ID ENOG_RAT Reviewed; 434 AA. AC P07323; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 04-NOV-2008, entry version 91. DE RecName: Full=Gamma-enolase; DE EC=4.2.1.11; DE AltName: Full=2-phospho-D-glycerate hydro-lyase; DE AltName: Full=Neural enolase; DE AltName: Full=Neuron-specific enolase; DE Short=NSE; DE AltName: Full=Enolase 2; GN Name=Eno2; Synonyms=Eno-2; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=86042683; PubMed=2865729; RA Sakimura K., Kushiya E., Obinata M., Odani S., Takahashi Y.; RT "Molecular cloning and the nucleotide sequence of cDNA for neuron- RT specific enolase messenger RNA of rat brain."; RL Proc. Natl. Acad. Sci. U.S.A. 82:7453-7457(1985). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Sprague-Dawley; TISSUE=Brain; RX MEDLINE=86308095; PubMed=3746946; RA Forss-Petter S., Danielson P., Sutcliffe J.G.; RT "Neuron-specific enolase: complete structure of rat mRNA, multiple RT transcriptional start sites, and evidence suggesting post- RT transcriptional control."; RL J. Neurosci. Res. 16:141-156(1986). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pituitary; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28. RX MEDLINE=88152493; PubMed=2450052; DOI=10.1016/0378-1119(87)90218-6; RA Sakimura K., Kushiya E., Takahashi Y., Suzuki Y.; RT "The structure and expression of neuron-specific enolase gene."; RL Gene 60:103-113(1987). RN [5] RP PROTEIN SEQUENCE OF 10-28; 32-50; 65-89; 106-120; 163-179; 184-193; RP 240-262; 270-285; 307-326; 336-394 AND 407-422, AND MASS SPECTROMETRY. RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord; RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.; RL Submitted (JUL-2007) to UniProtKB. RN [6] RP POSSIBLE FUNCTION AS A NEUROTROPHIC FACTOR. RX MEDLINE=95273031; PubMed=7753500; DOI=10.1016/0168-0102(94)00849-B; RA Hattori T., Takei N., Mizuno Y., Kato K., Kohsaka S.; RT "Neurotrophic and neuroprotective effects of neuron-specific enolase RT on cultured neurons from embryonic rat brain."; RL Neurosci. Res. 21:191-198(1995). RN [7] RP SUBCELLULAR LOCATION OF ALPHA/GAMMA HETERODIMER. RX PubMed=15041191; DOI=10.1016/j.neures.2003.12.006; RA Ueta H., Nagasawa H., Oyabu-Manabe Y., Toida K., Ishimura K., Hori H.; RT "Localization of enolase in synaptic plasma membrane as an alphagamma RT heterodimer in rat brain."; RL Neurosci. Res. 48:379-386(2004). CC -!- FUNCTION: Has neurotrophic and neuroprotective properties on a CC broad spectrum of central nervous system (CNS) neurons. Binds, in CC a calcium-dependent manner, to cultured neocortical neurons and CC promotes cell survival. CC -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate + CC H(2)O. CC -!- COFACTOR: Magnesium. Required for catalysis and for stabilizing CC the dimer. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 4/5. CC -!- SUBUNIT: Mammalian enolase is composed of 3 isozyme subunits, CC alpha, beta and gamma, which can form homodimers or heterodimers CC which are cell-type and development-specific. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane (By CC similarity). Note=Can translocate to the plasma membrane in either CC the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form CC (By similarity). CC -!- TISSUE SPECIFICITY: The alpha/alpha homodimer is expressed in CC embryo and in most adult tissues. The alpha/beta heterodimer and CC the beta/beta homodimer are found in striated muscle, and the CC alpha/gamma heterodimer and the gamma/gamma homodimer in neurons. CC -!- DEVELOPMENTAL STAGE: During ontogenesis, there is a transition CC from the alpha/alpha homodimer to the alpha/beta heterodimer in CC striated muscle cells, and to the alpha/gamma heterodimer in nerve CC cells. ENO2 levels in brain increase 10-30 days after birth. CC Levels continue to accumulate over the following few months CC (protein only). CC -!- SIMILARITY: Belongs to the enolase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M11931; AAA41119.1; -; mRNA. DR EMBL; M22770; AAA41725.1; -; Genomic_DNA. DR EMBL; AF019973; AAB72088.1; -; mRNA. DR EMBL; BC060310; AAH60310.1; -; mRNA. DR EMBL; X07727; CAA30556.1; -; Genomic_DNA. DR EMBL; X07728; CAA30556.1; JOINED; Genomic_DNA. DR EMBL; X07729; CAA30556.1; JOINED; Genomic_DNA. DR PIR; A24742; A24742. DR PIR; JC1039; JC1039. DR RefSeq; NP_647541.1; -. DR UniGene; Rn.10828; -. DR HSSP; P56252; 1PDZ. DR SMR; P07323; 2-434. DR PhosphoSite; P07323; -. DR Ensembl; ENSRNOG00000013141; Rattus norvegicus. DR GeneID; 24334; -. DR KEGG; rno:24334; -. DR NMPDR; fig|10116.3.peg.22203; -. DR RGD; 2554; Eno2. DR HOVERGEN; P07323; -. DR NextBio; 603019; -. DR ArrayExpress; P07323; -. DR GermOnline; ENSRNOG00000013141; Rattus norvegicus. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. DR InterPro; IPR000941; Enolase. DR PANTHER; PTHR11902; Enolase; 1. DR Pfam; PF00113; Enolase_C; 1. DR Pfam; PF03952; Enolase_N; 1. DR PIRSF; PIRSF001400; Enolase; 1. DR PRINTS; PR00148; ENOLASE. DR ProDom; PD000902; Enolase; 1. DR TIGRFAMs; TIGR01060; eno; 1. DR PROSITE; PS00164; ENOLASE; 1. PE 1: Evidence at protein level; KW Cell membrane; Cytoplasm; Direct protein sequencing; Glycolysis; KW Lyase; Magnesium; Membrane; Metal-binding; Phosphoprotein. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 434 Gamma-enolase. FT /FTId=PRO_0000134114. FT REGION 370 373 Substrate binding (By similarity). FT ACT_SITE 210 210 Proton donor (By similarity). FT ACT_SITE 343 343 Proton acceptor (By similarity). FT METAL 245 245 Magnesium (By similarity). FT METAL 293 293 Magnesium (By similarity). FT METAL 318 318 Magnesium (By similarity). FT BINDING 158 158 Substrate (By similarity). FT BINDING 167 167 Substrate (By similarity). FT BINDING 293 293 Substrate (By similarity). FT BINDING 318 318 Substrate (By similarity). FT BINDING 394 394 Substrate (By similarity). FT MOD_RES 44 44 Phosphotyrosine (By similarity). FT MOD_RES 80 80 Phosphoserine (By similarity). SQ SEQUENCE 434 AA; 47141 MW; BAFFCE2F04BCCA45 CRC64; MSIQKIWARE ILDSRGNPTV EVDLHTAKGL FRAAVPSGAS TGIYEALELR DGDKQRYLGK GVLKAVDHIN STIAPALISS GLSVVEQEKL DNLMLELDGT ENKSKFGANA ILGVSLAVCK AGAAEKDLPL YRHIAQLAGN SDLILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAESFRD AMRLGAEVYH TLKGVIKDKY GKDATNVGDE GGFAPNILEN SEALELVKEA IDKAGYTEKM VIGMDVAASE FYRDGKYDLD FKSPADPSRC ITGDQLGALY QDFVRNYPVV SIEDPFDQDD WAAWSKFTAN VGIQIVGDDL TVTNPKRIER AVEEKACNCL LLKVNQIGSV TEAIQACKLA QENGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEELGEE ARFAGHNFRN PSVL //