DHE4_HUMAN
ID DHE4_HUMAN Reviewed; 558 AA.
AC P49448; B2R8G0; Q9UDQ4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Glutamate dehydrogenase 2, mitochondrial;
DE Short=GDH 2;
DE EC=1.4.1.3;
DE Flags: Precursor;
GN Name=GLUD2; Synonyms=GLUDP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Retina;
RX PubMed=8207021; DOI=10.1016/s0021-9258(19)89484-x;
RA Shashidharan P., Michaelidis T.M., Robakis N.K., Kresovali A.,
RA Papamatheakis J., Plaitakis A.;
RT "Novel human glutamate dehydrogenase expressed in neural and testicular
RT tissues and encoded by an X-linked intronless gene.";
RL J. Biol. Chem. 269:16971-16976(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [5]
RP ADP-RIBOSYLATION AT CYS-172.
RX PubMed=16023112; DOI=10.1016/j.febslet.2005.06.041;
RA Choi M.M., Huh J.W., Yang S.J., Cho E.H., Choi S.Y., Cho S.W.;
RT "Identification of ADP-ribosylation site in human glutamate dehydrogenase
RT isozymes.";
RL FEBS Lett. 579:4125-4130(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP TRANSIT PEPTIDE CLEAVAGE SITE, AND SUBCELLULAR LOCATION.
RX PubMed=22709669; DOI=10.1016/j.neuint.2012.06.006;
RA Kotzamani D., Plaitakis A.;
RT "Alpha helical structures in the leader sequence of human GLUD2 glutamate
RT dehydrogenase responsible for mitochondrial import.";
RL Neurochem. Int. 61:463-469(2012).
CC -!- FUNCTION: Important for recycling the chief excitatory
CC neurotransmitter, glutamate, during neurotransmission.
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:0000255|PROSITE-ProRule:PRU10011};
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:0000255|PROSITE-ProRule:PRU10011};
CC -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:22709669}.
CC -!- TISSUE SPECIFICITY: Expressed in retina, testis and, at a lower level,
CC brain.
CC -!- PTM: Stoichiometry shows that ADP-ribosylation occurs in one subunit
CC per catalytically active homohexamer.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000305}.
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DR EMBL; X66310; CAA46995.1; -; Genomic_DNA.
DR EMBL; U08997; AAA20969.1; -; Genomic_DNA.
DR EMBL; AK313356; BAG36157.1; -; mRNA.
DR EMBL; AC006144; AAD05030.1; -; Genomic_DNA.
DR EMBL; BC050732; AAH50732.1; -; mRNA.
DR CCDS; CCDS14603.1; -.
DR PIR; A53719; A53719.
DR RefSeq; NP_036216.2; NM_012084.3.
DR PDB; 6G2U; X-ray; 2.93 A; A/B/C/D/E/F=54-558.
DR PDBsum; 6G2U; -.
DR AlphaFoldDB; P49448; -.
DR SMR; P49448; -.
DR BioGRID; 109009; 27.
DR IntAct; P49448; 13.
DR MINT; P49448; -.
DR STRING; 9606.ENSP00000327589; -.
DR BindingDB; P49448; -.
DR DrugBank; DB00142; Glutamic acid.
DR DrugBank; DB00157; NADH.
DR DrugCentral; P49448; -.
DR iPTMnet; P49448; -.
DR PhosphoSitePlus; P49448; -.
DR SwissPalm; P49448; -.
DR BioMuta; GLUD2; -.
DR DMDM; 13432152; -.
DR REPRODUCTION-2DPAGE; IPI00027146; -.
DR EPD; P49448; -.
DR jPOST; P49448; -.
DR MassIVE; P49448; -.
DR MaxQB; P49448; -.
DR PaxDb; P49448; -.
DR PeptideAtlas; P49448; -.
DR PRIDE; P49448; -.
DR ProteomicsDB; 56012; -.
DR Antibodypedia; 29957; 228 antibodies from 28 providers.
DR DNASU; 2747; -.
DR Ensembl; ENST00000328078.3; ENSP00000327589.1; ENSG00000182890.5.
DR Ensembl; ENST00000673493.1; ENSP00000500546.1; ENSG00000288118.1.
DR GeneID; 2747; -.
DR KEGG; hsa:2747; -.
DR MANE-Select; ENST00000328078.3; ENSP00000327589.1; NM_012084.4; NP_036216.2.
DR UCSC; uc004eto.4; human.
DR CTD; 2747; -.
DR DisGeNET; 2747; -.
DR GeneCards; GLUD2; -.
DR HGNC; HGNC:4336; GLUD2.
DR HPA; ENSG00000182890; Group enriched (liver, testis).
DR MalaCards; GLUD2; -.
DR MIM; 300144; gene.
DR neXtProt; NX_P49448; -.
DR OpenTargets; ENSG00000182890; -.
DR PharmGKB; PA28738; -.
DR VEuPathDB; HostDB:ENSG00000182890; -.
DR eggNOG; KOG2250; Eukaryota.
DR GeneTree; ENSGT00390000000854; -.
DR HOGENOM; CLU_025763_1_0_1; -.
DR InParanoid; P49448; -.
DR OMA; YHDINAH; -.
DR OrthoDB; 692851at2759; -.
DR PhylomeDB; P49448; -.
DR TreeFam; TF313945; -.
DR BioCyc; MetaCyc:HS00018-MON; -.
DR BRENDA; 1.4.1.3; 2681.
DR PathwayCommons; P49448; -.
DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR Reactome; R-HSA-8964539; Glutamate and glutamine metabolism.
DR SABIO-RK; P49448; -.
DR SignaLink; P49448; -.
DR SIGNOR; P49448; -.
DR BioGRID-ORCS; 2747; 14 hits in 707 CRISPR screens.
DR GeneWiki; GLUD2; -.
DR GenomeRNAi; 2747; -.
DR Pharos; P49448; Tbio.
DR PRO; PR:P49448; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P49448; protein.
DR Bgee; ENSG00000182890; Expressed in right testis and 99 other tissues.
DR ExpressionAtlas; P49448; baseline and differential.
DR Genevisible; P49448; HS.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
DR GO; GO:0043531; F:ADP binding; IDA:BHF-UCL.
DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:RHEA.
DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IDA:BHF-UCL.
DR GO; GO:0005525; F:GTP binding; IDA:BHF-UCL.
DR GO; GO:0070728; F:leucine binding; IDA:BHF-UCL.
DR GO; GO:0006537; P:glutamate biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0006538; P:glutamate catabolic process; IDA:BHF-UCL.
DR GO; GO:0006536; P:glutamate metabolic process; IDA: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 3D-structure; ADP-ribosylation; Mitochondrion; NADP; Oxidoreductase;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..53
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:22709669"
FT CHAIN 54..558
FT /note="Glutamate dehydrogenase 2, mitochondrial"
FT /id="PRO_0000007208"
FT ACT_SITE 183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 172
FT /note="ADP-ribosylcysteine"
FT /evidence="ECO:0000269|PubMed:16023112"
FT VARIANT 498
FT /note="S -> A (in dbSNP:rs9697983)"
FT /id="VAR_048867"
FT CONFLICT 286
FT /note="E -> Q (in Ref. 1; CAA46995/AAA20969)"
FT /evidence="ECO:0000305"
FT HELIX 66..87
FT /evidence="ECO:0007829|PDB:6G2U"
FT HELIX 95..109
FT /evidence="ECO:0007829|PDB:6G2U"
FT STRAND 113..123
FT /evidence="ECO:0007829|PDB:6G2U"
FT STRAND 129..138
FT /evidence="ECO:0007829|PDB:6G2U"
FT STRAND 142..152
FT /evidence="ECO:0007829|PDB:6G2U"
FT HELIX 158..174
FT /evidence="ECO:0007829|PDB:6G2U"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:6G2U"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:6G2U"
FT HELIX 195..211
FT /evidence="ECO:0007829|PDB:6G2U"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:6G2U"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:6G2U"
FT HELIX 230..242
FT /evidence="ECO:0007829|PDB:6G2U"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:6G2U"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:6G2U"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:6G2U"
FT HELIX 271..284
FT /evidence="ECO:0007829|PDB:6G2U"
FT HELIX 287..293
FT /evidence="ECO:0007829|PDB:6G2U"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:6G2U"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:6G2U"
FT HELIX 311..322
FT /evidence="ECO:0007829|PDB:6G2U"
FT STRAND 326..331
FT /evidence="ECO:0007829|PDB:6G2U"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:6G2U"
FT HELIX 345..355
FT /evidence="ECO:0007829|PDB:6G2U"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:6G2U"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:6G2U"
FT STRAND 375..381
FT /evidence="ECO:0007829|PDB:6G2U"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:6G2U"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:6G2U"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:6G2U"
FT STRAND 399..402
FT /evidence="ECO:0007829|PDB:6G2U"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:6G2U"
FT HELIX 411..419
FT /evidence="ECO:0007829|PDB:6G2U"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:6G2U"
FT HELIX 427..430
FT /evidence="ECO:0007829|PDB:6G2U"
FT HELIX 433..447
FT /evidence="ECO:0007829|PDB:6G2U"
FT TURN 451..455
FT /evidence="ECO:0007829|PDB:6G2U"
FT HELIX 456..477
FT /evidence="ECO:0007829|PDB:6G2U"
FT HELIX 491..497
FT /evidence="ECO:0007829|PDB:6G2U"
FT HELIX 502..527
FT /evidence="ECO:0007829|PDB:6G2U"
FT HELIX 534..551
FT /evidence="ECO:0007829|PDB:6G2U"
SQ SEQUENCE 558 AA; 61434 MW; F222B1B2CB74A6EA CRC64;
MYRYLAKALL PSRAGPAALG SAANHSAALL GRGRGQPAAA SQPGLALAAR RHYSELVADR
EDDPNFFKMV EGFFDRGASI VEDKLVKDLR TQESEEQKRN RVRGILRIIK PCNHVLSLSF
PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI RYSTDVSVDE VKALASLMTY KCAVVDVPFG
GAKAGVKINP KNYTENELEK ITRRFTMELA KKGFIGPGVD VPAPDMNTGE REMSWIADTY
ASTIGHYDIN AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFR
DKTFVVQGFG NVGLHSMRYL HRFGAKCIAV GESDGSIWNP DGIDPKELED FKLQHGSILG
FPKAKPYEGS ILEVDCDILI PAATEKQLTK SNAPRVKAKI IAEGANGPTT PEADKIFLER
NILVIPDLYL NAGGVTVSYF EWLKNLNHVS YGRLTFKYER DSNYHLLLSV QESLERKFGK
HGGTIPIVPT AEFQDSISGA SEKDIVHSAL AYTMERSARQ IMHTAMKYNL GLDLRTAAYV
NAIEKVFKVY SEAGVTFT
