DHE3_RAT
ID DHE3_RAT Reviewed; 558 AA.
AC P10860; Q66HI8; Q6LC16;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Glutamate dehydrogenase 1, mitochondrial;
DE Short=GDH 1;
DE EC=1.4.1.3 {ECO:0000250|UniProtKB:P00367};
DE AltName: Full=Memory-related gene 2 protein;
DE Short=MRG-2;
DE Flags: Precursor;
GN Name=Glud1; Synonyms=Glud;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=2704625; DOI=10.1093/nar/17.6.2356;
RA Amuro N., Ooki K., Ito A., Goto Y., Okazaki T.;
RT "Nucleotide sequence of rat liver glutamate dehydrogenase cDNA.";
RL Nucleic Acids Res. 17:2356-2357(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=2704624; DOI=10.1093/nar/17.6.2355;
RA Das A.T., Moerer P., Lamers W.H.;
RT "Nucleotide sequence of rat liver glutamate dehydrogenase cDNA.";
RL Nucleic Acids Res. 17:2355-2355(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=8094669; DOI=10.1111/j.1432-1033.1993.tb17611.x;
RA Das A.T., Arnberg A.C., Malingre H., Moerer P., Charles R., Moorman A.F.M.,
RA Lamers W.H.;
RT "Isolation and characterization of the rat gene encoding glutamate
RT dehydrogenase.";
RL Eur. J. Biochem. 211:795-803(1993).
RN [5]
RP PROTEIN SEQUENCE OF 108-123; 303-318; 347-363; 400-420; 481-496 AND
RP 504-516, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP PROTEIN SEQUENCE OF 161-190.
RX PubMed=1684101; DOI=10.1042/bj2800353;
RA Schwerdt G., Moller U., Huth W.;
RT "Identification of the CoA-modified forms of mitochondrial acetyl-CoA
RT acetyltransferase and of glutamate dehydrogenase as nearest-neighbour
RT proteins.";
RL Biochem. J. 280:353-357(1991).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 431-558, FUNCTION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RC STRAIN=Wistar; TISSUE=Hippocampus;
RX PubMed=9275181; DOI=10.1073/pnas.94.18.9669;
RA Cavallaro S., Meiri N., Yi C.-L., Musco S., Ma W., Goldberg J., Alkon D.L.;
RT "Late memory-related genes in the hippocampus revealed by RNA
RT fingerprinting.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:9669-9673(1997).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-128 AND THR-410, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Mitochondrial glutamate dehydrogenase that converts L-
CC glutamate into alpha-ketoglutarate. Plays a key role in glutamine
CC anaplerosis by producing alpha-ketoglutarate, an important intermediate
CC in the tricarboxylic acid cycle (By similarity). Plays a role in
CC insulin homeostasis (By similarity). May be involved in learning and
CC memory reactions by increasing the turnover of the excitatory
CC neurotransmitter glutamate (PubMed:9275181).
CC {ECO:0000250|UniProtKB:P00367, ECO:0000269|PubMed:9275181}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH +
CC NH4(+); Xref=Rhea:RHEA:15133, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.3;
CC Evidence={ECO:0000250|UniProtKB:P00367};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH +
CC NH4(+); Xref=Rhea:RHEA:11612, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.4.1.3;
CC Evidence={ECO:0000250|UniProtKB:P00367};
CC -!- ACTIVITY REGULATION: Subject to allosteric regulation. Activated by
CC ADP. Inhibited by GTP and ATP. ADP can occupy the NADH binding site and
CC activate the enzyme. Inhibited by SIRT4 (By similarity). Inhibited by
CC HADH (By similarity). {ECO:0000250|UniProtKB:P00367,
CC ECO:0000250|UniProtKB:P26443}.
CC -!- SUBUNIT: Homohexamer (By similarity). Interacts with HADH; this
CC interaction inhibits the activation of GLUD1 (By similarity).
CC {ECO:0000250|UniProtKB:P00366, ECO:0000250|UniProtKB:P26443}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P00367}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:P00367}. Note=Mostly
CC translocates into the mitochondria, only a small amount of the protein
CC localizes to the endoplasmic reticulum. {ECO:0000250|UniProtKB:P00367}.
CC -!- TISSUE SPECIFICITY: Widely expressed throughout the hippocampus. After
CC induction by training, highly expressed in the dentate gyrus, pyrimidal
CC layer and lacunosum moleculare. {ECO:0000269|PubMed:9275181}.
CC -!- INDUCTION: By water maze training in the hippocampus and in other
CC regions of the brain including the laterodorsal nucleus of the thalamus
CC and the cingulate cortex. {ECO:0000269|PubMed:9275181}.
CC -!- PTM: ADP-ribosylated by SIRT4, leading to inactivate glutamate
CC dehydrogenase activity. Stoichiometry shows that ADP-ribosylation
CC occurs in one subunit per catalytically active homohexamer.
CC {ECO:0000250|UniProtKB:P00367}.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000305}.
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DR EMBL; X14223; CAA32441.1; -; mRNA.
DR EMBL; X14044; CAA32202.1; -; mRNA.
DR EMBL; BC081841; AAH81841.1; -; mRNA.
DR EMBL; X64365; CAA45717.1; -; Genomic_DNA.
DR EMBL; U95148; AAB70012.1; -; mRNA.
DR PIR; S03707; S03707.
DR RefSeq; NP_036702.1; NM_012570.2.
DR AlphaFoldDB; P10860; -.
DR SMR; P10860; -.
DR BioGRID; 246566; 3.
DR IntAct; P10860; 9.
DR MINT; P10860; -.
DR STRING; 10116.ENSRNOP00000013789; -.
DR ChEMBL; CHEMBL2176833; -.
DR CarbonylDB; P10860; -.
DR iPTMnet; P10860; -.
DR PhosphoSitePlus; P10860; -.
DR World-2DPAGE; 0004:P10860; -.
DR jPOST; P10860; -.
DR PaxDb; P10860; -.
DR PRIDE; P10860; -.
DR Ensembl; ENSRNOT00000083446; ENSRNOP00000075032; ENSRNOG00000057367.
DR GeneID; 24399; -.
DR KEGG; rno:24399; -.
DR UCSC; RGD:2708; rat.
DR CTD; 2746; -.
DR RGD; 2708; Glud1.
DR eggNOG; KOG2250; Eukaryota.
DR GeneTree; ENSGT00390000000854; -.
DR HOGENOM; CLU_025763_1_0_1; -.
DR InParanoid; P10860; -.
DR OMA; PCFAAFP; -.
DR OrthoDB; 692851at2759; -.
DR PhylomeDB; P10860; -.
DR TreeFam; TF313945; -.
DR BRENDA; 1.4.1.3; 5301.
DR Reactome; R-RNO-2151201; Transcriptional activation of mitochondrial biogenesis.
DR Reactome; R-RNO-8964539; Glutamate and glutamine metabolism.
DR SABIO-RK; P10860; -.
DR PRO; PR:P10860; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000057367; Expressed in liver and 20 other tissues.
DR Genevisible; P10860; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0043531; F:ADP binding; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IDA:RGD.
DR GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:RHEA.
DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISO:RGD.
DR GO; GO:0070728; F:leucine binding; ISO:RGD.
DR GO; GO:0070403; F:NAD+ binding; ISO:RGD.
DR GO; GO:0021549; P:cerebellum development; IEP:RGD.
DR GO; GO:0006537; P:glutamate biosynthetic process; ISO:RGD.
DR GO; GO:0006538; P:glutamate catabolic process; ISO:RGD.
DR GO; GO:0006541; P:glutamine metabolic process; ISS:UniProtKB.
DR GO; GO:0007616; P:long-term memory; IEP:RGD.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISO:RGD.
DR GO; GO:0010044; P:response to aluminum ion; IDA:RGD.
DR GO; GO:0072350; P:tricarboxylic acid metabolic process; ISS:UniProtKB.
DR CDD; cd01076; NAD_bind_1_Glu_DH; 1.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
DR InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
DR InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR033922; NAD_bind_Glu_DH.
DR Pfam; PF00208; ELFV_dehydrog; 1.
DR Pfam; PF02812; ELFV_dehydrog_N; 1.
DR PRINTS; PR00082; GLFDHDRGNASE.
DR SMART; SM00839; ELFV_dehydrog; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; ADP-ribosylation; ATP-binding; Direct protein sequencing;
KW Endoplasmic reticulum; GTP-binding; Hydroxylation; Mitochondrion; NADP;
KW Nucleotide-binding; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..53
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P00367"
FT CHAIN 54..558
FT /note="Glutamate dehydrogenase 1, mitochondrial"
FT /id="PRO_0000007213"
FT ACT_SITE 183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT BINDING 141..143
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT BINDING 176
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT BINDING 252
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT BINDING 266
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT BINDING 270
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT BINDING 319
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT BINDING 322
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT BINDING 438
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT BINDING 444
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT BINDING 450
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT BINDING 516
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 68
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26443"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 84
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 84
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 90
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 110
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 110
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 135
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P26443"
FT MOD_RES 147
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P00367"
FT MOD_RES 162
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 162
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 171
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26443"
FT MOD_RES 172
FT /note="ADP-ribosylcysteine"
FT /evidence="ECO:0000250|UniProtKB:P00367"
FT MOD_RES 183
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 183
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P26443"
FT MOD_RES 187
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26443"
FT MOD_RES 191
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 191
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P26443"
FT MOD_RES 200
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26443"
FT MOD_RES 211
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26443"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00367"
FT MOD_RES 326
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26443"
FT MOD_RES 346
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P26443"
FT MOD_RES 346
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P26443"
FT MOD_RES 352
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P26443"
FT MOD_RES 352
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P26443"
FT MOD_RES 363
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 363
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 365
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 365
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P26443"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00367"
FT MOD_RES 386
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 390
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P26443"
FT MOD_RES 390
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P26443"
FT MOD_RES 399
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 410
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 415
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 415
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 457
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 457
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 457
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 477
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P26443"
FT MOD_RES 477
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P26443"
FT MOD_RES 480
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 480
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P26443"
FT MOD_RES 503
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 503
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 503
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 512
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00367"
FT MOD_RES 527
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 527
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 527
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 545
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 545
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 548
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26443"
FT CONFLICT 56..57
FT /note="AA -> GP (in Ref. 1; CAA32441)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 558 AA; 61416 MW; 388B8B5490C10F31 CRC64;
MYRRLGEVLL LSRAGPAALG SAAADSAALL GWARGQPSAV PQPGLTPVAR RHYSEAATDR
EDDPNFFKMV EGFFDRGASI VEDKLVEDLK TRENEEQKRN RVRGILRIIK PCNHVLSLSF
PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI RYSTDVSVDE VKALASLMTY KCAVVDVPFG
GAKAGVKINP KNYTDNELEK ITRRFTMELA KKGFIGPGID VPAPDMSTGE REMSWIADTY
ASTIGHYDIN AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGLG
DKTFVVQGFG NVGLHSMRYL HRFGAKCVGV GESDGSIWNP DGIDPKELED FKLQHGSILG
FPKAKVYEGS ILEADCDILI PAASEKQLTK SNAPRVKAKI IAEGANGPTT PEADKIFLER
NIMVIPDLYL NAGGVTVSYF EWLKNLNHVS YGRLTFKYER DSNYHLLMSV QESLERKFGK
HGGTIPVVPT AEFQDRISGA SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV
NAIEKVFKVY NEAGVTFT
