PDK4_HUMAN
ID PDK4_HUMAN Reviewed; 411 AA.
AC Q16654;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 4, mitochondrial;
DE EC=2.7.11.2;
DE AltName: Full=Pyruvate dehydrogenase kinase isoform 4;
DE Flags: Precursor;
GN Name=PDK4; Synonyms=PDHK4;
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 / MRNA].
RX PubMed=8798399; DOI=10.1074/jbc.271.37.22376;
RA Rowles J., Scherer S.W., Xi T., Majer M., Nickle D.C., Rommens J.M.,
RA Popov K.M., Harris R.A., Riebow N.L., Xia J., Tsui L.-C., Bogardus C.,
RA Prochazka M.;
RT "Cloning and characterization of PDK4 on 7q21.3 encoding a fourth pyruvate
RT dehydrogenase kinase isoenzyme in human.";
RL J. Biol. Chem. 271:22376-22382(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
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 TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=14966024; DOI=10.1152/japplphysiol.01318.2003;
RA Spriet L.L., Tunstall R.J., Watt M.J., Mehan K.A., Hargreaves M.,
RA Cameron-Smith D.;
RT "Pyruvate dehydrogenase activation and kinase expression in human skeletal
RT muscle during fasting.";
RL J. Appl. Physiol. 96:2082-2087(2004).
RN [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=15955060; DOI=10.1111/j.1742-4658.2005.04713.x;
RA Abbot E.L., McCormack J.G., Reynet C., Hassall D.G., Buchan K.W.,
RA Yeaman S.J.;
RT "Diverging regulation of pyruvate dehydrogenase kinase isoform gene
RT expression in cultured human muscle cells.";
RL FEBS J. 272:3004-3014(2005).
RN [6]
RP INDUCTION BY PPARD.
RX PubMed=17669420; DOI=10.1016/j.jmb.2007.06.091;
RA Degenhardt T., Saramaki A., Malinen M., Rieck M., Vaisanen S., Huotari A.,
RA Herzig K.H., Muller R., Carlberg C.;
RT "Three members of the human pyruvate dehydrogenase kinase gene family are
RT direct targets of the peroxisome proliferator-activated receptor
RT beta/delta.";
RL J. Mol. Biol. 372:341-355(2007).
RN [7]
RP FUNCTION.
RX PubMed=21852536; DOI=10.1101/gad.16771811;
RA Grassian A.R., Metallo C.M., Coloff J.L., Stephanopoulos G., Brugge J.S.;
RT "Erk regulation of pyruvate dehydrogenase flux through PDK4 modulates cell
RT proliferation.";
RL Genes Dev. 25:1716-1733(2011).
RN [8]
RP INDUCTION.
RX PubMed=20715114; DOI=10.1002/ijc.25599;
RA Blouin J.M., Penot G., Collinet M., Nacfer M., Forest C., Laurent-Puig P.,
RA Coumoul X., Barouki R., Benelli C., Bortoli S.;
RT "Butyrate elicits a metabolic switch in human colon cancer cells by
RT targeting the pyruvate dehydrogenase complex.";
RL Int. J. Cancer 128:2591-2601(2011).
RN [9]
RP FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=21816445; DOI=10.1016/j.metabol.2011.06.014;
RA Kulkarni S.S., Salehzadeh F., Fritz T., Zierath J.R., Krook A., Osler M.E.;
RT "Mitochondrial regulators of fatty acid metabolism reflect metabolic
RT dysfunction in type 2 diabetes mellitus.";
RL Metabolism 61:175-185(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 20-411 IN COMPLEX WITH ATP,
RP FUNCTION, ACTIVITY REGULATION, SUBUNIT, AND MUTAGENESIS OF TYR-157;
RP ARG-161; ASP-394 AND TRP-395.
RX PubMed=18658136; DOI=10.1074/jbc.m802249200;
RA Wynn R.M., Kato M., Chuang J.L., Tso S.C., Li J., Chuang D.T.;
RT "Pyruvate dehydrogenase kinase-4 structures reveal a metastable open
RT conformation fostering robust core-free basal activity.";
RL J. Biol. Chem. 283:25305-25315(2008).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 20-411 IN COMPLEX WITH ATP
RP ANALOG, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=21904029; DOI=10.1107/s090744491102405x;
RA Kukimoto-Niino M., Tokmakov A., Terada T., Ohbayashi N., Fujimoto T.,
RA Gomi S., Shiromizu I., Kawamoto M., Matsusue T., Shirouzu M., Yokoyama S.;
RT "Inhibitor-bound structures of human pyruvate dehydrogenase kinase 4.";
RL Acta Crystallogr. D 67:763-773(2011).
RN [12]
RP VARIANTS [LARGE SCALE ANALYSIS] VAL-17; MET-19 AND GLY-109.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Kinase that plays a key role in regulation of glucose and
CC fatty acid metabolism and homeostasis via phosphorylation of the
CC pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate
CC dehydrogenase activity, and thereby regulates metabolite flux through
CC the tricarboxylic acid cycle, down-regulates aerobic respiration and
CC inhibits the formation of acetyl-coenzyme A from pyruvate. Inhibition
CC of pyruvate dehydrogenase decreases glucose utilization and increases
CC fat metabolism in response to prolonged fasting and starvation. Plays
CC an important role in maintaining normal blood glucose levels under
CC starvation, and is involved in the insulin signaling cascade. Via its
CC regulation of pyruvate dehydrogenase activity, plays an important role
CC in maintaining normal blood pH and in preventing the accumulation of
CC ketone bodies under starvation. In the fed state, mediates cellular
CC responses to glucose levels and to a high-fat diet. Regulates both
CC fatty acid oxidation and de novo fatty acid biosynthesis. Plays a role
CC in the generation of reactive oxygen species. Protects detached
CC epithelial cells against anoikis. Plays a role in cell proliferation
CC via its role in regulating carbohydrate and fatty acid metabolism.
CC {ECO:0000269|PubMed:15955060, ECO:0000269|PubMed:18658136,
CC ECO:0000269|PubMed:21816445, ECO:0000269|PubMed:21852536}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[pyruvate dehydrogenase E1 alpha subunit] = ADP
CC + H(+) + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha subunit];
CC Xref=Rhea:RHEA:23052, Rhea:RHEA-COMP:13689, Rhea:RHEA-COMP:13690,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.2;
CC Evidence={ECO:0000269|PubMed:21904029};
CC -!- SUBUNIT: Homodimer. Interacts with the pyruvate dehydrogenase complex
CC subunit DLAT, and is part of the multimeric pyruvate dehydrogenase
CC complex that contains multiple copies of pyruvate dehydrogenase (E1),
CC dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide
CC dehydrogenase (DLD, E3). {ECO:0000269|PubMed:18658136,
CC ECO:0000269|PubMed:21904029}.
CC -!- INTERACTION:
CC Q16654; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-2861674, EBI-742388;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- TISSUE SPECIFICITY: Ubiquitous; highest levels of expression in heart
CC and skeletal muscle. {ECO:0000269|PubMed:14966024,
CC ECO:0000269|PubMed:21816445}.
CC -!- INDUCTION: Up-regulated by prolonged fasting, in glucose-deprived cells
CC and in response to a high-fat diet. Down-regulated by insulin. Up-
CC regulated by PPARD. {ECO:0000269|PubMed:14966024,
CC ECO:0000269|PubMed:15955060, ECO:0000269|PubMed:17669420,
CC ECO:0000269|PubMed:20715114, ECO:0000269|PubMed:21816445}.
CC -!- SIMILARITY: Belongs to the PDK/BCKDK protein kinase family.
CC {ECO:0000305}.
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DR EMBL; U54628; AAC50670.1; -; Genomic_DNA.
DR EMBL; U54618; AAC50670.1; JOINED; Genomic_DNA.
DR EMBL; U54619; AAC50670.1; JOINED; Genomic_DNA.
DR EMBL; U54620; AAC50670.1; JOINED; Genomic_DNA.
DR EMBL; U54621; AAC50670.1; JOINED; Genomic_DNA.
DR EMBL; U54622; AAC50670.1; JOINED; Genomic_DNA.
DR EMBL; U54623; AAC50670.1; JOINED; Genomic_DNA.
DR EMBL; U54624; AAC50670.1; JOINED; Genomic_DNA.
DR EMBL; U54625; AAC50670.1; JOINED; Genomic_DNA.
DR EMBL; U54626; AAC50670.1; JOINED; Genomic_DNA.
DR EMBL; U54627; AAC50670.1; JOINED; Genomic_DNA.
DR EMBL; U54617; AAC50669.1; -; mRNA.
DR EMBL; AC002451; AAB67048.1; -; Genomic_DNA.
DR EMBL; BC040239; AAH40239.1; -; mRNA.
DR CCDS; CCDS5643.1; -.
DR RefSeq; NP_002603.1; NM_002612.3.
DR PDB; 2E0A; X-ray; 1.86 A; A/B=20-411.
DR PDB; 2ZDX; X-ray; 2.54 A; A/B=20-411.
DR PDB; 2ZDY; X-ray; 2.40 A; A/B=20-411.
DR PDB; 2ZKJ; X-ray; 2.00 A; A/B=20-411.
DR PDB; 3D2R; X-ray; 2.03 A; A/B=20-411.
DR PDB; 7EAT; X-ray; 2.10 A; A/B=10-411.
DR PDB; 7EBB; X-ray; 1.90 A; A/B=10-411.
DR PDB; 7EBG; X-ray; 1.95 A; A/B=10-411.
DR PDBsum; 2E0A; -.
DR PDBsum; 2ZDX; -.
DR PDBsum; 2ZDY; -.
DR PDBsum; 2ZKJ; -.
DR PDBsum; 3D2R; -.
DR PDBsum; 7EAT; -.
DR PDBsum; 7EBB; -.
DR PDBsum; 7EBG; -.
DR AlphaFoldDB; Q16654; -.
DR SMR; Q16654; -.
DR BioGRID; 111192; 18.
DR IntAct; Q16654; 48.
DR STRING; 9606.ENSP00000005178; -.
DR BindingDB; Q16654; -.
DR ChEMBL; CHEMBL4141; -.
DR DrugBank; DB08356; 4-[4-(4-methoxyphenyl)-5-methyl-1H-pyrazol-3-yl]benzene-1,3-diol.
DR DrugBank; DB00755; Tretinoin.
DR DrugCentral; Q16654; -.
DR GuidetoPHARMACOLOGY; 2144; -.
DR iPTMnet; Q16654; -.
DR PhosphoSitePlus; Q16654; -.
DR BioMuta; PDK4; -.
DR DMDM; 3183120; -.
DR EPD; Q16654; -.
DR jPOST; Q16654; -.
DR MassIVE; Q16654; -.
DR PaxDb; Q16654; -.
DR PeptideAtlas; Q16654; -.
DR PRIDE; Q16654; -.
DR ProteomicsDB; 61013; -.
DR Antibodypedia; 15901; 637 antibodies from 36 providers.
DR DNASU; 5166; -.
DR Ensembl; ENST00000005178.6; ENSP00000005178.5; ENSG00000004799.8.
DR GeneID; 5166; -.
DR KEGG; hsa:5166; -.
DR MANE-Select; ENST00000005178.6; ENSP00000005178.5; NM_002612.4; NP_002603.1.
DR UCSC; uc003uoa.4; human.
DR CTD; 5166; -.
DR DisGeNET; 5166; -.
DR GeneCards; PDK4; -.
DR HGNC; HGNC:8812; PDK4.
DR HPA; ENSG00000004799; Tissue enhanced (skeletal muscle, tongue).
DR MIM; 602527; gene.
DR neXtProt; NX_Q16654; -.
DR OpenTargets; ENSG00000004799; -.
DR PharmGKB; PA33157; -.
DR VEuPathDB; HostDB:ENSG00000004799; -.
DR eggNOG; KOG0787; Eukaryota.
DR GeneTree; ENSGT01030000234646; -.
DR HOGENOM; CLU_023861_1_1_1; -.
DR InParanoid; Q16654; -.
DR OMA; HQENCPS; -.
DR OrthoDB; 1242599at2759; -.
DR PhylomeDB; Q16654; -.
DR TreeFam; TF314918; -.
DR BRENDA; 2.7.11.2; 2681.
DR PathwayCommons; Q16654; -.
DR Reactome; R-HSA-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR Reactome; R-HSA-5362517; Signaling by Retinoic Acid.
DR SignaLink; Q16654; -.
DR SIGNOR; Q16654; -.
DR BioGRID-ORCS; 5166; 8 hits in 1113 CRISPR screens.
DR ChiTaRS; PDK4; human.
DR EvolutionaryTrace; Q16654; -.
DR GeneWiki; PDK4; -.
DR GenomeRNAi; 5166; -.
DR Pharos; Q16654; Tchem.
DR PRO; PR:Q16654; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q16654; protein.
DR Bgee; ENSG00000004799; Expressed in seminal vesicle and 186 other tissues.
DR ExpressionAtlas; Q16654; baseline and differential.
DR Genevisible; Q16654; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0004740; F:pyruvate dehydrogenase (acetyl-transferring) kinase activity; EXP:Reactome.
DR GO; GO:0071398; P:cellular response to fatty acid; IMP:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; IDA:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:2000811; P:negative regulation of anoikis; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:UniProtKB.
DR GO; GO:0010510; P:regulation of acetyl-CoA biosynthetic process from pyruvate; IMP:UniProtKB.
DR GO; GO:0045124; P:regulation of bone resorption; IEA:Ensembl.
DR GO; GO:0010565; P:regulation of cellular ketone metabolic process; ISS:UniProtKB.
DR GO; GO:0042304; P:regulation of fatty acid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0046320; P:regulation of fatty acid oxidation; ISS:UniProtKB.
DR GO; GO:0010906; P:regulation of glucose metabolic process; IMP:UniProtKB.
DR GO; GO:0006885; P:regulation of pH; ISS:UniProtKB.
DR GO; GO:0042594; P:response to starvation; ISS:UniProtKB.
DR Gene3D; 1.20.140.20; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR036784; AK/P_DHK_N_sf.
DR InterPro; IPR018955; BCDHK/PDK_N.
DR InterPro; IPR039028; BCKD/PDK.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR PANTHER; PTHR11947; PTHR11947; 1.
DR Pfam; PF10436; BCDHK_Adom3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR SUPFAM; SSF69012; SSF69012; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Carbohydrate metabolism; Glucose metabolism;
KW Kinase; Mitochondrion; Nucleotide-binding; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..411
FT /note="[Pyruvate dehydrogenase (acetyl-transferring)]
FT kinase isozyme 4, mitochondrial"
FT /id="PRO_0000023445"
FT DOMAIN 138..368
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT BINDING 254..261
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:18658136"
FT BINDING 293
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:18658136"
FT BINDING 312..313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:18658136"
FT BINDING 329..334
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:18658136"
FT SITE 157
FT /note="Interaction with the other subunit in the homodimer"
FT SITE 161
FT /note="Interaction with the other subunit in the homodimer"
FT SITE 395
FT /note="Interaction with the other subunit in the homodimer"
FT VARIANT 17
FT /note="A -> V (in dbSNP:rs56391840)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042298"
FT VARIANT 19
FT /note="L -> M (in dbSNP:rs55761955)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042299"
FT VARIANT 109
FT /note="D -> G (in dbSNP:rs34898343)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042300"
FT MUTAGEN 157
FT /note="Y->F: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18658136"
FT MUTAGEN 161
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18658136"
FT MUTAGEN 394
FT /note="D->A: Loss of activity; when associated with A-395."
FT /evidence="ECO:0000269|PubMed:18658136"
FT MUTAGEN 395
FT /note="W->A: Loss of activity; when associated with A-394."
FT /evidence="ECO:0000269|PubMed:18658136"
FT HELIX 22..27
FT /evidence="ECO:0007829|PDB:2E0A"
FT HELIX 37..42
FT /evidence="ECO:0007829|PDB:2E0A"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:7EBB"
FT HELIX 50..72
FT /evidence="ECO:0007829|PDB:2E0A"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:2E0A"
FT HELIX 83..100
FT /evidence="ECO:0007829|PDB:2E0A"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:2E0A"
FT HELIX 110..127
FT /evidence="ECO:0007829|PDB:2E0A"
FT HELIX 130..142
FT /evidence="ECO:0007829|PDB:2E0A"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:2E0A"
FT HELIX 153..180
FT /evidence="ECO:0007829|PDB:2E0A"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:2E0A"
FT HELIX 200..219
FT /evidence="ECO:0007829|PDB:2E0A"
FT STRAND 225..234
FT /evidence="ECO:0007829|PDB:2E0A"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:2E0A"
FT HELIX 245..266
FT /evidence="ECO:0007829|PDB:2E0A"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:2E0A"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:2E0A"
FT STRAND 276..282
FT /evidence="ECO:0007829|PDB:2E0A"
FT STRAND 284..293
FT /evidence="ECO:0007829|PDB:2E0A"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:2E0A"
FT HELIX 303..306
FT /evidence="ECO:0007829|PDB:2E0A"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:7EBG"
FT HELIX 333..343
FT /evidence="ECO:0007829|PDB:2E0A"
FT STRAND 347..353
FT /evidence="ECO:0007829|PDB:2E0A"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:2E0A"
FT STRAND 357..367
FT /evidence="ECO:0007829|PDB:2E0A"
FT TURN 368..370
FT /evidence="ECO:0007829|PDB:2E0A"
FT HELIX 380..385
FT /evidence="ECO:0007829|PDB:2E0A"
SQ SEQUENCE 411 AA; 46469 MW; C17B78B6057000E9 CRC64;
MKAARFVLRS AGSLNGAGLV PREVEHFSRY SPSPLSMKQL LDFGSENACE RTSFAFLRQE
LPVRLANILK EIDILPTQLV NTSSVQLVKS WYIQSLMDLV EFHEKSPDDQ KALSDFVDTL
IKVRNRHHNV VPTMAQGIIE YKDACTVDPV TNQNLQYFLD RFYMNRISTR MLMNQHILIF
SDSQTGNPSH IGSIDPNCDV VAVVQDAFEC SRMLCDQYYL SSPELKLTQV NGKFPDQPIH
IVYVPSHLHH MLFELFKNAM RATVEHQENQ PSLTPIEVIV VLGKEDLTIK ISDRGGGVPL
RIIDRLFSYT YSTAPTPVMD NSRNAPLAGF GYGLPISRLY AKYFQGDLNL YSLSGYGTDA
IIYLKALSSE SIEKLPVFNK SAFKHYQMSS EADDWCIPSR EPKNLAKEVA M
