KHK_HUMAN
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 03-AUG-2022, entry version 201.
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}.
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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 33 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
