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   27-MAR-2024, entry version 191.
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; 32.
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   GlyGen; P49448; 1 site, 1 O-linked glycan (1 site).
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; 9606-ENSP00000327589; -.
DR   PeptideAtlas; P49448; -.
DR   ProteomicsDB; 56012; -.
DR   Pumba; P49448; -.
DR   Antibodypedia; 29957; 242 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   AGR; HGNC:4336; -.
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; DINALSC; -.
DR   OrthoDB; 45283at2759; -.
DR   PhylomeDB; P49448; -.
DR   TreeFam; TF313945; -.
DR   BioCyc; MetaCyc:HS00018-MONOMER; -.
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; 15 hits in 783 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 100 other cell types or tissues.
DR   ExpressionAtlas; P49448; baseline and differential.
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   Gene3D; 1.10.287.140; -; 1.
DR   Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR006095; Glu/Leu/Phe/Val/Trp_DH.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val/Trp_DH_dimer.
DR   InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR033922; NAD_bind_Glu_DH.
DR   PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11606:SF15; GLUTAMATE DEHYDROGENASE 2, MITOCHONDRIAL; 1.
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; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
DR   Genevisible; P49448; HS.
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
//