LOCUS       NP_075608                434 aa            linear   ROD 15-OCT-2024
DEFINITION  alpha-enolase isoform 2 [Mus musculus].
ACCESSION   NP_075608 XP_001006583
VERSION     NP_075608.2
DBSOURCE    REFSEQ: accession NM_023119.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Grammer,C., Komorowska,J.A. and Swann,J.B.
  TITLE     Vhl safeguards thymic epithelial cell identity and thymopoietic
            capacity by constraining Hif1a activity during development
  JOURNAL   iScience 27 (7), 110258 (2024)
   PUBMED   39040069
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Ayyangar,U., Karkhanis,A., Tay,H., Afandi,A.F.B., Bhattacharjee,O.,
            Ks,L., Lee,S.H., Chan,J. and Raghavan,S.
  TITLE     Metabolic rewiring of macrophages by epidermal-derived lactate
            promotes sterile inflammation in the murine skin
  JOURNAL   EMBO J 43 (7), 1113-1134 (2024)
   PUBMED   38418556
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Chen,L.J., Li,J.Y., Nguyen,P., He,M., Chen,Z.B., Subramaniam,S.,
            Shyy,J.Y. and Chien,S.
  TITLE     Single-cell RNA sequencing unveils unique transcriptomic signatures
            of endothelial cells and role of ENO1 in response to disturbed flow
  JOURNAL   Proc Natl Acad Sci U S A 121 (5), e2318904121 (2024)
   PUBMED   38261622
  REMARK    GeneRIF: Single-cell RNA sequencing unveils unique transcriptomic
            signatures of endothelial cells and role of ENO1 in response to
            disturbed flow.
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Chung,I.C., Huang,W.C., Huang,Y.T., Chen,M.L., Tsai,A.W., Wu,P.Y.
            and Yuan,T.T.
  TITLE     Unrevealed roles of extracellular enolase-1 (ENO1) in promoting
            glycolysis and pro-cancer activities in multiple myeloma via
            hypoxia-inducible factor 1alpha
  JOURNAL   Oncol Rep 50 (5) (2023)
   PUBMED   37800625
  REMARK    GeneRIF: Unrevealed roles of extracellular enolase-1 (ENO1) in
            promoting glycolysis and pro-cancer activities in multiple myeloma
            via hypoxia-inducible factor 1alpha.
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Kawakami,H., Chen,K.Q., Zhang,R., Pappas,M.P., Bailey,A.,
            Reisz,J.A., Corcoran,D., Nishinakamura,R., D'Alessandro,A. and
            Kawakami,Y.
  TITLE     Sall4 restricts glycolytic metabolism in limb buds through
            transcriptional regulation of glycolytic enzyme genes
  JOURNAL   Dev Biol 501, 28-38 (2023)
   PUBMED   37301463
REFERENCE   6  (residues 1 to 434)
  AUTHORS   Lucas,M., Goblet,C., Keller,A., Lamande,N., Gros,F., Whalen,R.G.
            and Lazar,M.
  TITLE     Modulation of embryonic and muscle-specific enolase gene products
            in the developing mouse hindlimb
  JOURNAL   Differentiation 51 (1), 1-7 (1992)
   PUBMED   1280607
REFERENCE   7  (residues 1 to 434)
  AUTHORS   Keller,A., Ott,M.O., Lamande,N., Lucas,M., Gros,F., Buckingham,M.
            and Lazar,M.
  TITLE     Activation of the gene encoding the glycolytic enzyme beta-enolase
            during early myogenesis precedes an increased expression during
            fetal muscle development
  JOURNAL   Mech Dev 38 (1), 41-54 (1992)
   PUBMED   1525038
REFERENCE   8  (residues 1 to 434)
  AUTHORS   Lalley,P.A., Minna,J.D. and Francke,U.
  TITLE     Conservation of autosomal gene synteny groups in mouse and man
  JOURNAL   Nature 274 (5667), 160-163 (1978)
   PUBMED   662012
REFERENCE   9  (residues 1 to 434)
  AUTHORS   Lalley,P.A., Francke,U. and Minna,J.D.
  TITLE     Homologous genes for enolase, phosphogluconate dehydrogenase,
            phosphoglucomutase, and adenylate kinase are syntenic on mouse
            chromosome 4 and human chromosome 1p
  JOURNAL   Proc Natl Acad Sci U S A 75 (5), 2382-2386 (1978)
   PUBMED   209463
REFERENCE   10 (residues 1 to 434)
  AUTHORS   D'Ancona,G.G. and Croce,C.M.
  TITLE     Assignment of the gene for enolase to mouse chromosome 4 using
            somatic cell hybrids
  JOURNAL   Cytogenet Cell Genet 19 (1), 1-6 (1977)
   PUBMED   891258
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL606903.8.
            
            On Oct 30, 2007 this sequence version replaced NP_075608.1.
            
            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 :: BC083334.1, AK150192.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 81.24 cM"
     Protein         1..434
                     /product="alpha-enolase isoform 2"
                     /EC_number="4.2.1.11"
                     /note="non-neural enolase; 2-phospho-D-glycerate
                     hydro-lyase; alpha-enolase; 2-phospho-D-glycerate
                     hydrolase; c-Myc promoter binding protein"
                     /calculated_mol_wt=47010
     Region          2..432
                     /region_name="PLN00191"
                     /note="enolase"
                     /db_xref="CDD:215095"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P06733; propagated from
                     UniProtKB/Swiss-Prot (P17182.3)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18034455; propagated from
                     UniProtKB/Swiss-Prot (P17182.3)"
     Site            60
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P17182.3)"
     Site            71
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P06733; propagated from
                     UniProtKB/Swiss-Prot (P17182.3)"
     Site            89
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P17182.3)"
     Site            92
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P17182.3)"
     Site            126
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P17182.3)"
     Site            193
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P17182.3)"
     Site            199
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P06733; propagated from
                     UniProtKB/Swiss-Prot (P17182.3)"
     Site            202
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P17182.3)"
     Site            228
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P17182.3)"
     Site            233
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P06733; propagated from
                     UniProtKB/Swiss-Prot (P17182.3)"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P06733; propagated from
                     UniProtKB/Swiss-Prot (P17182.3)"
     Site            256
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P17182.3)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P17182.3)"
     Site            281
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P06733; propagated from
                     UniProtKB/Swiss-Prot (P17182.3)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P06733; propagated from
                     UniProtKB/Swiss-Prot (P17182.3)"
     Site            291
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P06733; propagated from
                     UniProtKB/Swiss-Prot (P17182.3)"
     Site            335
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P17182.3)"
     Site            343
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P17182.3)"
     Region          405..434
                     /region_name="Required for interaction with PLG.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P17182.3)"
     Site            406
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P17182.3)"
     Site            420
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P06733; propagated from
                     UniProtKB/Swiss-Prot (P17182.3)"
     CDS             1..434
                     /gene="Eno1"
                     /gene_synonym="Eno-1; MBP-1; NNE"
                     /coded_by="NM_023119.3:44..1348"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS18971.1"
                     /db_xref="GeneID:13806"
                     /db_xref="MGI:MGI:95393"
ORIGIN      
        1 msilrihare ifdsrgnptv evdlytakgl fraavpsgas tgiyealelr dndktrfmgk
       61 gvsqavehin ktiapalvsk kvnvveqeki dklmiemdgt enkskfgana ilgvslavck
      121 agavekgvpl yrhiadlagn pevilpvpaf nvinggshag nklamqefmi lpvgassfre
      181 amrigaevyh nlknvikeky gkdatnvgde ggfapnilen kealellkta iakagytdqv
      241 vigmdvaase fyrsgkydld fkspddpsry itpdqladly ksfvqnypvv siedpfdqdd
      301 wgawqkftas agiqvvgddl tvtnpkriak aasekscncl llkvnqigsv teslqackla
      361 qsngwgvmvs hrsgetedtf iadlvvglct gqiktgapcr serlakynqi lrieeelgsk
      421 akfagrsfrn plak
//
