LOCUS       NP_033441                249 aa            linear   ROD 11-OCT-2024
DEFINITION  triosephosphate isomerase [Mus musculus].
ACCESSION   NP_033441
VERSION     NP_033441.3
DBSOURCE    REFSEQ: accession NM_009415.3
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 249)
  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   2  (residues 1 to 249)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 249)
  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   4  (residues 1 to 249)
  AUTHORS   Gehlen-Breitbach,S., Schmid,T., Frob,F., Rodrian,G., Weider,M.,
            Wegner,M. and Golz,L.
  TITLE     The Tip60/Ep400 chromatin remodeling complex impacts basic cellular
            functions in cranial neural crest-derived tissue during early
            orofacial development
  JOURNAL   Int J Oral Sci 15 (1), 16 (2023)
   PUBMED   37024457
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 249)
  AUTHORS   Stein,B.D., Ferrarone,J.R., Gardner,E.E., Chang,J.W., Wu,D.,
            Hollstein,P.E., Liang,R.J., Yuan,M., Chen,Q., Coukos,J.S.,
            Sindelar,M., Ngo,B., Gross,S.S., Shaw,R.J., Zhang,C., Asara,J.M.,
            Moellering,R.E., Varmus,H. and Cantley,L.C.
  TITLE     LKB1-Dependent Regulation of TPI1 Creates a Divergent Metabolic
            Liability between Human and Mouse Lung Adenocarcinoma
  JOURNAL   Cancer Discov 13 (4), 1002-1025 (2023)
   PUBMED   36715544
  REMARK    GeneRIF: LKB1-Dependent Regulation of TPI1 Creates a Divergent
            Metabolic Liability between Human and Mouse Lung Adenocarcinoma.
REFERENCE   6  (residues 1 to 249)
  AUTHORS   Siracusa,L.D., Jenkins,N.A. and Copeland,N.G.
  TITLE     Identification and applications of repetitive probes for gene
            mapping in the mouse
  JOURNAL   Genetics 127 (1), 169-179 (1991)
   PUBMED   1673105
REFERENCE   7  (residues 1 to 249)
  AUTHORS   Minna,J.D., Bruns,G.A., Krinsky,A.H., Lalley,P.A., Francke,U. and
            Gerald,P.S.
  TITLE     Assignment of a Mus musculus gene for triosephosphate isomerase to
            chromosome 6 and for glyoxalase-I to chromosome 17 using somatic
            cell hybrids
  JOURNAL   Somatic Cell Genet 4 (2), 241-252 (1978)
   PUBMED   566476
REFERENCE   8  (residues 1 to 249)
  AUTHORS   Leinwand,L.A., Kozak,C.A. and Ruddle,F.H.
  TITLE     Assignment of the genes for triose phosphate isomerase to
            chromosome 6 and tripeptidase-1 to chromosome 10 in Mus musculus by
            somatic cell hybridization
  JOURNAL   Somatic Cell Genet 4 (2), 233-240 (1978)
   PUBMED   566475
REFERENCE   9  (residues 1 to 249)
  AUTHORS   Kozak,C.A. and Ruddle,F.H.
  TITLE     Assignment of the genes for thymidine kinase and galactokinase to
            Mus musculus chromosome 11 and the preferential segregation of this
            chromosome in Chinese hamster/mouse somatic cell hybrids
  JOURNAL   Somatic Cell Genet 3 (2), 121-133 (1977)
   PUBMED   204065
REFERENCE   10 (residues 1 to 249)
  AUTHORS   Bruns,G.A. and Gerald,P.S.
  TITLE     Human glyceraldehyde-3-phosphate dehydrogenase in man-rodent
            somatic cell hybrids
  JOURNAL   Science 192 (4234), 54-56 (1976)
   PUBMED   176725
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BU945752.1, BC046761.1, AK008034.1, AK010808.1 and CD766215.1.
            
            On Jul 23, 2019 this sequence version replaced NP_033441.2.
            
            CCDS Note: The coding region has been updated to extend the
            N-terminus to one that is more supported by the available
            transcript data. The 5'-most translation start codon, which appears
            to be mouse-specific, is used in the updated sequence. An
            alternative downstream start codon, which is well-conserved, is
            also present, and it would result in a protein that is 13 aa
            shorter at the N-terminus. The 5'-most start codon has a weak Kozak
            signal, so it is possible that ribosomal leaky scanning may
            sometimes allow the downstream start codon to be used. There is no
            experimental evidence indicating which start codon is
            preferentially used in vivo.
            
            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 :: SRR7345562.1181931.1,
                                           SRR7652917.1215528.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849380, SAMN00849381
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
                     /chromosome="6"
                     /map="6 59.17 cM"
     Protein         1..249
                     /product="triosephosphate isomerase"
                     /EC_number="5.3.1.1"
                     /EC_number="4.2.3.3"
                     /note="triose-phosphate isomerase; methylglyoxal synthase"
                     /calculated_mol_wt=26582
     Region          2..247
                     /region_name="PTZ00333"
                     /note="triosephosphate isomerase; Provisional"
                     /db_xref="CDD:240365"
     Site            order(12,14,96,166,172,212,231,233..234)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238190"
     Site            order(12,15,46..48,50,53,65,83,86..87,98..99)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238190"
     Site            order(14,96,166)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238190"
     Site            14
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P60174; propagated from
                     UniProtKB/Swiss-Prot (P17751.5)"
     Site            80
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P60174; propagated from
                     UniProtKB/Swiss-Prot (P17751.5)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48500; propagated from
                     UniProtKB/Swiss-Prot (P17751.5)"
     Site            156
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P17751.5)"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P17751.5)"
     Site            173
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P17751.5)"
     Site            194
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P17751.5)"
     Site            194
                     /site_type="methylation"
                     /note="N6-methyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P60174; propagated from
                     UniProtKB/Swiss-Prot (P17751.5)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P17751.5)"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P60174; propagated from
                     UniProtKB/Swiss-Prot (P17751.5)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P60174; propagated from
                     UniProtKB/Swiss-Prot (P17751.5)"
     Site            238
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P60174; propagated from
                     UniProtKB/Swiss-Prot (P17751.5)"
     CDS             1..249
                     /gene="Tpi1"
                     /gene_synonym="TIM; Tpi; Tpi-1"
                     /coded_by="NM_009415.3:37..786"
                     /db_xref="CCDS:CCDS20530.2"
                     /db_xref="GeneID:21991"
                     /db_xref="MGI:MGI:98797"
ORIGIN      
        1 maptrkffvg gnwkmngrkk clgelictln aanvpagtev vcapptayid farqkldpki
       61 avaaqncykv tngaftgeis pgmikdlgat wvvlghserr hvfgesdeli gqkvshalae
      121 glgviacige kldereagit ekvvfeqtkv iadnvkdwsk vvlayepvwa igtgktatpq
      181 qaqevheklr gwlksnvndg vaqstriiyg gsvtgatcke lasqpdvdgf lvggaslkpe
      241 fvdiinakq
//
