigawa,T., Terada,T., Shirouzu,M., Yoshida,M., Tanaka,A.,
            Sugano,S., Yokoyama,S. and Hirota,H.
  TITLE     Solution structure of the antifreeze-like domain of human sialic
            acid synthase
  JOURNAL   Protein Sci 15 (5), 1010-1016 (2006)
   PUBMED   16597820
  REMARK    GeneRIF: The structure of the C-terminal antifreeze-like domain of
            human sialic acid synthase was determined. The structure comprises
            one alpha- and two single-turn 3(10)-helices and two beta-strands,
            and is similar to those of the type III antifreeze proteins.
REFERENCE   6  (bases 1 to 1179)
  AUTHORS   Hao,J., Balagurumoorthy,P., Sarilla,S. and Sundaramoorthy,M.
  TITLE     Cloning, expression, and characterization of sialic acid synthases
  JOURNAL   Biochem Biophys Res Commun 338 (3), 1507-1514 (2005)
   PUBMED   16274664
  REMARK    GeneRIF: sialic acid synthases kinetics and preliminary mutagenesis
            experiments reveal the importance of C-terminal antifreeze protein
            domain
REFERENCE   7  (bases 1 to 1179)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   8  (bases 1 to 1179)
  AUTHORS   Nakata,D., Close,B.E., Colley,K.J., Matsuda,T. and Kitajima,K.
  TITLE     Molecular cloning and expression of the mouse N-acetylneuraminic
            acid 9-phosphate synthase which does not have deaminoneuraminic
            acid (KDN) 9-phosphate synthase activity
  JOURNAL   Biochem Biophys Res Commun 273 (2), 642-648 (2000)
   PUBMED   10873658
REFERENCE   9  (bases 1 to 1179)
  AUTHORS   Lawrence,S.M., Huddleston,K.A., Pitts,L.R., Nguyen,N., Lee,Y.C.,
            Vann,W.F., Coleman,T.A. and Betenbaugh,M.J.
  TITLE     Cloning and expression of the human N-acetylneuraminic acid
            phosphate synthase gene with 2-keto-3-deoxy-D-glycero-
            D-galacto-nononic acid biosynthetic ability
  JOURNAL   J Biol Chem 275 (23), 17869-17877 (2000)
   PUBMED   10749855
REFERENCE   10 (bases 1 to 1179)
  AUTHORS   Lolas,F.
  TITLE     Event-related slow brain potentials, cognitive processes, and
            alexithymia
  JOURNAL   Psychother Psychosom 30 (2), 116-129 (1978)
   PUBMED   693772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK316608.1 and BQ446501.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 22, 2018 this sequence version replaced NM_018946.3.
            
            Summary: This gene encodes an enzyme that functions in the
            biosynthetic pathways of sialic acids. In vitro, the encoded
            protein uses N-acetylmannosamine 6-phosphate and mannose
            6-phosphate as substrates to generate phosphorylated forms of
            N-acetylneuraminic acid (Neu5Ac) and
            2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN),
            respectively; however, it exhibits much higher activity toward the
            Neu5Ac phosphate product. In insect cells, expression of this gene
            results in Neu5Ac and KDN production. This gene is related to the
            E. coli sialic acid synthase gene neuB, and it can partially
            restore sialic acid synthase activity in an E. coli neuB-negative
            mutant. [provided by RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.231306.1, BC000008.2
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000210444.6/ ENSP00000210444.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
            COMPLETENESS: full length.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-1157              AK316608.1         16-1172
            1158-1179           BQ446501.1         24-45               c
FEATURES             Location/Qualifiers
     source          1..1179
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.33"
     gene            1..1179
                     /gene="NANS"
                     /gene_synonym="HEL-S-100; SAS; SEMDCG; SEMDG"
                     /note="N-acetylneuraminate synthase"
                     /db_xref="GeneID:54187"
                     /db_xref="HGNC:HGNC:19237"
                     /db_xref="MIM:605202"
     exon            1..209
                     /gene="NANS"
                     /gene_synonym="HEL-S-100; SAS; SEMDCG; SEMDG"
                     /inference="alignment:Splign:2.1.0"
     CDS             78..1157
                     /gene="NANS"
                     /gene_synonym="HEL-S-100; SAS; SEMDCG; SEMDG"
                     /EC_number="2.5.1.57"
                     /EC_number="2.5.1.132"
                     /note="sialic acid synthase; sialic acid phosphate
                     synthase; N-acetylneuraminic acid phosphate synthase;
                     epididymis secretory protein Li 100; N-acetylneuraminic
                     acid synthase; 3-deoxy-D-glycero-D-galacto-nononate
                     9-phosphate synthase"
                     /codon_start=1
                     /product="N-acetylneuraminate-9-phosphate synthase"
                     /protein_id="NP_061819.2"
                     /db_xref="CCDS:CCDS6733.1"
                     /db_xref="GeneID:54187"
                     /db_xref="HGNC:HGNC:19237"
                     /db_xref="MIM:605202"
                     /translation="MPLELELCPGRWVGGQHPCFIIAEIGQNHQGDLDVAKRMIRMAK
                     ECGADCAKFQKSELEFKFNRKALERPYTSKHSWGKTYGEHKRHLEFSHDQYRELQRYA
                     EEVGIFFTASGMDEMAVEFLHELNVPFFKVGSGDTNNFPYLEKTAKKGRPMVISSGMQ
                     SMDTMKQVYQIVKPLNPNFCFLQCTSAYPLQPEDVNLRVISEYQKLFPDIPIGYSGHE
                     TGIAISVAAVALGAKVLERHITLDKTWKGSDHSASLEPGELAELVRSVRLVERALGSP
                     TKQLLPCEMACNEKLGKSVVAKVKIPEGTILTMDMLTVKVGEPKGYPPEDIFNLVGKK
                     VLVTVEEDDTIMEELVDNHGKKIKS"
     exon            210..425
                     /gene="NANS"
                     /gene_synonym="HEL-S-100; SAS; SEMDCG; SEMDG"
                     /inference="alignment:Splign:2.1.0"
     exon            426..525
                     /gene="NANS"
                     /gene_synonym="HEL-S-100; SAS; SEMDCG; SEMDG"
                     /inference="alignment:Splign:2.1.0"
     exon            526..680
                     /gene="NANS"
                     /gene_synonym="HEL-S-100; SAS; SEMDCG; SEMDG"
                     /inference="alignment:Splign:2.1.0"
     exon            681..947
                     /gene="NANS"
                     /gene_synonym="HEL-S-100; SAS; SEMDCG; SEMDG"
                     /inference="alignment:Splign:2.1.0"
     exon            948..1179
                     /gene="NANS"
                     /gene_synonym="HEL-S-100; SAS; SEMDCG; SEMDG"
                     /inference="alignment:Splign:2.1.0"
     regulatory      1159..1164
                     /regulatory_class="polyA_signal_sequence"
                     /gene="NANS"
                     /gene_synonym="HEL-S-100; SAS; SEMDCG; SEMDG"
                     /note="hexamer: AATAAA"
     polyA_site      1179
                     /gene="NANS"
                     /gene_synonym="HEL-S-100; SAS; SEMDCG; SEMDG"
                     /note="major polyA site"
ORIGIN      
        1 acagaacaga gtagaggcgg cggcggcggc ggccggaccc agactggtag tgaggctttg
       61 gaccccgagc cgctgcaatg ccgctggagc tggagctgtg tcccgggcgc tgggtgggcg
      121 ggcaacaccc gtgcttcatc attgccgaga tcggccagaa ccaccagggc gacctggacg
      181 tagccaagcg catgatccgc atggccaagg agtgtggggc tgattgtgct aagttccaga
      241 agagtgagct agaattcaag tttaatcgga aagccttgga gaggccatac acctcgaagc
      301 attcctgggg gaagacgtac ggggagcaca aacgacatct ggagttcagc catgaccagt
      361 acagggagct gcagaggtac gccgaggagg ttgggatctt cttcactgcc tctggcatgg
      421 atgagatggc agttgaattc ctgcatgaac tgaatgttcc atttttcaaa gttggatctg
      481 gagacactaa taattttcct tatctggaaa agacagccaa aaaaggtcgc ccaatggtga
      541 tctccagtgg gatgcagtca atggacacca tgaagcaagt ttatcagatc gtgaagcccc
      601 tcaaccccaa cttctgcttc ttgcagtgta ccagcgcata cccgctccag cctgaggacg
      661 tcaacctgcg ggtcatctcg gaatatcaga agctctttcc tgacattccc atagggtatt
      721 ctgggcatga aacaggcata gcgatatctg tggccgcagt ggctctgggg gccaaggtgt
      781 tggaacgtca cataactttg gacaagacct ggaaggggag tgaccactcg gcctcgctgg
      841 agcctggaga actggccgag ctggtgcggt cagtgcgtct tgtggagcgt gccctgggct
      901 ccccaaccaa gcagctgctg ccctgtgaga tggcctgcaa tgagaagctg ggcaagtctg
      961 tggtggccaa agtgaaaatt ccggaaggca ccattctaac aatggacatg ctcaccgtga
     1021 aggtgggtga gcccaaaggc tatcctcctg aagacatctt taatctagtg ggcaagaagg
     1081 tcctggtcac tgttgaagag gatgacacca tcatggaaga attggtagat aatcatggca
     1141 aaaaaatcaa gtcttaaaaa taaagtgcca ttctctgaa
//
