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Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 1) (Non-neural enolase) (NNE)

 ENOA_RAT                Reviewed;         434 AA.
P04764; Q66HI3; Q6AYV3; Q6P504;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
20-JUN-2018, entry version 180.
RecName: Full=Alpha-enolase;
EC=4.2.1.11;
AltName: Full=2-phospho-D-glycerate hydro-lyase;
AltName: Full=Enolase 1;
AltName: Full=Non-neural enolase;
Short=NNE;
Name=Eno1; Synonyms=Eno-1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL
STAGE.
TISSUE=Brain, and Liver;
PubMed=2989793; DOI=10.1093/nar/13.12.4365;
Sakimura K., Kushiya E., Obinata M., Takahashi Y.;
"Molecular cloning and the nucleotide sequence of cDNA to mRNA for
non-neuronal enolase (alpha alpha enolase) of rat brain and liver.";
Nucleic Acids Res. 13:4365-4378(1985).
[2]
SEQUENCE REVISION.
Takahashi Y.;
Submitted (JAN-1986) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart, Pituitary, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 10-28; 33-50; 72-103; 106-120; 163-179; 184-193;
203-228; 234-262; 270-281; 307-326; 336-394 AND 407-420, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
[5]
PROTEIN SEQUENCE OF 46-57; 97-109; 245-262 AND 369-382, AND
INTERACTION WITH PLG.
TISSUE=Embryonic brain;
PubMed=7964722;
Nakajima K., Hamanoue M., Takemoto N., Hattori T., Kato K.,
Kohsaka S.;
"Plasminogen binds specifically to alpha-enolase on rat neuronal
plasma membrane.";
J. Neurochem. 63:2048-2057(1994).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 93-153.
TISSUE=Lymphoma;
Bole-Feysot C., Kelly P.A.;
"Rat cDNA encoding alpha enolase (2-phospho-D-glycerate hydro-lyase)
(non-neural enolase) (NNE).";
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[7]
DEVELOPMENTAL STAGE.
PubMed=8594891;
Keller A., Rouzeau J.-D., Farhadian F., Wisnewsky C., Marotte F.,
Lamande N., Samuel J.L., Schwartz K., Lazar M., Lucas M.;
"Differential expression of alpha- and beta-enolase genes during rat
heart development and hypertrophy.";
Am. J. Physiol. 269:H1843-H1851(1995).
[8]
INDUCTION.
PubMed=10662718;
Merkulova T., Keller A., Oliviero P., Marotte F., Samuel J.L.,
Rappaport L., Lamande N., Lucas M.;
"Thyroid hormones differentially modulate enolase isozymes during rat
skeletal and cardiac muscle development.";
Am. J. Physiol. 278:E330-E339(2000).
[9]
SUBCELLULAR LOCATION OF ALPHA/GAMMA HETERODIMER.
PubMed=15041191; DOI=10.1016/j.neures.2003.12.006;
Ueta H., Nagasawa H., Oyabu-Manabe Y., Toida K., Ishimura K., Hori H.;
"Localization of enolase in synaptic plasma membrane as an alphagamma
heterodimer in rat brain.";
Neurosci. Res. 48:379-386(2004).
[10]
IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
PubMed=19423663; DOI=10.1530/REP-09-0052;
Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.;
"Identification of novel immunodominant epididymal sperm proteins
using combinatorial approach.";
Reproduction 138:81-93(2009).
-!- FUNCTION: Multifunctional enzyme that, as well as its role in
glycolysis, plays a part in various processes such as growth
control, hypoxia tolerance and allergic responses. May also
function in the intravascular and pericellular fibrinolytic system
due to its ability to serve as a receptor and activator of
plasminogen on the cell surface of several cell-types such as
leukocytes and neurons. Stimulates immunoglobulin production.
-!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate +
H(2)O.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Note=Binds two Mg(2+) per subunit. Required for catalysis and for
stabilizing the dimer.;
-!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
glyceraldehyde 3-phosphate: step 4/5.
-!- SUBUNIT: Mammalian enolase is composed of 3 isozyme subunits,
alpha, beta and gamma, which can form homodimers or heterodimers
which are cell-type and development-specific (By similarity). ENO1
interacts with PLG in the neuronal plasma membrane and promotes
its activation. The C-terminal lysine is required for this binding
(PubMed:7964722). Interacts with ENO4 and PGAM2 (By similarity).
Interacts with CMTM6 (By similarity).
{ECO:0000250|UniProtKB:P06733, ECO:0000250|UniProtKB:P17182,
ECO:0000269|PubMed:7964722}.
-!- INTERACTION:
Q5VU43-11:PDE4DIP (xeno); NbExp=2; IntAct=EBI-915852, EBI-10769071;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Can
translocate to the plasma membrane in either the homodimeric
(alpha/alpha) or heterodimeric (alpha/gamma) form.
-!- TISSUE SPECIFICITY: Expressed in flagella of epididymal sperm. The
alpha/alpha homodimer is expressed in embryo and in most adult
tissues. The alpha/beta heterodimer and the beta/beta homodimer
are found in striated muscle, and the alpha/gamma heterodimer and
the gamma/gamma homodimer in neurons.
{ECO:0000269|PubMed:19423663}.
-!- DEVELOPMENTAL STAGE: During ontogenesis, there is a transition
from the alpha/alpha homodimer to the alpha/beta heterodimer in
striated muscle cells, and to the alpha/gamma heterodimer in nerve
cells. In brain, levels of ENO1 decrease around 10 dpc and then
gradually increase to adult age. In embryonic heart, ENO1 levels
decrease rapidly during cardiac development.
{ECO:0000269|PubMed:2989793, ECO:0000269|PubMed:8594891}.
-!- PTM: ISGylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH63174.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; X02610; CAA26456.1; -; mRNA.
EMBL; BC063174; AAH63174.1; ALT_INIT; mRNA.
EMBL; BC078896; AAH78896.1; -; mRNA.
EMBL; BC081847; AAH81847.2; -; mRNA.
EMBL; AF241613; AAK01319.1; -; mRNA.
PIR; A23126; A23126.
RefSeq; NP_001103378.1; NM_001109908.1.
RefSeq; NP_036686.2; NM_012554.3.
UniGene; Rn.117044; -.
UniGene; Rn.4236; -.
ProteinModelPortal; P04764; -.
SMR; P04764; -.
BioGrid; 246510; 2.
IntAct; P04764; 5.
MINT; P04764; -.
STRING; 10116.ENSRNOP00000024106; -.
MoonProt; P04764; -.
iPTMnet; P04764; -.
PhosphoSitePlus; P04764; -.
SwissPalm; P04764; -.
World-2DPAGE; 0004:P04764; -.
PaxDb; P04764; -.
PRIDE; P04764; -.
Ensembl; ENSRNOT00000024106; ENSRNOP00000024106; ENSRNOG00000017895.
Ensembl; ENSRNOT00000081579; ENSRNOP00000073191; ENSRNOG00000017895.
GeneID; 24333; -.
KEGG; rno:24333; -.
UCSC; RGD:2553; rat.
CTD; 2023; -.
RGD; 2553; Eno1.
eggNOG; KOG2670; Eukaryota.
eggNOG; COG0148; LUCA.
GeneTree; ENSGT00910000144064; -.
HOGENOM; HOG000072174; -.
HOVERGEN; HBG000067; -.
InParanoid; P04764; -.
KO; K01689; -.
OMA; EFMIIPV; -.
OrthoDB; EOG091G07NH; -.
PhylomeDB; P04764; -.
TreeFam; TF300391; -.
BRENDA; 4.2.1.11; 5301.
SABIO-RK; P04764; -.
UniPathway; UPA00109; UER00187.
PRO; PR:P04764; -.
Proteomes; UP000002494; Chromosome 5.
Bgee; ENSRNOG00000017895; -.
ExpressionAtlas; P04764; baseline and differential.
Genevisible; P04764; RN.
GO; GO:0099738; C:cell cortex region; IDA:CAFA.
GO; GO:0009986; C:cell surface; IDA:CAFA.
GO; GO:0005737; C:cytoplasm; IDA:CAFA.
GO; GO:0005829; C:cytosol; IDA:CAFA.
GO; GO:0030426; C:growth cone; IDA:CAFA.
GO; GO:0045121; C:membrane raft; IDA:CAFA.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0000015; C:phosphopyruvate hydratase complex; IDA:CAFA.
GO; GO:0005886; C:plasma membrane; IDA:CAFA.
GO; GO:0097060; C:synaptic membrane; IDA:RGD.
GO; GO:0019899; F:enzyme binding; IPI:CAFA.
GO; GO:0031072; F:heat shock protein binding; IPI:RGD.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0004634; F:phosphopyruvate hydratase activity; IDA:CAFA.
GO; GO:0046982; F:protein heterodimerization activity; IDA:CAFA.
GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
GO; GO:0061621; P:canonical glycolysis; IDA:CAFA.
GO; GO:0071456; P:cellular response to hypoxia; IDA:CAFA.
GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:CAFA.
GO; GO:0006096; P:glycolytic process; IDA:CAFA.
GO; GO:0051290; P:protein heterotetramerization; IDA:CAFA.
CDD; cd03313; enolase; 1.
Gene3D; 3.20.20.120; -; 1.
Gene3D; 3.30.390.10; -; 1.
HAMAP; MF_00318; Enolase; 1.
InterPro; IPR000941; Enolase.
InterPro; IPR036849; Enolase-like_C_sf.
InterPro; IPR029017; Enolase-like_N.
InterPro; IPR034390; Enolase-like_superfamily.
InterPro; IPR020810; Enolase_C.
InterPro; IPR020809; Enolase_CS.
InterPro; IPR020811; Enolase_N.
PANTHER; PTHR11902; PTHR11902; 1.
Pfam; PF00113; Enolase_C; 1.
Pfam; PF03952; Enolase_N; 1.
PIRSF; PIRSF001400; Enolase; 1.
PRINTS; PR00148; ENOLASE.
SFLD; SFLDG00178; enolase; 1.
SFLD; SFLDS00001; Enolase; 1.
SMART; SM01192; Enolase_C; 1.
SMART; SM01193; Enolase_N; 1.
SUPFAM; SSF51604; SSF51604; 1.
TIGRFAMs; TIGR01060; eno; 1.
PROSITE; PS00164; ENOLASE; 1.
1: Evidence at protein level;
Acetylation; Cell membrane; Complete proteome; Cytoplasm;
Direct protein sequencing; Glycolysis; Isopeptide bond; Lyase;
Magnesium; Membrane; Metal-binding; Phosphoprotein;
Plasminogen activation; Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P06733}.
CHAIN 2 434 Alpha-enolase.
/FTId=PRO_0000134099.
REGION 370 373 Substrate binding. {ECO:0000250}.
REGION 405 434 Required for interaction with PLG.
{ECO:0000269|PubMed:7964722}.
ACT_SITE 210 210 Proton donor. {ECO:0000250}.
ACT_SITE 343 343 Proton acceptor. {ECO:0000250}.
METAL 40 40 Magnesium 1. {ECO:0000250}.
METAL 245 245 Magnesium 2. {ECO:0000250}.
METAL 293 293 Magnesium 2. {ECO:0000250}.
METAL 318 318 Magnesium 2. {ECO:0000250}.
BINDING 158 158 Substrate. {ECO:0000250}.
BINDING 167 167 Substrate. {ECO:0000250}.
BINDING 293 293 Substrate. {ECO:0000250}.
BINDING 318 318 Substrate. {ECO:0000250}.
BINDING 394 394 Substrate. {ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P06733}.
MOD_RES 5 5 N6-acetyllysine.
{ECO:0000250|UniProtKB:P06733}.
MOD_RES 44 44 Phosphotyrosine.
{ECO:0000250|UniProtKB:P06733}.
MOD_RES 60 60 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P17182}.
MOD_RES 60 60 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P17182}.
MOD_RES 64 64 N6-acetyllysine.
{ECO:0000250|UniProtKB:P06733}.
MOD_RES 71 71 N6-acetyllysine.
{ECO:0000250|UniProtKB:P06733}.
MOD_RES 89 89 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P06733}.
MOD_RES 89 89 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P17182}.
MOD_RES 126 126 N6-acetyllysine.
{ECO:0000250|UniProtKB:P06733}.
MOD_RES 193 193 N6-acetyllysine.
{ECO:0000250|UniProtKB:P06733}.
MOD_RES 199 199 N6-acetyllysine.
{ECO:0000250|UniProtKB:P06733}.
MOD_RES 202 202 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P17182}.
MOD_RES 228 228 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P06733}.
MOD_RES 228 228 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P17182}.
MOD_RES 233 233 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P06733}.
MOD_RES 233 233 N6-malonyllysine; alternate.
{ECO:0000250}.
MOD_RES 256 256 N6-acetyllysine.
{ECO:0000250|UniProtKB:P06733}.
MOD_RES 263 263 Phosphoserine.
{ECO:0000250|UniProtKB:P06733}.
MOD_RES 281 281 N6-acetyllysine.
{ECO:0000250|UniProtKB:P06733}.
MOD_RES 285 285 N6-acetyllysine.
{ECO:0000250|UniProtKB:P06733}.
MOD_RES 287 287 Phosphotyrosine.
{ECO:0000250|UniProtKB:P06733}.
MOD_RES 291 291 Phosphoserine.
{ECO:0000250|UniProtKB:P06733}.
MOD_RES 335 335 N6-acetyllysine.
{ECO:0000250|UniProtKB:P17182}.
MOD_RES 343 343 N6-acetyllysine.
{ECO:0000250|UniProtKB:P17182}.
MOD_RES 406 406 N6-acetyllysine.
{ECO:0000250|UniProtKB:P17182}.
MOD_RES 420 420 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P06733}.
MOD_RES 420 420 N6-malonyllysine; alternate.
{ECO:0000250}.
MOD_RES 420 420 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P17182}.
CROSSLNK 202 202 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P06733}.
CONFLICT 48 48 E -> Q (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 93 96 LMIE -> DQIK (in Ref. 6; AAK01319).
{ECO:0000305}.
CONFLICT 125 125 E -> G (in Ref. 1; CAA26456).
{ECO:0000305}.
CONFLICT 144 144 I -> T (in Ref. 1; CAA26456).
{ECO:0000305}.
CONFLICT 151 151 N -> D (in Ref. 6; AAK01319).
{ECO:0000305}.
CONFLICT 250 250 E -> Q (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 374 374 G -> E (in Ref. 1; CAA26456).
{ECO:0000305}.
SEQUENCE 434 AA; 47128 MW; 736660B2D5E936DC CRC64;
MSILKIHARE IFDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR DNDKTRFMGK
GVSKAVEHIN KTIAPALVSK KLNVVEQEKI DQLMIEMDGT ENKSKFGANA ILGVSLAVCK
AGAVEKGVPL YRHIADLAGN PEVILPVPAF NVINGGSHAG NKLAMQEFMI LPVGASSFRE
AMRIGAEVYH NLKNVIKEKY GKDATNVGDE GGFAPNILEN KEALELLKSA IAKAGYTDQV
VIGMDVAASE FYRAGKYDLD FKSPDDASRY ITPDQLADLY KSFIKDYPVV SIEDPFDQDD
WDAWQKFTAT AGIQVVGDDL TVTNPKRIAK AAGEKSCNCL LLKVNQIGSV TESLQACKLA
QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQI LRIEEELGSK
AKFAGRSFRN PLAK


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