G3P3_YEAST
ID G3P3_YEAST Reviewed; 332 AA.
AC P00359; D6VUX4; Q6Q5P9;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 3;
DE Short=GAPDH 3;
DE EC=1.2.1.12;
GN Name=TDH3; Synonyms=GPD3; OrderedLocusNames=YGR192C; ORFNames=G7576;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=385592; DOI=10.1016/s0021-9258(19)83593-7;
RA Holland J.P., Holland M.J.;
RT "The primary structure of a glyceraldehyde-3-phosphate dehydrogenase gene
RT from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 254:9839-9845(1979).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7645350; DOI=10.1002/yea.320110609;
RA Arroyo J., Garcia-Gonzalez M., Garcia-Saez M.I., Sanchez M., Nombela C.;
RT "The complete sequence of a 9037 bp DNA fragment of the right arm of
RT Saccharomyces cerevisiae chromosome VII.";
RL Yeast 11:587-591(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP PARTIAL PROTEIN SEQUENCE OF 2-332, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=11946592; DOI=10.1016/0014-5793(72)80040-1;
RA Jones G.M., Harris J.I.;
RT "Glyceraldehyde 3-phosphate dehydrogenase: Amino acid sequence of enzyme
RT from baker's yeast.";
RL FEBS Lett. 22:185-189(1972).
RN [7]
RP PROTEIN SEQUENCE OF 47-58.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7895733; DOI=10.1002/elps.11501501210;
RA Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B.,
RA Volpe T., Warner J.R., McLaughlin C.S.;
RT "Protein identifications for a Saccharomyces cerevisiae protein database.";
RL Electrophoresis 15:1466-1486(1994).
RN [8]
RP PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 38531 / Y41, and ATCC 44827 / SKQ2N;
RX PubMed=7737086; DOI=10.1002/elps.1150160124;
RA Norbeck J., Blomberg A.;
RT "Gene linkage of two-dimensional polyacrylamide gel electrophoresis
RT resolved proteins from isogene families in Saccharomyces cerevisiae by
RT microsequencing of in-gel trypsin generated peptides.";
RL Electrophoresis 16:149-156(1995).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=11502169; DOI=10.1021/bi010277r;
RA Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S.,
RA Schmitter J.-M.;
RT "Yeast mitochondrial dehydrogenases are associated in a supramolecular
RT complex.";
RL Biochemistry 40:9758-9769(2001).
RN [10]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [15]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-46 AND LYS-63, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
RA Garcia-Saez I., Kozielski F., Job D., Boscheron C.;
RT "Structure of GAPDH 3 from S.cerevisiae at 2.0 A resolution.";
RL Submitted (DEC-2010) to the PDB data bank.
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS), AND SUBUNIT.
RX PubMed=22869137; DOI=10.1107/s1744309112028989;
RA Liu Q., Wang H., Liu H., Teng M., Li X.;
RT "Preliminary crystallographic analysis of glyceraldehyde-3-phosphate
RT dehydrogenase 3 from Saccharomyces cerevisiae.";
RL Acta Crystallogr. F 68:978-980(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-
CC phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10009};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:22869137}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11502169}.
CC Mitochondrion {ECO:0000269|PubMed:16823961}.
CC -!- MISCELLANEOUS: There are three genes for G3PDH in yeast.
CC -!- MISCELLANEOUS: Present with 169000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; V01300; CAA24607.1; -; Genomic_DNA.
DR EMBL; J01324; AAA88714.1; -; Genomic_DNA.
DR EMBL; X82408; CAA57803.1; -; Genomic_DNA.
DR EMBL; Z72977; CAA97218.1; -; Genomic_DNA.
DR EMBL; AY557831; AAS56157.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08285.1; -; Genomic_DNA.
DR PIR; S55870; DEBYG2.
DR RefSeq; NP_011708.3; NM_001181321.3.
DR PDB; 3PYM; X-ray; 2.00 A; A/B=1-332.
DR PDB; 4IQ8; X-ray; 2.49 A; A=1-332.
DR PDBsum; 3PYM; -.
DR PDBsum; 4IQ8; -.
DR AlphaFoldDB; P00359; -.
DR SMR; P00359; -.
DR BioGRID; 33445; 298.
DR DIP; DIP-4309N; -.
DR IntAct; P00359; 102.
DR MINT; P00359; -.
DR STRING; 4932.YGR192C; -.
DR MoonDB; P00359; Curated.
DR MoonProt; P00359; -.
DR CarbonylDB; P00359; -.
DR iPTMnet; P00359; -.
DR COMPLUYEAST-2DPAGE; P00359; -.
DR SWISS-2DPAGE; P00359; -.
DR MaxQB; P00359; -.
DR PaxDb; P00359; -.
DR PRIDE; P00359; -.
DR TopDownProteomics; P00359; -.
DR EnsemblFungi; YGR192C_mRNA; YGR192C; YGR192C.
DR GeneID; 853106; -.
DR KEGG; sce:YGR192C; -.
DR SGD; S000003424; TDH3.
DR VEuPathDB; FungiDB:YGR192C; -.
DR eggNOG; KOG0657; Eukaryota.
DR GeneTree; ENSGT00940000153298; -.
DR HOGENOM; CLU_030140_0_3_1; -.
DR InParanoid; P00359; -.
DR OMA; NCVAPMA; -.
DR BioCyc; YEAST:YGR192C-MON; -.
DR BRENDA; 1.2.1.12; 984.
DR Reactome; R-SCE-70171; Glycolysis.
DR Reactome; R-SCE-70263; Gluconeogenesis.
DR SABIO-RK; P00359; -.
DR UniPathway; UPA00109; UER00184.
DR PRO; PR:P00359; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P00359; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IDA:SGD.
DR GO; GO:1904408; F:melatonin binding; IDA:SGD.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0006915; P:apoptotic process; IMP:SGD.
DR GO; GO:0006094; P:gluconeogenesis; IEP:SGD.
DR GO; GO:0006096; P:glycolytic process; IEP:SGD.
DR GO; GO:0015886; P:heme transport; IMP:SGD.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:SGD.
DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10836; PTHR10836; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 1.
DR PIRSF; PIRSF000149; GAP_DH; 1.
DR PRINTS; PR00078; G3PDHDRGNASE.
DR SMART; SM00846; Gp_dh_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Glycolysis;
KW Isopeptide bond; Mitochondrion; NAD; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11946592"
FT CHAIN 2..332
FT /note="Glyceraldehyde-3-phosphate dehydrogenase 3"
FT /id="PRO_0000145591"
FT ACT_SITE 150
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 11..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 149..151
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 209..210
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 177
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 46
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 63
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 136
FT /note="E -> V (in Ref. 1; CAA24607/AAA88714)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="N -> D (in Ref. 1; CAA24607/AAA88714)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="D -> G (in Ref. 5; AAS56157)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="V -> I (in Ref. 1; CAA24607/AAA88714)"
FT /evidence="ECO:0000305"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:3PYM"
FT HELIX 11..22
FT /evidence="ECO:0007829|PDB:3PYM"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:3PYM"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:3PYM"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:3PYM"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:3PYM"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:3PYM"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:3PYM"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:3PYM"
FT TURN 85..89
FT /evidence="ECO:0007829|PDB:3PYM"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:3PYM"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:3PYM"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:3PYM"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:3PYM"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:3PYM"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:3PYM"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:3PYM"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:3PYM"
FT HELIX 150..166
FT /evidence="ECO:0007829|PDB:3PYM"
FT STRAND 168..178
FT /evidence="ECO:0007829|PDB:3PYM"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:3PYM"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:3PYM"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:3PYM"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:3PYM"
FT HELIX 211..218
FT /evidence="ECO:0007829|PDB:3PYM"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:3PYM"
FT STRAND 225..234
FT /evidence="ECO:0007829|PDB:3PYM"
FT STRAND 239..249
FT /evidence="ECO:0007829|PDB:3PYM"
FT HELIX 253..265
FT /evidence="ECO:0007829|PDB:3PYM"
FT TURN 266..271
FT /evidence="ECO:0007829|PDB:3PYM"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:3PYM"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:3PYM"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:3PYM"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:3PYM"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:3PYM"
FT STRAND 305..312
FT /evidence="ECO:0007829|PDB:3PYM"
FT HELIX 316..331
FT /evidence="ECO:0007829|PDB:3PYM"
SQ SEQUENCE 332 AA; 35747 MW; 6CFFFEE7061BC36F CRC64;
MVRVAINGFG RIGRLVMRIA LSRPNVEVVA LNDPFITNDY AAYMFKYDST HGRYAGEVSH
DDKHIIVDGK KIATYQERDP ANLPWGSSNV DIAIDSTGVF KELDTAQKHI DAGAKKVVIT
APSSTAPMFV MGVNEEKYTS DLKIVSNASC TTNCLAPLAK VINDAFGIEE GLMTTVHSLT
ATQKTVDGPS HKDWRGGRTA SGNIIPSSTG AAKAVGKVLP ELQGKLTGMA FRVPTVDVSV
VDLTVKLNKE TTYDEIKKVV KAAAEGKLKG VLGYTEDAVV SSDFLGDSHS SIFDASAGIQ
LSPKFVKLVS WYDNEYGYST RVVDLVEHVA KA
