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 27-MAR-2024, entry version 209. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.ENSRNOP00000073191; -. DR MoonProt; P04764; -. DR GlyGen; P04764; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P04764; -. DR PhosphoSitePlus; P04764; -. DR SwissPalm; P04764; -. DR jPOST; P04764; -. DR PaxDb; 10116-ENSRNOP00000024106; -. DR Ensembl; ENSRNOT00000081579.2; ENSRNOP00000073191.1; ENSRNOG00000017895.8. DR Ensembl; ENSRNOT00055026761; ENSRNOP00055021685; ENSRNOG00055015695. DR Ensembl; ENSRNOT00060044686; ENSRNOP00060037039; ENSRNOG00060025698. DR Ensembl; ENSRNOT00065018506; ENSRNOP00065014146; ENSRNOG00065011372. DR GeneID; 24333; -. DR KEGG; rno:24333; -. DR UCSC; RGD:2553; rat. DR AGR; RGD:2553; -. DR CTD; 2023; -. DR RGD; 2553; Eno1. DR eggNOG; KOG2670; Eukaryota. DR GeneTree; ENSGT00950000182805; -. DR InParanoid; P04764; -. DR OrthoDB; 1093250at2759; -. 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 cell types or tissues. DR ExpressionAtlas; P04764; baseline and differential. 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: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: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:0045892; P:negative regulation of DNA-templated transcription; 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:2001171; P:positive regulation of ATP biosynthetic process; 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; Enolase-like C-terminal domain; 1. DR Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 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 NCBIfam; TIGR01060; eno; 1. DR PANTHER; PTHR11902:SF58; ALPHA-ENOLASE; 1. 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 SFLD; SFLDS00001; Enolase; 1. DR SFLD; SFLDF00002; enolase; 1. DR SMART; SM01192; Enolase_C; 1. DR SMART; SM01193; Enolase_N; 1. DR SUPFAM; SSF51604; Enolase C-terminal domain-like; 1. DR SUPFAM; SSF54826; Enolase N-terminal domain-like; 1. DR PROSITE; PS00164; ENOLASE; 1. DR World-2DPAGE; 0004:P04764; -. DR Genevisible; P04764; RN. 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 //