ENOA_RAT
ID ENOA_RAT Reviewed; 434 AA.
AC P04764; Q66HI3; Q6AYV3; Q6P504;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Alpha-enolase;
DE EC=4.2.1.11 {ECO:0000269|PubMed:8594891};
DE AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE AltName: Full=Enolase 1;
DE AltName: Full=Non-neural enolase;
DE Short=NNE;
GN Name=Eno1; Synonyms=Eno-1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Brain, and Liver;
RX PubMed=2989793; DOI=10.1093/nar/13.12.4365;
RA Sakimura K., Kushiya E., Obinata M., Takahashi Y.;
RT "Molecular cloning and the nucleotide sequence of cDNA to mRNA for non-
RT neuronal enolase (alpha alpha enolase) of rat brain and liver.";
RL Nucleic Acids Res. 13:4365-4378(1985).
RN [2]
RP SEQUENCE REVISION.
RA Takahashi Y.;
RL Submitted (JAN-1986) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart, Pituitary, and Testis;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 10-28; 33-50; 72-103; 106-120; 163-179; 184-193;
RP 203-228; 234-262; 270-281; 307-326; 336-394 AND 407-420, AND IDENTIFICATION
RP BY 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 [5]
RP PROTEIN SEQUENCE OF 46-57; 97-109; 245-262 AND 369-382, AND INTERACTION
RP WITH PLG.
RC TISSUE=Embryonic brain;
RX PubMed=7964722; DOI=10.1046/j.1471-4159.1994.63062048.x;
RA Nakajima K., Hamanoue M., Takemoto N., Hattori T., Kato K., Kohsaka S.;
RT "Plasminogen binds specifically to alpha-enolase on rat neuronal plasma
RT membrane.";
RL J. Neurochem. 63:2048-2057(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 93-153.
RC TISSUE=Lymphoma;
RA Bole-Feysot C., Kelly P.A.;
RT "Rat cDNA encoding alpha enolase (2-phospho-D-glycerate hydro-lyase) (non-
RT neural enolase) (NNE).";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP DEVELOPMENTAL STAGE, AND CATALYTIC ACTIVITY.
RX PubMed=8594891; DOI=10.1152/ajpheart.1995.269.6.h1843;
RA Keller A., Rouzeau J.-D., Farhadian F., Wisnewsky C., Marotte F.,
RA Lamande N., Samuel J.L., Schwartz K., Lazar M., Lucas M.;
RT "Differential expression of alpha- and beta-enolase genes during rat heart
RT development and hypertrophy.";
RL Am. J. Physiol. 269:H1843-H1851(1995).
RN [8]
RP INDUCTION.
RX PubMed=10662718; DOI=10.1152/ajpendo.2000.278.2.e330;
RA Merkulova T., Keller A., Oliviero P., Marotte F., Samuel J.L.,
RA Rappaport L., Lamande N., Lucas M.;
RT "Thyroid hormones differentially modulate enolase isozymes during rat
RT skeletal and cardiac muscle development.";
RL Am. J. Physiol. 278:E330-E339(2000).
RN [9]
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).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=19423663; DOI=10.1530/rep-09-0052;
RA Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.;
RT "Identification of novel immunodominant epididymal sperm proteins using
RT combinatorial approach.";
RL Reproduction 138:81-93(2009).
CC -!- FUNCTION: Glycolytic enzyme that catalyzes the conversion of 2-
CC phosphoglycerate to phosphoenolpyruvate. In addition to glycolysis,
CC involved in various processes such as growth control, hypoxia tolerance
CC and allergic responses. May also function in the intravascular and
CC pericellular fibrinolytic system due to its ability to serve as a
CC receptor and activator of plasminogen on the cell surface of several
CC cell-types such as leukocytes and neurons. Stimulates immunoglobulin
CC production. {ECO:0000250|UniProtKB:P06733}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289,
CC ChEBI:CHEBI:58702; EC=4.2.1.11;
CC Evidence={ECO:0000269|PubMed:8594891};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10165;
CC Evidence={ECO:0000305|PubMed:8594891};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P06733};
CC Note=Binds two Mg(2+) per subunit. Required for catalysis and for
CC stabilizing the dimer. {ECO:0000250|UniProtKB:P06733};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000305|PubMed:8594891}.
CC -!- SUBUNIT: Mammalian enolase is composed of 3 isozyme subunits, alpha,
CC beta and gamma, which can form homodimers or heterodimers which are
CC cell-type and development-specific (By similarity). ENO1 interacts with
CC PLG in the neuronal plasma membrane and promotes its activation. The C-
CC terminal lysine is required for this binding (PubMed:7964722).
CC Interacts with ENO4 and PGAM2 (By similarity). Interacts with CMTM6 (By
CC similarity). {ECO:0000250|UniProtKB:P06733,
CC ECO:0000250|UniProtKB:P17182, ECO:0000269|PubMed:7964722}.
CC -!- INTERACTION:
CC P04764; Q5VU43-11: PDE4DIP; Xeno; NbExp=2; IntAct=EBI-915852, EBI-10769071;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Can translocate to
CC the plasma membrane in either the homodimeric (alpha/alpha) or
CC heterodimeric (alpha/gamma) form.
CC -!- TISSUE SPECIFICITY: Expressed in flagella of epididymal sperm. The
CC alpha/alpha homodimer is expressed in embryo and in most adult tissues.
CC The alpha/beta heterodimer and the beta/beta homodimer are found in
CC striated muscle, and the alpha/gamma heterodimer and the gamma/gamma
CC homodimer in neurons. {ECO:0000269|PubMed:19423663}.
CC -!- DEVELOPMENTAL STAGE: During ontogenesis, there is a transition from the
CC alpha/alpha homodimer to the alpha/beta heterodimer in striated muscle
CC cells, and to the alpha/gamma heterodimer in nerve cells. In brain,
CC levels of ENO1 decrease around 10 dpc and then gradually increase to
CC adult age. In embryonic heart, ENO1 levels decrease rapidly during
CC cardiac development. {ECO:0000269|PubMed:2989793,
CC ECO:0000269|PubMed:8594891}.
CC -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P06733}.
CC -!- PTM: Lysine 2-hydroxyisobutyrylation (Khib) by p300/EP300 activates the
CC phosphopyruvate hydratase activity. {ECO:0000250|UniProtKB:P06733}.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH63174.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X02610; CAA26456.1; -; mRNA.
DR EMBL; BC063174; AAH63174.1; ALT_INIT; mRNA.
DR EMBL; BC078896; AAH78896.1; -; mRNA.
DR EMBL; BC081847; AAH81847.2; -; mRNA.
DR EMBL; AF241613; AAK01319.1; -; mRNA.
DR PIR; A23126; A23126.
DR RefSeq; NP_001103378.1; NM_001109908.1.
DR RefSeq; NP_036686.2; NM_012554.3.
DR AlphaFoldDB; P04764; -.
DR SMR; P04764; -.
DR BioGRID; 246510; 4.
DR IntAct; P04764; 10.
DR MINT; P04764; -.
DR STRING; 10116.ENSRNOP00000024106; -.
DR MoonProt; P04764; -.
DR iPTMnet; P04764; -.
DR PhosphoSitePlus; P04764; -.
DR SwissPalm; P04764; -.
DR World-2DPAGE; 0004:P04764; -.
DR jPOST; P04764; -.
DR PaxDb; P04764; -.
DR PRIDE; P04764; -.
DR Ensembl; ENSRNOT00000081579; ENSRNOP00000073191; ENSRNOG00000017895.
DR GeneID; 24333; -.
DR KEGG; rno:24333; -.
DR UCSC; RGD:2553; rat.
DR CTD; 2023; -.
DR RGD; 2553; Eno1.
DR eggNOG; KOG2670; Eukaryota.
DR GeneTree; ENSGT00950000182805; -.
DR InParanoid; P04764; -.
DR OMA; EFMIIPV; -.
DR OrthoDB; 773373at2759; -.
DR PhylomeDB; P04764; -.
DR TreeFam; TF300391; -.
DR BRENDA; 4.2.1.11; 5301.
DR Reactome; R-RNO-70171; Glycolysis.
DR Reactome; R-RNO-70263; Gluconeogenesis.
DR SABIO-RK; P04764; -.
DR UniPathway; UPA00109; UER00187.
DR PRO; PR:P04764; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000017895; Expressed in adult mammalian kidney and 18 other tissues.
DR ExpressionAtlas; P04764; baseline and differential.
DR Genevisible; P04764; RN.
DR GO; GO:0005938; C:cell cortex; IDA:CAFA.
DR GO; GO:0009986; C:cell surface; IDA:CAFA.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0005829; C:cytosol; IDA:CAFA.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; ISO:RGD.
DR GO; GO:0030426; C:growth cone; IDA:CAFA.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:CAFA.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0005640; C:nuclear outer membrane; ISO:RGD.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IDA:CAFA.
DR GO; GO:0005886; C:plasma membrane; IDA:CAFA.
DR GO; GO:0097060; C:synaptic membrane; IDA:RGD.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; IPI:CAFA.
DR GO; GO:0051020; F:GTPase binding; ISO:RGD.
DR GO; GO:0031072; F:heat shock protein binding; IPI:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IDA:CAFA.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
DR GO; GO:0001222; F:transcription corepressor binding; ISO:RGD.
DR GO; GO:0061621; P:canonical glycolysis; IDA:CAFA.
DR GO; GO:0071456; P:cellular response to hypoxia; IDA:CAFA.
DR GO; GO:0098761; P:cellular response to interleukin-7; ISO:RGD.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:CAFA.
DR GO; GO:0006094; P:gluconeogenesis; ISO:RGD.
DR GO; GO:0006096; P:glycolytic process; IDA:CAFA.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:RGD.
DR GO; GO:1903298; P:negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; ISO:RGD.
DR GO; GO:0051099; P:positive regulation of binding; ISO:RGD.
DR GO; GO:0045933; P:positive regulation of muscle contraction; ISO:RGD.
DR GO; GO:0010756; P:positive regulation of plasminogen activation; ISO:RGD.
DR GO; GO:0009615; P:response to virus; ISO:RGD.
DR CDD; cd03313; enolase; 1.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR HAMAP; MF_00318; Enolase; 1.
DR InterPro; IPR000941; Enolase.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR020810; Enolase_C.
DR InterPro; IPR020809; Enolase_CS.
DR InterPro; IPR020811; Enolase_N.
DR PANTHER; PTHR11902; PTHR11902; 1.
DR Pfam; PF00113; Enolase_C; 1.
DR Pfam; PF03952; Enolase_N; 1.
DR PIRSF; PIRSF001400; Enolase; 1.
DR PRINTS; PR00148; ENOLASE.
DR SFLD; SFLDF00002; enolase; 1.
DR SMART; SM01192; Enolase_C; 1.
DR SMART; SM01193; Enolase_N; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR TIGRFAMs; TIGR01060; eno; 1.
DR PROSITE; PS00164; ENOLASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cytoplasm; Direct protein sequencing;
KW Glycolysis; Hydroxylation; Isopeptide bond; Lyase; Magnesium; Membrane;
KW Metal-binding; Phosphoprotein; Plasminogen activation; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT CHAIN 2..434
FT /note="Alpha-enolase"
FT /id="PRO_0000134099"
FT REGION 405..434
FT /note="Required for interaction with PLG"
FT /evidence="ECO:0000269|PubMed:7964722"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT ACT_SITE 343
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT BINDING 318
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT BINDING 370..373
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT BINDING 394
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 5
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 44
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 60
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17182"
FT MOD_RES 60
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17182"
FT MOD_RES 64
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 71
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 89
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 89
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17182"
FT MOD_RES 126
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 193
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 202
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17182"
FT MOD_RES 228
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 228
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 228
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17182"
FT MOD_RES 233
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 233
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 256
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 281
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 281
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 285
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 287
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 335
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P17182"
FT MOD_RES 343
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P17182"
FT MOD_RES 406
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P17182"
FT MOD_RES 420
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 420
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 420
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17182"
FT CROSSLNK 202
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT CONFLICT 48
FT /note="E -> Q (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 93..96
FT /note="LMIE -> DQIK (in Ref. 6; AAK01319)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="E -> G (in Ref. 1; CAA26456)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="I -> T (in Ref. 1; CAA26456)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="N -> D (in Ref. 6; AAK01319)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="E -> Q (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="G -> E (in Ref. 1; CAA26456)"
FT /evidence="ECO:0000305"
SQ 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
