ID HXK3_HUMAN Reviewed; 923 AA.
AC P52790; Q8N1E7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 2.
DT 24-JAN-2024, entry version 197.
DE RecName: Full=Hexokinase-3 {ECO:0000305};
DE EC=2.7.1.1 {ECO:0000269|PubMed:8717435};
DE AltName: Full=Hexokinase type III {ECO:0000303|PubMed:8812439};
DE Short=HK III {ECO:0000303|PubMed:8812439};
DE AltName: Full=Hexokinase-C {ECO:0000250|UniProtKB:P27926};
GN Name=HK3 {ECO:0000312|HGNC:HGNC:4925};
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].
RC TISSUE=Liver;
RX PubMed=8812439; DOI=10.1006/geno.1996.0448;
RA Furuta H., Nishi S., Le Beau M.M., Fernald A.A., Yano H., Bell G.I.;
RT "Sequence of human hexokinase III cDNA and assignment of the human
RT hexokinase III gene (HK3) to chromosome band 5q35.2 by fluorescence in situ
RT hybridization.";
RL Genomics 36:206-209(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 358-923, FUNCTION, CATALYTIC ACTIVITY, AND
RP ACTIVITY REGULATION.
RC TISSUE=Liver;
RX PubMed=8717435; DOI=10.1007/bf00714329;
RA Palma F., Agostini D., Mason P., Dacha M., Piccoli G., Biagiarelli B.,
RA Fiorani M., Stocchi V.;
RT "Purification and characterization of the carboxyl-domain of human
RT hexokinase type III expressed as fusion protein.";
RL Mol. Cell. Biochem. 155:23-29(1996).
RN [5] {ECO:0007744|PDB:3HM8}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 480-922 IN COMPLEX WITH GLUCOSE.
RA Nedyalkova L., Tong Y., Rabeh W., Tempel W., Landry R., Arrowsmith C.H.,
RA Edwards A.M., Bountra C., Weigelt J., Bochkarev A., Park H.;
RT "Crystal structure of the C-terminal Hexokinase domain of human HK3.";
RL Submitted (MAY-2009) to the PDB data bank.
RN [6]
RP VARIANTS [LARGE SCALE ANALYSIS] TRP-480 AND VAL-499.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Catalyzes the phosphorylation of hexose, such as D-glucose
CC and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D-
CC fructose 6-phosphate, respectively) (PubMed:8717435). Mediates the
CC initial step of glycolysis by catalyzing phosphorylation of D-glucose
CC to D-glucose 6-phosphate (PubMed:8717435).
CC {ECO:0000269|PubMed:8717435}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-hexose = ADP + D-hexose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61567, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC Evidence={ECO:0000269|PubMed:8717435};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741;
CC Evidence={ECO:0000269|PubMed:8717435};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:16125, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:37721, ChEBI:CHEBI:61527, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC Evidence={ECO:0000250|UniProtKB:P27926};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126;
CC Evidence={ECO:0000250|UniProtKB:P27926};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC Evidence={ECO:0000269|PubMed:8717435};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826;
CC Evidence={ECO:0000269|PubMed:8717435};
CC -!- ACTIVITY REGULATION: Hexokinase is an allosteric enzyme inhibited by
CC its product D-glucose 6-phosphate. {ECO:0000269|PubMed:8717435}.
CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC {ECO:0000305|PubMed:8717435}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 1/4.
CC {ECO:0000305|PubMed:8717435}.
CC -!- INTERACTION:
CC P52790; Q92870-2: APBB2; NbExp=3; IntAct=EBI-2965780, EBI-21535880;
CC P52790; Q86V38: ATN1; NbExp=3; IntAct=EBI-2965780, EBI-11954292;
CC P52790; P48643: CCT5; NbExp=3; IntAct=EBI-2965780, EBI-355710;
CC P52790; P50570-2: DNM2; NbExp=3; IntAct=EBI-2965780, EBI-10968534;
CC P52790; P42858: HTT; NbExp=3; IntAct=EBI-2965780, EBI-466029;
CC P52790; Q92876: KLK6; NbExp=3; IntAct=EBI-2965780, EBI-2432309;
CC P52790; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2965780, EBI-16439278;
CC P52790; P60891: PRPS1; NbExp=3; IntAct=EBI-2965780, EBI-749195;
CC P52790; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-2965780, EBI-396669;
CC P52790; O76024: WFS1; NbExp=3; IntAct=EBI-2965780, EBI-720609;
CC -!- DOMAIN: The N- and C-terminal halves of this hexokinase contain a
CC hexokinase domain. The catalytic activity is associated with the C-
CC terminus while regulatory function is associated with the N-terminus.
CC {ECO:0000250|UniProtKB:P19367}.
CC -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01084, ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Hexokinase entry;
CC URL="https://en.wikipedia.org/wiki/Hexokinase";
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DR EMBL; U51333; AAC50732.1; -; mRNA.
DR EMBL; CH471195; EAW85048.1; -; Genomic_DNA.
DR EMBL; BC028129; AAH28129.1; -; mRNA.
DR EMBL; U42303; AAC50422.1; -; mRNA.
DR CCDS; CCDS4407.1; -.
DR RefSeq; NP_002106.2; NM_002115.2.
DR PDB; 3HM8; X-ray; 2.80 A; A/B/C/D=480-922.
DR PDBsum; 3HM8; -.
DR AlphaFoldDB; P52790; -.
DR SMR; P52790; -.
DR BioGRID; 109348; 35.
DR IntAct; P52790; 26.
DR MINT; P52790; -.
DR STRING; 9606.ENSP00000292432; -.
DR ChEMBL; CHEMBL2709; -.
DR iPTMnet; P52790; -.
DR PhosphoSitePlus; P52790; -.
DR SwissPalm; P52790; -.
DR BioMuta; HK3; -.
DR DMDM; 206729871; -.
DR EPD; P52790; -.
DR jPOST; P52790; -.
DR MassIVE; P52790; -.
DR MaxQB; P52790; -.
DR PaxDb; 9606-ENSP00000292432; -.
DR PeptideAtlas; P52790; -.
DR PRIDE; P52790; -.
DR ProteomicsDB; 56534; -.
DR Antibodypedia; 29158; 483 antibodies from 35 providers.
DR DNASU; 3101; -.
DR Ensembl; ENST00000292432.10; ENSP00000292432.5; ENSG00000160883.11.
DR GeneID; 3101; -.
DR KEGG; hsa:3101; -.
DR MANE-Select; ENST00000292432.10; ENSP00000292432.5; NM_002115.3; NP_002106.2.
DR UCSC; uc003mfa.4; human.
DR AGR; HGNC:4925; -.
DR CTD; 3101; -.
DR DisGeNET; 3101; -.
DR GeneCards; HK3; -.
DR HGNC; HGNC:4925; HK3.
DR HPA; ENSG00000160883; Group enriched (bone marrow, lymphoid tissue).
DR MIM; 142570; gene.
DR neXtProt; NX_P52790; -.
DR OpenTargets; ENSG00000160883; -.
DR PharmGKB; PA29303; -.
DR VEuPathDB; HostDB:ENSG00000160883; -.
DR eggNOG; KOG1369; Eukaryota.
DR GeneTree; ENSGT00950000182787; -.
DR HOGENOM; CLU_014393_1_0_1; -.
DR InParanoid; P52790; -.
DR OMA; VRPCEVG; -.
DR OrthoDB; 5481886at2759; -.
DR PhylomeDB; P52790; -.
DR TreeFam; TF314238; -.
DR BioCyc; MetaCyc:HS08548-MONOMER; -.
DR BRENDA; 2.7.1.1; 2681.
DR PathwayCommons; P52790; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-70171; Glycolysis.
DR SABIO-RK; P52790; -.
DR SignaLink; P52790; -.
DR SIGNOR; P52790; -.
DR UniPathway; UPA00109; UER00180.
DR UniPathway; UPA00242; -.
DR BioGRID-ORCS; 3101; 12 hits in 1150 CRISPR screens.
DR EvolutionaryTrace; P52790; -.
DR GeneWiki; HK3; -.
DR GenomeRNAi; 3101; -.
DR Pharos; P52790; Tbio.
DR PRO; PR:P52790; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P52790; Protein.
DR Bgee; ENSG00000160883; Expressed in monocyte and 103 other cell types or tissues.
DR ExpressionAtlas; P52790; baseline and differential.
DR Genevisible; P52790; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008865; F:fructokinase activity; ISS:UniProtKB.
DR GO; GO:0004340; F:glucokinase activity; ISS:UniProtKB.
DR GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR GO; GO:0004396; F:hexokinase activity; IDA:MGI.
DR GO; GO:0061621; P:canonical glycolysis; TAS:Reactome.
DR GO; GO:0046835; P:carbohydrate phosphorylation; IBA:GO_Central.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; ISS:UniProtKB.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; ISS:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0001678; P:intracellular glucose homeostasis; IBA:GO_Central.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 2.
DR Gene3D; 3.30.420.40; -; 2.
DR Gene3D; 3.40.367.20; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR001312; Hexokinase.
DR InterPro; IPR019807; Hexokinase_BS.
DR InterPro; IPR022673; Hexokinase_C.
DR InterPro; IPR022672; Hexokinase_N.
DR PANTHER; PTHR19443; HEXOKINASE; 1.
DR PANTHER; PTHR19443:SF1; HEXOKINASE-3; 1.
DR Pfam; PF00349; Hexokinase_1; 2.
DR Pfam; PF03727; Hexokinase_2; 2.
DR PRINTS; PR00475; HEXOKINASE.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 4.
DR PROSITE; PS00378; HEXOKINASE_1; 1.
DR PROSITE; PS51748; HEXOKINASE_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; ATP-binding; Glycolysis; Kinase;
KW Nucleotide-binding; Reference proteome; Repeat; Transferase.
FT CHAIN 1..923
FT /note="Hexokinase-3"
FT /id="PRO_0000197590"
FT DOMAIN 27..471
FT /note="Hexokinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT DOMAIN 477..912
FT /note="Hexokinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..220
FT /note="Hexokinase small subdomain 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 221..460
FT /note="Hexokinase large subdomain 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 531..661
FT /note="Hexokinase small subdomain 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 662..901
FT /note="Hexokinase large subdomain 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT BINDING 95..104
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 95..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 168
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 185..186
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 221..222
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 222
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 245
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 248
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 273
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 304..307
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 426..428
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 438..439
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 542..547
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 542..546
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 609..610
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 626..627
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:3HM8"
FT BINDING 662..663
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:3HM8"
FT BINDING 663
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 686
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 686
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 688..689
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:3HM8"
FT BINDING 714
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:3HM8"
FT BINDING 748
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:3HM8"
FT BINDING 753..754
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 790..794
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 867..869
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 869..873
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 903
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT VARIANT 281
FT /note="G -> R (in dbSNP:rs35610191)"
FT /id="VAR_034004"
FT VARIANT 480
FT /note="R -> W (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs376532514)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036186"
FT VARIANT 499
FT /note="A -> V (in a breast cancer sample; somatic mutation;
FT dbSNP:rs755546220)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036187"
FT CONFLICT 277
FT /note="F -> L (in Ref. 1; AAC50732)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="Q -> L (in Ref. 4; AAC50422)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="E -> Q (in Ref. 4; AAC50422)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="V -> I (in Ref. 4; AAC50422)"
FT /evidence="ECO:0000305"
FT CONFLICT 510
FT /note="K -> R (in Ref. 4; AAC50422)"
FT /evidence="ECO:0000305"
FT CONFLICT 512..513
FT /note="LR -> SE (in Ref. 4; AAC50422)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="A -> S (in Ref. 4; AAC50422)"
FT /evidence="ECO:0000305"
FT CONFLICT 519
FT /note="L -> S (in Ref. 4; AAC50422)"
FT /evidence="ECO:0000305"
FT CONFLICT 530..531
FT /note="PD -> LT (in Ref. 4; AAC50422)"
FT /evidence="ECO:0000305"
FT CONFLICT 577..578
FT /note="GQ -> AE (in Ref. 4; AAC50422)"
FT /evidence="ECO:0000305"
FT CONFLICT 604
FT /note="L -> T (in Ref. 4; AAC50422)"
FT /evidence="ECO:0000305"
FT CONFLICT 708
FT /note="R -> H (in Ref. 4; AAC50422)"
FT /evidence="ECO:0000305"
FT CONFLICT 718
FT /note="F -> L (in Ref. 4; AAC50422)"
FT /evidence="ECO:0000305"
FT CONFLICT 728
FT /note="S -> R (in Ref. 4; AAC50422)"
FT /evidence="ECO:0000305"
FT CONFLICT 750
FT /note="M -> I (in Ref. 4; AAC50422)"
FT /evidence="ECO:0000305"
FT CONFLICT 831
FT /note="A -> V (in Ref. 4; AAC50422)"
FT /evidence="ECO:0000305"
FT CONFLICT 836
FT /note="A -> P (in Ref. 4; AAC50422)"
FT /evidence="ECO:0000305"
FT CONFLICT 853
FT /note="E -> G (in Ref. 1; AAC50732)"
FT /evidence="ECO:0000305"
FT CONFLICT 918
FT /note="A -> T (in Ref. 4; AAC50422)"
FT /evidence="ECO:0000305"
FT HELIX 480..487
FT /evidence="ECO:0007829|PDB:3HM8"
FT HELIX 488..490
FT /evidence="ECO:0007829|PDB:3HM8"
FT HELIX 494..513
FT /evidence="ECO:0007829|PDB:3HM8"
FT STRAND 536..566
FT /evidence="ECO:0007829|PDB:3HM8"
FT HELIX 570..573
FT /evidence="ECO:0007829|PDB:3HM8"
FT HELIX 577..595
FT /evidence="ECO:0007829|PDB:3HM8"
FT STRAND 604..608
FT /evidence="ECO:0007829|PDB:3HM8"
FT HELIX 639..649
FT /evidence="ECO:0007829|PDB:3HM8"
FT STRAND 657..661
FT /evidence="ECO:0007829|PDB:3HM8"
FT HELIX 663..672
FT /evidence="ECO:0007829|PDB:3HM8"
FT STRAND 678..695
FT /evidence="ECO:0007829|PDB:3HM8"
FT HELIX 696..698
FT /evidence="ECO:0007829|PDB:3HM8"
FT STRAND 706..712
FT /evidence="ECO:0007829|PDB:3HM8"
FT HELIX 715..717
FT /evidence="ECO:0007829|PDB:3HM8"
FT TURN 718..727
FT /evidence="ECO:0007829|PDB:3HM8"
FT HELIX 730..737
FT /evidence="ECO:0007829|PDB:3HM8"
FT STRAND 739..741
FT /evidence="ECO:0007829|PDB:3HM8"
FT HELIX 748..750
FT /evidence="ECO:0007829|PDB:3HM8"
FT HELIX 753..769
FT /evidence="ECO:0007829|PDB:3HM8"
FT HELIX 774..776
FT /evidence="ECO:0007829|PDB:3HM8"
FT HELIX 780..783
FT /evidence="ECO:0007829|PDB:3HM8"
FT HELIX 790..796
FT /evidence="ECO:0007829|PDB:3HM8"
FT HELIX 803..811
FT /evidence="ECO:0007829|PDB:3HM8"
FT TURN 812..814
FT /evidence="ECO:0007829|PDB:3HM8"
FT HELIX 819..854
FT /evidence="ECO:0007829|PDB:3HM8"
FT STRAND 858..867
FT /evidence="ECO:0007829|PDB:3HM8"
FT HELIX 869..873
FT /evidence="ECO:0007829|PDB:3HM8"
FT HELIX 877..888
FT /evidence="ECO:0007829|PDB:3HM8"
FT STRAND 892..898
FT /evidence="ECO:0007829|PDB:3HM8"
FT HELIX 903..918
FT /evidence="ECO:0007829|PDB:3HM8"
SQ SEQUENCE 923 AA; 99025 MW; DA75F2A9DBB895FF CRC64;
MDSIGSSGLR QGEETLSCSE EGLPGPSDSS ELVQECLQQF KVTRAQLQQI QASLLGSMEQ
ALRGQASPAP AVRMLPTYVG STPHGTEQGD FVVLELGATG ASLRVLWVTL TGIEGHRVEP
RSQEFVIPQE VMLGAGQQLF DFAAHCLSEF LDAQPVNKQG LQLGFSFSFP CHQTGLDRST
LISWTKGFRC SGVEGQDVVQ LLRDAIRRQG AYNIDVVAVV NDTVGTMMGC EPGVRPCEVG
LVVDTGTNAC YMEEARHVAV LDEDRGRVCV SVEWGSFSDD GALGPVLTTF DHTLDHESLN
PGAQRFEKMI GGLYLGELVR LVLAHLARCG VLFGGCTSPA LLSQGSILLE HVAEMEDPST
GAARVHAILQ DLGLSPGASD VELVQHVCAA VCTRAAQLCA AALAAVLSCL QHSREQQTLQ
VAVATGGRVC ERHPRFCSVL QGTVMLLAPE CDVSLIPSVD GGGRGVAMVT AVAARLAAHR
RLLEETLAPF RLNHDQLAAV QAQMRKAMAK GLRGEASSLR MLPTFVRATP DGSERGDFLA
LDLGGTNFRV LLVRVTTGVQ ITSEIYSIPE TVAQGSGQQL FDHIVDCIVD FQQKQGLSGQ
SLPLGFTFSF PCRQLGLDQG ILLNWTKGFK ASDCEGQDVV SLLREAITRR QAVELNVVAI
VNDTVGTMMS CGYEDPRCEI GLIVGTGTNA CYMEELRNVA GVPGDSGRMC INMEWGAFGD
DGSLAMLSTR FDASVDQASI NPGKQRFEKM ISGMYLGEIV RHILLHLTSL GVLFRGQQIQ
RLQTRDIFKT KFLSEIESDS LALRQVRAIL EDLGLPLTSD DALMVLEVCQ AVSQRAAQLC
GAGVAAVVEK IRENRGLEEL AVSVGVDGTL YKLHPRFSSL VAATVRELAP RCVVTFLQSE
DGSGKGAALV TAVACRLAQL TRV
//
