ID KHK_HUMAN Reviewed; 298 AA. AC P50053; Q6IBK2; Q99532; Q9BRJ3; Q9UMN1; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2015, sequence version 2. DT 12-OCT-2022, entry version 202. DE RecName: Full=Ketohexokinase {ECO:0000312|HGNC:HGNC:6315}; DE EC=2.7.1.3 {ECO:0000269|PubMed:12941785}; DE AltName: Full=Hepatic fructokinase; GN Name=KHK {ECO:0000312|HGNC:HGNC:6315}; 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 [MRNA], VARIANTS FRUCT ARG-40 AND THR-43, AND VARIANT RP ILE-49. RX PubMed=7833921; DOI=10.1093/hmg/3.9.1627; RA Bonthron D.T., Brady N., Donaldson I.A., Steinmann B.; RT "Molecular basis of essential fructosuria: molecular cloning and mutational RT analysis of human ketohexokinase (fructokinase)."; RL Hum. Mol. Genet. 3:1627-1631(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; 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 [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26 AND 71-298, ALTERNATIVE SPLICING, RP AND TISSUE SPECIFICITY. RX PubMed=9799106; DOI=10.1046/j.1432-1327.1998.2570085.x; RA Hayward B.E., Bonthron D.T.; RT "Structure and alternative splicing of the ketohexokinase gene."; RL Eur. J. Biochem. 257:85-91(1998). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [8] {ECO:0007744|PDB:2HQQ, ECO:0007744|PDB:2HW1} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH BETA-D-FRUCTOSE AND RP AMP-PNP, X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF ISOFORM A, SUBUNIT, AND RP SUBSTRATE-BINDING SITES. RX PubMed=19237742; DOI=10.1107/s0907444908041115; RA Trinh C.H., Asipu A., Bonthron D.T., Phillips S.E.; RT "Structures of alternatively spliced isoforms of human ketohexokinase."; RL Acta Crystallogr. D 65:201-211(2009). RN [9] RP CHARACTERIZATION OF VARIANTS FRUCT ARG-40 AND THR-43, FUNCTION, RP BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY. RX PubMed=12941785; DOI=10.2337/diabetes.52.9.2426; RA Asipu A., Hayward B.E., O'Reilly J., Bonthron D.T.; RT "Properties of normal and mutant recombinant human ketohexokinases and RT implications for the pathogenesis of essential fructosuria."; RL Diabetes 52:2426-2432(2003). CC -!- FUNCTION: Catalyzes the phosphorylation of the ketose sugar fructose to CC fructose-1-phosphate. {ECO:0000269|PubMed:12941785}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + beta-D-fructose = ADP + beta-D-fructose 1-phosphate + CC H(+); Xref=Rhea:RHEA:18145, ChEBI:CHEBI:15378, ChEBI:CHEBI:28645, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:138881, ChEBI:CHEBI:456216; CC EC=2.7.1.3; Evidence={ECO:0000269|PubMed:12941785}; CC -!- ACTIVITY REGULATION: Requires potassium. Inhibition by ADP. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.8 mM for D-fructose (at 25 degrees Celsius) CC {ECO:0000269|PubMed:12941785}; CC KM=0.15 mM for Mg-ATP (at 25 degrees Celsius) CC {ECO:0000269|PubMed:12941785}; CC Note=kcat is 7.6 sec(-1). {ECO:0000269|PubMed:12941785}; CC -!- PATHWAY: Carbohydrate metabolism; fructose metabolism. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19237742}. CC -!- INTERACTION: CC P50053; Q9NQ69: LHX9; NbExp=3; IntAct=EBI-1053974, EBI-10175218; CC P50053-2; Q92624: APPBP2; NbExp=3; IntAct=EBI-12204387, EBI-743771; CC P50053-2; P50458: LHX2; NbExp=3; IntAct=EBI-12204387, EBI-12179869; CC P50053-2; Q9NQ69: LHX9; NbExp=3; IntAct=EBI-12204387, EBI-10175218; CC P50053-2; P60891-1: PRPS1; NbExp=4; IntAct=EBI-12204387, EBI-16205225; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=C {ECO:0000269|PubMed:9799106}; Synonyms=Central, CC hepatic/renal/intestinal {ECO:0000269|PubMed:9799106}; CC IsoId=P50053-1; Sequence=Displayed; CC Name=A {ECO:0000269|PubMed:9799106}; Synonyms=Peripheral CC {ECO:0000269|PubMed:9799106}; CC IsoId=P50053-2; Sequence=VSP_004669; CC -!- TISSUE SPECIFICITY: Most abundant in liver, kidney, gut, spleen and CC pancreas. Low levels also found in adrenal, muscle, brain and eye. CC {ECO:0000269|PubMed:9799106}. CC -!- DISEASE: Fructosuria (FRUCT) [MIM:229800]: Benign defect of CC intermediary metabolism. {ECO:0000269|PubMed:12941785, CC ECO:0000269|PubMed:7833921}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: [Isoform A]: More widely distributed but with a low CC expression level. KM=7 mM for D-fructose (at 25 degrees Celsius). CC KM=036 mM for Mg-ATP (at 25 degrees Celsius). kcat is 6.9 sec(-1). CC {ECO:0000269|PubMed:12941785}. CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X78678; CAA55347.1; -; mRNA. DR EMBL; X78677; CAA55346.1; -; mRNA. DR EMBL; CR456801; CAG33082.1; -; mRNA. DR EMBL; AC013403; AAX93167.1; -; Genomic_DNA. DR EMBL; CH471053; EAX00643.1; -; Genomic_DNA. DR EMBL; BC006233; AAH06233.1; -; mRNA. DR EMBL; Y09336; CAA70516.1; -; Genomic_DNA. DR EMBL; Y09341; CAA70522.1; -; Genomic_DNA. DR EMBL; Y09341; CAA70523.1; -; Genomic_DNA. DR EMBL; Y09340; CAA70521.1; -; Genomic_DNA. DR EMBL; AJ005168; CAA06409.1; -; Genomic_DNA. DR CCDS; CCDS1734.1; -. [P50053-2] DR CCDS; CCDS1735.1; -. [P50053-1] DR RefSeq; NP_000212.1; NM_000221.2. [P50053-2] DR RefSeq; NP_006479.1; NM_006488.2. [P50053-1] DR PDB; 2HLZ; X-ray; 1.85 A; A/B/C/D=5-298. DR PDB; 2HQQ; X-ray; 1.86 A; A=1-298. DR PDB; 2HW1; X-ray; 2.10 A; A=1-298. DR PDB; 3B3L; X-ray; 2.90 A; A/B/C/D=1-298. DR PDB; 3NBV; X-ray; 2.30 A; A/B=5-298. DR PDB; 3NBW; X-ray; 2.34 A; A/B=5-298. DR PDB; 3NC2; X-ray; 2.50 A; A/B=5-298. DR PDB; 3NC9; X-ray; 2.40 A; A/B=5-298. DR PDB; 3NCA; X-ray; 2.60 A; A/B=5-298. DR PDB; 3Q92; X-ray; 2.80 A; A/B=5-298. DR PDB; 3QA2; X-ray; 2.52 A; A/B=5-298. DR PDB; 3QAI; X-ray; 2.70 A; A/B=5-298. DR PDB; 3RO4; X-ray; 2.60 A; A/B=5-298. DR PDB; 5WBM; X-ray; 2.16 A; A/B=5-298. DR PDB; 5WBO; X-ray; 2.25 A; A/B=5-298. DR PDB; 5WBP; X-ray; 2.74 A; A/B=5-298. DR PDB; 5WBQ; X-ray; 2.40 A; A/B=5-298. DR PDB; 5WBR; X-ray; 2.58 A; A/B=5-298. DR PDB; 5WBZ; X-ray; 2.40 A; A/B=5-298. DR PDB; 6UL7; X-ray; 2.30 A; A=1-298. DR PDB; 6W0N; X-ray; 2.41 A; A/B=5-298. DR PDB; 6W0W; X-ray; 2.80 A; A/B=5-298. DR PDB; 6W0X; X-ray; 2.38 A; A/B=5-298. DR PDB; 6W0Y; X-ray; 2.54 A; A/B=5-298. DR PDB; 6W0Z; X-ray; 2.30 A; A/B=5-298. DR PDBsum; 2HLZ; -. DR PDBsum; 2HQQ; -. DR PDBsum; 2HW1; -. DR PDBsum; 3B3L; -. DR PDBsum; 3NBV; -. DR PDBsum; 3NBW; -. DR PDBsum; 3NC2; -. DR PDBsum; 3NC9; -. DR PDBsum; 3NCA; -. DR PDBsum; 3Q92; -. DR PDBsum; 3QA2; -. DR PDBsum; 3QAI; -. DR PDBsum; 3RO4; -. DR PDBsum; 5WBM; -. DR PDBsum; 5WBO; -. DR PDBsum; 5WBP; -. DR PDBsum; 5WBQ; -. DR PDBsum; 5WBR; -. DR PDBsum; 5WBZ; -. DR PDBsum; 6UL7; -. DR PDBsum; 6W0N; -. DR PDBsum; 6W0W; -. DR PDBsum; 6W0X; -. DR PDBsum; 6W0Y; -. DR PDBsum; 6W0Z; -. DR AlphaFoldDB; P50053; -. DR SMR; P50053; -. DR BioGRID; 109996; 26. DR DIP; DIP-50184N; -. DR IntAct; P50053; 8. DR STRING; 9606.ENSP00000260599; -. DR BindingDB; P50053; -. DR ChEMBL; CHEMBL1275212; -. DR iPTMnet; P50053; -. DR PhosphoSitePlus; P50053; -. DR BioMuta; KHK; -. DR DMDM; 1730044; -. DR REPRODUCTION-2DPAGE; IPI00029488; -. DR EPD; P50053; -. DR jPOST; P50053; -. DR MassIVE; P50053; -. DR MaxQB; P50053; -. DR PaxDb; P50053; -. DR PeptideAtlas; P50053; -. DR PRIDE; P50053; -. DR ProteomicsDB; 56192; -. [P50053-1] DR ProteomicsDB; 56193; -. [P50053-2] DR Antibodypedia; 2054; 500 antibodies from 32 providers. DR DNASU; 3795; -. DR Ensembl; ENST00000260598.10; ENSP00000260598.5; ENSG00000138030.13. [P50053-1] DR Ensembl; ENST00000260599.10; ENSP00000260599.6; ENSG00000138030.13. [P50053-2] DR GeneID; 3795; -. DR KEGG; hsa:3795; -. DR MANE-Select; ENST00000260598.10; ENSP00000260598.5; NM_006488.3; NP_006479.1. DR UCSC; uc002ril.3; human. [P50053-1] DR CTD; 3795; -. DR DisGeNET; 3795; -. DR GeneCards; KHK; -. DR HGNC; HGNC:6315; KHK. DR HPA; ENSG00000138030; Group enriched (intestine, kidney, liver). DR MalaCards; KHK; -. DR MIM; 229800; phenotype. DR MIM; 614058; gene. DR neXtProt; NX_P50053; -. DR OpenTargets; ENSG00000138030; -. DR Orphanet; 2056; Essential fructosuria. DR PharmGKB; PA30095; -. DR VEuPathDB; HostDB:ENSG00000138030; -. DR eggNOG; KOG2947; Eukaryota. DR GeneTree; ENSGT00390000007458; -. DR HOGENOM; CLU_027634_3_0_1; -. DR InParanoid; P50053; -. DR OMA; AQFPQAW; -. DR OrthoDB; 720391at2759; -. DR TreeFam; TF323942; -. DR BioCyc; MetaCyc:HS06437-MON; -. DR BRENDA; 2.7.1.3; 2681. DR PathwayCommons; P50053; -. DR Reactome; R-HSA-5657562; Essential fructosuria. DR Reactome; R-HSA-70350; Fructose catabolism. DR SABIO-RK; P50053; -. DR SignaLink; P50053; -. DR SIGNOR; P50053; -. DR UniPathway; UPA00202; -. DR BioGRID-ORCS; 3795; 13 hits in 1076 CRISPR screens. DR EvolutionaryTrace; P50053; -. DR GenomeRNAi; 3795; -. DR Pharos; P50053; Tchem. DR PRO; PR:P50053; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P50053; protein. DR Bgee; ENSG00000138030; Expressed in right lobe of liver and 139 other tissues. DR ExpressionAtlas; P50053; baseline and differential. DR Genevisible; P50053; HS. DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004454; F:ketohexokinase activity; IDA:MGI. DR GO; GO:0006000; P:fructose metabolic process; IBA:GO_Central. DR GO; GO:0070873; P:regulation of glycogen metabolic process; IBA:GO_Central. DR GO; GO:0009750; P:response to fructose; IBA:GO_Central. DR GO; GO:0009749; P:response to glucose; IBA:GO_Central. DR GO; GO:0032868; P:response to insulin; IBA:GO_Central. DR GO; GO:0009744; P:response to sucrose; IBA:GO_Central. DR GO; GO:0010043; P:response to zinc ion; IBA:GO_Central. DR CDD; cd01939; Ketohexokinase; 1. DR Gene3D; 3.40.1190.20; -; 1. DR InterPro; IPR034093; KHK. DR InterPro; IPR011611; PfkB_dom. DR InterPro; IPR029056; Ribokinase-like. DR Pfam; PF00294; PfkB; 1. DR SUPFAM; SSF53613; SSF53613; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Carbohydrate metabolism; KW Disease variant; Kinase; Nucleotide-binding; Reference proteome; KW Transferase. FT CHAIN 1..298 FT /note="Ketohexokinase" FT /id="PRO_0000080088" FT BINDING 15 FT /ligand="beta-D-fructose" FT /ligand_id="ChEBI:CHEBI:28645" FT /evidence="ECO:0000269|PubMed:19237742, FT ECO:0007744|PDB:2HW1" FT BINDING 41 FT /ligand="beta-D-fructose" FT /ligand_id="ChEBI:CHEBI:28645" FT /evidence="ECO:0007744|PDB:2HW1" FT BINDING 42 FT /ligand="beta-D-fructose" FT /ligand_id="ChEBI:CHEBI:28645" FT /evidence="ECO:0007744|PDB:2HW1" FT BINDING 45 FT /ligand="beta-D-fructose" FT /ligand_id="ChEBI:CHEBI:28645" FT /evidence="ECO:0007744|PDB:2HW1" FT BINDING 108 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305|PubMed:19237742, FT ECO:0007744|PDB:2HW1" FT BINDING 226..229 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305|PubMed:19237742, FT ECO:0007744|PDB:2HW1" FT BINDING 255..258 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305|PubMed:19237742, FT ECO:0007744|PDB:2HW1" FT BINDING 258 FT /ligand="beta-D-fructose" FT /ligand_id="ChEBI:CHEBI:28645" FT /evidence="ECO:0007744|PDB:2HW1" FT VAR_SEQ 72..115 FT /note="LVADFRRRGVDVSQVAWQSKGDTPSSCCIINNSNGNRTIVLHDT -> VLDD FT LRRYSVDLRYTVFQTTGSVPIATVIINEASGSRTILYYDR (in isoform A)" FT /evidence="ECO:0000305" FT /id="VSP_004669" FT VARIANT 40 FT /note="G -> R (in FRUCT; loss of ketohexokinase function; FT insoluble; dbSNP:rs104893643)" FT /evidence="ECO:0000269|PubMed:12941785, FT ECO:0000269|PubMed:7833921" FT /id="VAR_006072" FT VARIANT 43 FT /note="A -> T (in FRUCT; no effect on ketohexokinase FT function; decreases enzyme activity but no effect in FT substrate affinity; decreases thermal stability; FT dbSNP:rs104893644)" FT /evidence="ECO:0000269|PubMed:12941785, FT ECO:0000269|PubMed:7833921" FT /id="VAR_006073" FT VARIANT 49 FT /note="V -> I (in dbSNP:rs2304681)" FT /evidence="ECO:0000269|PubMed:7833921" FT /id="VAR_006074" FT STRAND 5..10 FT /evidence="ECO:0007829|PDB:2HLZ" FT STRAND 13..22 FT /evidence="ECO:0007829|PDB:2HLZ" FT STRAND 29..31 FT /evidence="ECO:0007829|PDB:2HLZ" FT STRAND 33..41 FT /evidence="ECO:0007829|PDB:2HLZ" FT HELIX 42..53 FT /evidence="ECO:0007829|PDB:2HLZ" FT STRAND 57..63 FT /evidence="ECO:0007829|PDB:2HLZ" FT HELIX 67..78 FT /evidence="ECO:0007829|PDB:2HLZ" FT STRAND 86..88 FT /evidence="ECO:0007829|PDB:2HLZ" FT STRAND 90..92 FT /evidence="ECO:0007829|PDB:2HQQ" FT STRAND 96..102 FT /evidence="ECO:0007829|PDB:2HLZ" FT TURN 103..105 FT /evidence="ECO:0007829|PDB:2HLZ" FT STRAND 108..113 FT /evidence="ECO:0007829|PDB:2HLZ" FT HELIX 122..126 FT /evidence="ECO:0007829|PDB:2HLZ" FT HELIX 130..132 FT /evidence="ECO:0007829|PDB:2HLZ" FT STRAND 133..139 FT /evidence="ECO:0007829|PDB:2HLZ" FT HELIX 143..157 FT /evidence="ECO:0007829|PDB:2HLZ" FT HELIX 162..164 FT /evidence="ECO:0007829|PDB:2HLZ" FT STRAND 167..172 FT /evidence="ECO:0007829|PDB:2HLZ" FT HELIX 177..184 FT /evidence="ECO:0007829|PDB:2HLZ" FT STRAND 185..191 FT /evidence="ECO:0007829|PDB:2HLZ" FT HELIX 193..198 FT /evidence="ECO:0007829|PDB:2HLZ" FT HELIX 204..211 FT /evidence="ECO:0007829|PDB:2HLZ" FT HELIX 212..214 FT /evidence="ECO:0007829|PDB:2HLZ" FT STRAND 220..224 FT /evidence="ECO:0007829|PDB:2HLZ" FT HELIX 226..228 FT /evidence="ECO:0007829|PDB:2HLZ" FT STRAND 230..233 FT /evidence="ECO:0007829|PDB:2HLZ" FT STRAND 239..242 FT /evidence="ECO:0007829|PDB:2HLZ" FT HELIX 256..269 FT /evidence="ECO:0007829|PDB:2HLZ" FT HELIX 274..289 FT /evidence="ECO:0007829|PDB:2HLZ" FT STRAND 291..294 FT /evidence="ECO:0007829|PDB:2HLZ" FT HELIX 295..297 FT /evidence="ECO:0007829|PDB:2HLZ" SQ SEQUENCE 298 AA; 32523 MW; BE77FC325CAC5721 CRC64; MEEKQILCVG LVVLDVISLV DKYPKEDSEI RCLSQRWQRG GNASNSCTVL SLLGAPCAFM GSMAPGHVAD FLVADFRRRG VDVSQVAWQS KGDTPSSCCI INNSNGNRTI VLHDTSLPDV SATDFEKVDL TQFKWIHIEG RNASEQVKML QRIDAHNTRQ PPEQKIRVSV EVEKPREELF QLFGYGDVVF VSKDVAKHLG FQSAEEALRG LYGRVRKGAV LVCAWAEEGA DALGPDGKLL HSDAFPPPRV VDTLGAGDTF NASVIFSLSQ GRSVQEALRF GCQVAGKKCG LQGFDGIV //