LOCUS       NM_005383               1143 bp    mRNA    linear   PRI 03-APR-2024
DEFINITION  Homo sapiens neuraminidase 2 (NEU2), mRNA.
ACCESSION   NM_005383
VERSION     NM_005383.2
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 1143)
  AUTHORS   Nath,S., Mondal,S., Butti,R., Prasanna Gunasekaran,V.,
            Chatterjee,U., Halder,A., Kundu,G.C. and Mandal,C.
  TITLE     Desialylation of Sonic-Hedgehog by Neu2 Inhibits Its Association
            with Patched1 Reducing Stemness-Like Properties in Pancreatic
            Cancer Sphere-forming Cells
  JOURNAL   Cells 9 (6), 1512 (2020)
   PUBMED   32575925
  REMARK    GeneRIF: Desialylation of Sonic-Hedgehog by Neu2 Inhibits Its
            Association with Patched1 Reducing Stemness-Like Properties in
            Pancreatic Cancer Sphere-forming Cells.
            Publication Status: Online-Only
REFERENCE   2  (bases 1 to 1143)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (bases 1 to 1143)
  AUTHORS   van der Wal,D.E., Davis,A.M., Mach,M. and Marks,D.C.
  TITLE     The role of neuraminidase 1 and 2 in glycoprotein Ibalpha-mediated
            integrin alphaIIbbeta3 activation
  JOURNAL   Haematologica 105 (4), 1081-1094 (2020)
   PUBMED   31273092
  REMARK    GeneRIF: The role of neuraminidase 1 and 2 in glycoprotein
            Ibalpha-mediated integrin alphaIIbbeta3 activation.
REFERENCE   4  (bases 1 to 1143)
  AUTHORS   Rondelli,V., Brocca,P., Fragneto,G., Daillant,J., Tringali,C.,
            Cantu',L. and Del Favero,E.
  TITLE     Membrane restructuring following in situ sialidase digestion of
            gangliosides: Complex model bilayers by synchrotron radiation
            reflectivity
  JOURNAL   Biochim Biophys Acta Biomembr 1859 (5), 845-851 (2017)
   PUBMED   28087363
  REMARK    GeneRIF: Synchrotron radiation reflectometry was used to access the
            transverse structure of model membranes under the action of the
            human sialidase NEU2, down to the Angstrom length scale
REFERENCE   5  (bases 1 to 1143)
  AUTHORS   Wang,L., Seino,J., Tomotake,H., Funakoshi,Y., Hirayama,H. and
            Suzuki,T.
  TITLE     Co-Expression of NEU2 and GBA3 Causes a Drastic Reduction in
            Cytosolic Sialyl Free N-glycans in Human MKN45 Stomach Cancer
            Cells-Evidence for the Physical Interaction of NEU2 and GBA3
  JOURNAL   Biomolecules 5 (3), 1499-1514 (2015)
   PUBMED   26193330
  REMARK    GeneRIF: cytosolic GBA3 is likely involved in the catabolism of
            cytosolic sialyl free N-glycans, possibly by stabilizing the
            activity of the NEU2 protein
            Publication Status: Online-Only
REFERENCE   6  (bases 1 to 1143)
  AUTHORS   Seyrantepe,V., Landry,K., Trudel,S., Hassan,J.A., Morales,C.R. and
            Pshezhetsky,A.V.
  TITLE     Neu4, a novel human lysosomal lumen sialidase, confers normal
            phenotype to sialidosis and galactosialidosis cells
  JOURNAL   J Biol Chem 279 (35), 37021-37029 (2004)
   PUBMED   15213228
REFERENCE   7  (bases 1 to 1143)
  AUTHORS   Tringali,C., Papini,N., Fusi,P., Croci,G., Borsani,G., Preti,A.,
            Tortora,P., Tettamanti,G., Venerando,B. and Monti,E.
  TITLE     Properties of recombinant human cytosolic sialidase HsNEU2. The
            enzyme hydrolyzes monomerically dispersed GM1 ganglioside molecules
  JOURNAL   J Biol Chem 279 (5), 3169-3179 (2004)
   PUBMED   14613940
  REMARK    GeneRIF: HsNEU2 differentially recognizes the type of sialosyl
            linkage, the aglycone part of the substrate, and the supramolecular
            organization (monomer/micelle/vesicle) of gangliosides
REFERENCE   8  (bases 1 to 1143)
  AUTHORS   Monti,E., Preti,A., Nesti,C., Ballabio,A. and Borsani,G.
  TITLE     Expression of a novel human sialidase encoded by the NEU2 gene
  JOURNAL   Glycobiology 9 (12), 1313-1321 (1999)
   PUBMED   10561456
REFERENCE   9  (bases 1 to 1143)
  AUTHORS   Monti,E., Preti,A., Rossi,E., Ballabio,A. and Borsani,G.
  TITLE     Cloning and characterization of NEU2, a human gene homologous to
            rodent soluble sialidases
  JOURNAL   Genomics 57 (1), 137-143 (1999)
   PUBMED   10191093
REFERENCE   10 (bases 1 to 1143)
  AUTHORS   Miyagi,T., Konno,K., Emori,Y., Kawasaki,H., Suzuki,K., Yasui,A. and
            Tsuik,S.
  TITLE     Molecular cloning and expression of cDNA encoding rat skeletal
            muscle cytosolic sialidase
  JOURNAL   J Biol Chem 268 (35), 26435-26440 (1993)
   PUBMED   8253770
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC069151.1.
            
            On Jan 31, 2009 this sequence version replaced NM_005383.1.
            
            Summary: This gene belongs to a family of glycohydrolytic enzymes
            which remove sialic acid residues from glycoproteins and
            glycolipids. Expression studies in COS7 cells confirmed that this
            gene encodes a functional sialidase. Its cytosolic localization was
            demonstrated by cell fractionation experiments. [provided by
            RefSeq, Jul 2008].
            
            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 :: BC069151.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2145893
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000233840.3/ ENSP00000233840.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1143
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.1"
     gene            1..1143
                     /gene="NEU2"
                     /gene_synonym="SIAL2"
                     /note="neuraminidase 2"
                     /db_xref="GeneID:4759"
                     /db_xref="HGNC:HGNC:7759"
                     /db_xref="MIM:605528"
     CDS             1..1143
                     /gene="NEU2"
                     /gene_synonym="SIAL2"
                     /EC_number="3.2.1.18"
                     /note="cytosolic sialidase; N-acetyl-alpha-neuraminidase
                     2; sialidase 2 (cytosolic sialidase)"
                     /codon_start=1
                     /product="sialidase-2"
                     /protein_id="NP_005374.2"
                     /db_xref="CCDS:CCDS2501.1"
                     /db_xref="GeneID:4759"
                     /db_xref="HGNC:HGNC:7759"
                     /db_xref="MIM:605528"
                     /translation="MASLPVLQKESVFQSGAHAYRIPALLYLPGQQSLLAFAEQRASK
                     KDEHAELIVLRRGDYDAPTHQVQWQAQEVVAQARLDGHRSMNPCPLYDAQTGTLFLFF
                     IAIPGQVTEQQQLQTRANVTRLCQVTSTDHGRTWSSPRDLTDAAIGPAYREWSTFAVG
                     PGHCLQLHDRARSLVVPAYAYRKLHPIQRPIPSAFCFLSHDHGRTWARGHFVAQDTLE
                     CQVAEVETGEQRVVTLNARSHLRARVQAQSTNDGLDFQESQLVKKLVEPPPQGCQGSV
                     ISFPSPRSGPGSPAQWLLYTHPTHSWQRADLGAYLNPRPPAPEAWSEPVLLAKGSCAY
                     SDLQSMGTGPDGSPLFGCLYEANDYEEIVFLMFTLKQAFPAEYLPQ"
     exon            1..201
                     /gene="NEU2"
                     /gene_synonym="SIAL2"
                     /inference="alignment:Splign:2.1.0"
     exon            202..1143
                     /gene="NEU2"
                     /gene_synonym="SIAL2"
                     /inference="alignment:Splign:2.1.0"
ORIGIN      
        1 atggcgtccc ttcctgtcct gcagaaggag agcgtgttcc agtcgggagc ccatgcctac
       61 agaatccctg ccctgctcta cctgcctggg cagcagtccc tgctggcctt cgcggaacag
      121 cgggcaagca agaaggatga gcacgcagag ctgattgtcc tgcgcagagg agactacgac
      181 gcacccaccc accaggttca gtggcaagct caggaggtgg tggcccaggc ccggctggat
      241 ggccaccggt ccatgaaccc atgccccttg tatgacgcgc agacggggac cctcttcctc
      301 ttcttcattg ccatccctgg gcaagtcacg gagcaacagc agctgcagac cagggccaat
      361 gtgacgcggc tgtgccaagt caccagcact gaccacggga ggacctggag ctcccccaga
      421 gacctcactg atgcggccat cggcccagcc taccgggagt ggtccacctt tgcagtgggc
      481 ccggggcatt gtttgcagct tcacgacagg gcccggagcc tggtggtgcc cgcctacgcc
      541 taccggaaac ttcaccccat ccaaaggccg atcccctctg ccttctgctt cctcagccat
      601 gaccatgggc gcacgtgggc gcgagggcac tttgtggccc aggacaccct ggagtgccag
      661 gtggccgaag tcgagactgg ggagcagagg gtggtgaccc tcaacgcgag aagccacctc
      721 cgagccaggg tccaggccca gagcaccaat gacgggcttg atttccagga gtctcagctg
      781 gtgaagaagc tggtggagcc gccgccccag ggctgccagg ggagcgtcat cagcttcccc
      841 agcccccgct cggggcctgg ctccccagcc cagtggctgc tctacactca ccccacacac
      901 tcctggcaga gggccgacct gggtgcctac ctcaacccgc gacctccagc ccctgaggcc
      961 tggtcagagc cggtactgct ggccaagggc agctgtgcct actcagacct ccagagcatg
     1021 ggcaccggcc ctgatgggtc ccccttgttt gggtgtctgt acgaagccaa tgattacgag
     1081 gagattgtct ttctcatgtt caccctgaag caagccttcc cagctgagta cctgcctcag
     1141 tga
//
