ID HXK1_HUMAN Reviewed; 917 AA. AC P19367; E9PCK0; O43443; O43444; O75574; Q5VTC3; Q96HC8; Q9NNZ4; Q9NNZ5; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 3. DT 02-SEP-2026, entry version 263. DE RecName: Full=Hexokinase-1 {ECO:0000305}; DE EC=2.7.1.1 {ECO:0000269|PubMed:1637300}; DE AltName: Full=Brain form hexokinase {ECO:0000303|PubMed:8706938}; DE AltName: Full=Hexokinase type I {ECO:0000303|PubMed:9531504}; DE Short=HK I {ECO:0000303|PubMed:9531504}; DE AltName: Full=Hexokinase-A {ECO:0000250|UniProtKB:P05708}; GN Name=HK1 {ECO:0000312|HGNC:HGNC:4922}; 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] (ISOFORM 1), AND VARIANT MET-776. RX PubMed=3207429; DOI=10.1016/s0006-291x(88)80964-1; RA Nishi S., Seino S., Bell G.I.; RT "Human hexokinase: sequences of amino- and carboxyl-terminal halves are RT homologous."; RL Biochem. Biophys. Res. Commun. 157:937-943(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING. RX PubMed=9531504; DOI=10.1042/bj3310607; RA Ruzzo A., Andreoni F., Magnani M.; RT "Structure of the human hexokinase type I gene and nucleotide sequence of RT the 5' flanking region."; RL Biochem. J. 331:607-613(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; 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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-126 (ISOFORM 4), AND ALTERNATIVE SPLICING. RX PubMed=10978502; DOI=10.1016/s0167-4781(00)00147-0; RA Andreoni F., Ruzzo A., Magnani M.; RT "Structure of the 5' region of the human hexokinase type I (HKI) gene and RT identification of an additional testis-specific HKI mRNA."; RL Biochim. Biophys. Acta 1493:19-26(2000). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20 (ISOFORM 2). RA Murakami K., Piomelli S.; RT "The erythrocyte-specific hexokinase isozyme (HKR) and the common RT hexokinase isozyme (HKI) are produced from a single gene by alternate RT promoters."; RL Blood 90:272-272(1998). RN [7] RP PROTEIN SEQUENCE OF 1-20; 31-42; 382-396 AND 900-910, ACETYLATION AT MET-1, RP AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RA Bienvenut W.V., Waridel P., Quadroni M.; RL Submitted (MAR-2009) to UniProtKB. RN [8] RP PROTEIN SEQUENCE OF 11-31 AND 103-120, AND SUBCELLULAR LOCATION. RC TISSUE=Placenta; RX PubMed=1985912; DOI=10.1016/s0021-9258(18)52464-9; RA Magnani M., Serafini G., Bianchi M., Casabianca A., Stocchi V.; RT "Human hexokinase type I microheterogeneity is due to different amino- RT terminal sequences."; RL J. Biol. Chem. 266:502-505(1991). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 287-917, FUNCTION, CATALYTIC ACTIVITY, RP ACTIVITY REGULATION, AND VARIANT MET-776. RC TISSUE=Placenta; RX PubMed=1637300; DOI=10.1042/bj2850193; RA Magnani M., Bianchi M., Casabianca A., Stocchi V., Daniele A., Altruda F., RA Ferrone M., Silengo L.; RT "A recombinant human 'mini'-hexokinase is catalytically active and RT regulated by hexose 6-phosphates."; RL Biochem. J. 285:193-199(1992). RN [10] RP ALTERNATIVE SPLICING. RX PubMed=9028305; DOI=10.1182/blood.v89.3.762; RA Murakami K., Piomelli S.; RT "Identification of the cDNA for human red blood cell-specific hexokinase RT isozyme."; RL Blood 89:762-766(1997). RN [11] RP CRYSTALLIZATION. RX PubMed=8706938; DOI=10.1016/0014-5793(96)00688-6; RA Aleshin A.E., Zeng C., Fromm H.J., Honatko R.B.; RT "Crystallization and preliminary X-ray analysis of human brain RT hexokinase."; RL FEBS Lett. 391:9-10(1996). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP INVOLVEMENT IN HMSNR. RX PubMed=19536174; DOI=10.1038/ejhg.2009.99; RA Hantke J., Chandler D., King R., Wanders R.J., Angelicheva D., Tournev I., RA McNamara E., Kwa M., Guergueltcheva V., Kaneva R., Baas F., Kalaydjieva L.; RT "A mutation in an alternative untranslated exon of hexokinase 1 associated RT with hereditary motor and sensory neuropathy -- Russe (HMSNR)."; RL Eur. J. Hum. Genet. 17:1606-1614(2009). RN [14] 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 [15] RP INTERACTION WITH ATF2 AND VDAC1. RX PubMed=22304920; DOI=10.1016/j.cell.2012.01.016; RA Lau E., Kluger H., Varsano T., Lee K., Scheffler I., Rimm D.L., Ideker T., RA Ronai Z.A.; RT "PKCepsilon promotes oncogenic functions of ATF2 in the nucleus while RT blocking its apoptotic function at mitochondria."; RL Cell 148:543-555(2012). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [17] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND ACTIVITY RP REGULATION. RX PubMed=27374331; DOI=10.1016/j.cell.2016.05.076; RA Wolf A.J., Reyes C.N., Liang W., Becker C., Shimada K., Wheeler M.L., RA Cho H.C., Popescu N.I., Coggeshall K.M., Arditi M., Underhill D.M.; RT "Hexokinase is an innate immune receptor for the detection of bacterial RT peptidoglycan."; RL Cell 166:624-636(2016). RN [18] RP INTERACTION WITH SMAD5. RX PubMed=28675158; DOI=10.1038/cr.2017.85; RA Fang Y., Liu Z., Chen Z., Xu X., Xiao M., Yu Y., Zhang Y., Zhang X., Du Y., RA Jiang C., Zhao Y., Wang Y., Fan B., Terheyden-Keighley D., Liu Y., Shi L., RA Hui Y., Zhang X., Zhang B., Feng H., Ma L., Zhang Q., Jin G., Yang Y., RA Xiang B., Liu L., Zhang X.; RT "Smad5 acts as an intracellular pH messenger and maintains bioenergetic RT homeostasis."; RL Cell Res. 27:1083-1099(2017). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 16-914 IN COMPLEX WITH GLUCOSE AND RP GLUCOSE-6-PHOSPHATE, SUBUNIT, AND DOMAIN. RX PubMed=9493266; DOI=10.1016/s0969-2126(98)00006-9; RA Aleshin A.E., Zeng C., Bourenkov G.P., Bartunik H.D., Fromm H.J., RA Honzatko R.B.; RT "The mechanism of regulation of hexokinase: new insights from the crystal RT structure of recombinant human brain hexokinase complexed with glucose and RT glucose-6-phosphate."; RL Structure 6:39-50(1998). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 16-914, AND DOMAIN. RX PubMed=9735292; DOI=10.1006/jmbi.1998.2017; RA Aleshin A.E., Zeng C., Bartunik H.D., Fromm H.J., Honzatko R.B.; RT "Regulation of hexokinase I: crystal structure of recombinant human brain RT hexokinase complexed with glucose and phosphate."; RL J. Mol. Biol. 282:345-357(1998). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH AMP-PNP AND RP MAGNESIUM, SUBUNIT, AND DOMAIN. RX PubMed=10574795; DOI=10.1016/s0969-2126(00)80032-5; RA Rosano C., Sabini E., Rizzi M., Deriu D., Murshudov G., Bianchi M., RA Serafini G., Magnani M., Bolognesi M.; RT "Binding of non-catalytic ATP to human hexokinase I highlights the RT structural components for enzyme-membrane association control."; RL Structure 7:1427-1437(1999). RN [22] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GLUCOSE; RP GLUCOSE-6-PHOSPHATE AND ADP. RX PubMed=10686099; DOI=10.1006/jmbi.1999.3494; RA Aleshin A.E., Kirby C., Liu X., Bourenkov G.P., Bartunik H.D., Fromm H.J., RA Honzatko R.B.; RT "Crystal structures of mutant monomeric hexokinase I reveal multiple ADP RT binding sites and conformational changes relevant to allosteric RT regulation."; RL J. Mol. Biol. 296:1001-1015(2000). RN [23] RP VARIANT CNSHA5 SER-529. RX PubMed=7655856; DOI=10.1006/bcmd.1995.0002; RA Bianchi M., Magnani M.; RT "Hexokinase mutations that produce nonspherocytic hemolytic anemia."; RL Blood Cells Mol. Dis. 21:2-8(1995). RN [24] RP VARIANT CNSHA5 SER-680. RX PubMed=12393545; DOI=10.1182/blood-2002-06-1851; RA van Wijk R., Rijksen G., Huizinga E.G., Nieuwenhuis H.K., van Solinge W.W.; RT "HK Utrecht: missense mutation in the active site of human hexokinase RT associated with hexokinase deficiency and severe nonspherocytic hemolytic RT anemia."; RL Blood 101:345-347(2003). RN [25] RP INVOLVEMENT IN RP79, AND VARIANT RP79 LYS-847. RX PubMed=25190649; DOI=10.1167/iovs.14-15419; RA Sullivan L.S., Koboldt D.C., Bowne S.J., Lang S., Blanton S.H., Cadena E., RA Avery C.E., Lewis R.A., Webb-Jones K., Wheaton D.H., Birch D.G., Coussa R., RA Ren H., Lopez I., Chakarova C., Koenekoop R.K., Garcia C.A., Fulton R.S., RA Wilson R.K., Weinstock G.M., Daiger S.P.; RT "A dominant mutation in hexokinase 1 (HK1) causes retinitis pigmentosa."; RL Invest. Ophthalmol. Vis. Sci. 55:7147-7158(2014). RN [26] RP INVOLVEMENT IN RP79, VARIANT RP79 LYS-847, CHARACTERIZATION OF VARIANT RP79 RP LYS-847, AND FUNCTION. RX PubMed=25316723; DOI=10.1167/iovs.14-15520; RA Wang F., Wang Y., Zhang B., Zhao L., Lyubasyuk V., Wang K., Xu M., Li Y., RA Wu F., Wen C., Bernstein P.S., Lin D., Zhu S., Wang H., Zhang K., Chen R.; RT "A missense mutation in HK1 leads to autosomal dominant retinitis RT pigmentosa."; RL Invest. Ophthalmol. Vis. Sci. 55:7159-7164(2014). RN [27] RP INVOLVEMENT IN NEDVIBA, VARIANTS NEDVIBA GLU-414; GLU-418; LEU-445 AND RP MET-457, AND CHARACTERIZATION OF VARIANTS NEDVIBA GLU-418 AND LEU-445. RX PubMed=30778173; DOI=10.1038/s41431-019-0366-9; RA Okur V., Cho M.T., van Wijk R., van Oirschot B., Picker J., Coury S.A., RA Grange D., Manwaring L., Krantz I., Muraresku C.C., Hulick P.J., May H., RA Pierce E., Place E., Bujakowska K., Telegrafi A., Douglas G., RA Monaghan K.G., Begtrup A., Wilson A., Retterer K., Anyane-Yeboa K., RA Chung W.K.; RT "De novo variants in HK1 associated with neurodevelopmental abnormalities RT and visual impairment."; RL Eur. J. Hum. Genet. 27:1081-1089(2019). RN [28] RP VARIANT HMSNR 7-ARG--SER-917 DEL (ISOFORM 3). RX PubMed=34193129; DOI=10.1186/s12920-021-01019-5; RA Kanwal S., Choi Y.J., Lim S.O., Choi H.J., Park J.H., Nuzhat R., Khan A., RA Perveen S., Choi B.O., Chung K.W.; RT "Novel homozygous mutations in Pakistani families with Charcot-Marie-Tooth RT disease."; RL BMC Med. Genomics 14:174-174(2021). CC -!- FUNCTION: Catalyzes the phosphorylation of various hexoses, such as D- CC glucose, D-glucosamine, D-fructose, D-mannose and 2-deoxy-D-glucose, to CC hexose 6-phosphate (D-glucose 6-phosphate, D-glucosamine 6-phosphate, CC D-fructose 6-phosphate, D-mannose 6-phosphate and 2-deoxy-D-glucose 6- CC phosphate, respectively) (PubMed:1637300, PubMed:25316723, CC PubMed:27374331). Does not phosphorylate N-acetyl-D-glucosamine CC (PubMed:27374331). Mediates the initial step of glycolysis by CC catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate (By CC similarity). Involved in innate immunity and inflammation by acting as CC a pattern recognition receptor for bacterial peptidoglycan CC (PubMed:27374331). When released in the cytosol, N-acetyl-D-glucosamine CC component of bacterial peptidoglycan inhibits the hexokinase activity CC of HK1 and causes its dissociation from mitochondrial outer membrane, CC thereby activating the NLRP3 inflammasome (PubMed:27374331). CC {ECO:0000250|UniProtKB:P05708, ECO:0000269|PubMed:1637300, CC ECO:0000269|PubMed:25316723, ECO:0000269|PubMed:27374331}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a D-hexose + ATP = a D-hexose 6-phosphate + ADP + H(+); CC Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:229467, ChEBI:CHEBI:456216; CC EC=2.7.1.1; Evidence={ECO:0000269|PubMed:1637300, CC ECO:0000269|PubMed:27374331}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741; CC Evidence={ECO:0000269|PubMed:1637300, ECO:0000269|PubMed:27374331}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-fructose + ATP = D-fructose 6-phosphate + ADP + 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:P05708}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126; CC Evidence={ECO:0000250|UniProtKB:P05708}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glucose + ATP = D-glucose 6-phosphate + ADP + 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:0000250|UniProtKB:P05708}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826; CC Evidence={ECO:0000250|UniProtKB:P05708}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-mannose + ATP = D-mannose 6-phosphate + ADP + H(+); CC Xref=Rhea:RHEA:11028, ChEBI:CHEBI:4208, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58735, ChEBI:CHEBI:456216; EC=2.7.1.1; CC Evidence={ECO:0000250|UniProtKB:P05708}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11029; CC Evidence={ECO:0000250|UniProtKB:P05708}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glucosamine + ATP = D-glucosamine 6-phosphate + ADP + H(+); CC Xref=Rhea:RHEA:10948, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:58723, ChEBI:CHEBI:58725, ChEBI:CHEBI:456216; EC=2.7.1.1; CC Evidence={ECO:0000269|PubMed:27374331}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10949; CC Evidence={ECO:0000269|PubMed:27374331}; CC -!- ACTIVITY REGULATION: Hexokinase is an allosteric enzyme inhibited by CC its product D-glucose 6-phosphate (PubMed:1637300). Hexokinase activity CC is inhibited by N-acetyl-D-glucosamine (PubMed:27374331). CC {ECO:0000269|PubMed:1637300, ECO:0000269|PubMed:27374331}. CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism. CC {ECO:0000305|PubMed:1637300, ECO:0000305|PubMed:27374331}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 1/4. CC {ECO:0000250|UniProtKB:P05708}. CC -!- SUBUNIT: Monomer (PubMed:10686099). Interacts with RABL2/RABL2A; binds CC preferentially to GTP-bound RABL2 (By similarity). Interacts with VDAC1 CC (PubMed:22304920). The HK1-VDAC1 complex interacts with ATF2 CC (PubMed:22304920). Interacts (via N-terminal spermatogenic cell- CC specific region) with PFKM (via C-terminus) (By similarity). Interacts CC with SMAD5 (PubMed:28675158). {ECO:0000250|UniProtKB:P17710, CC ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:22304920, CC ECO:0000269|PubMed:28675158}. CC -!- INTERACTION: CC P19367; P13569: CFTR; NbExp=5; IntAct=EBI-713162, EBI-349854; CC P19367; P12931: SRC; NbExp=2; IntAct=EBI-713162, EBI-621482; CC P19367; P21796: VDAC1; NbExp=3; IntAct=EBI-713162, EBI-354158; CC P19367; P05480: Src; Xeno; NbExp=8; IntAct=EBI-713162, EBI-298680; CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane CC {ECO:0000269|PubMed:1985912, ECO:0000269|PubMed:27374331}; Peripheral CC membrane protein {ECO:0000305}. Cytoplasm, cytosol CC {ECO:0000269|PubMed:27374331}. Note=The mitochondrial-binding peptide CC (MBP) region promotes association with the mitochondrial outer membrane CC (Probable). Dissociates from the mitochondrial outer membrane following CC inhibition by N-acetyl-D-glucosamine, leading to relocation to the CC cytosol (PubMed:27374331). {ECO:0000269|PubMed:27374331, CC ECO:0000305|PubMed:1985912}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=Common; CC IsoId=P19367-1; Sequence=Displayed; CC Name=2; Synonyms=Erythrocyte, R; CC IsoId=P19367-2; Sequence=VSP_002071; CC Name=3; Synonyms=TA, TB; CC IsoId=P19367-3; Sequence=VSP_002072; CC Name=4; Synonyms=TD; CC IsoId=P19367-4; Sequence=VSP_002073; CC -!- TISSUE SPECIFICITY: Isoform 2: Erythrocyte specific (Ref.6). Isoform 3: CC Testis-specific (PubMed:10978502). Isoform 4: Testis-specific CC (PubMed:10978502). {ECO:0000269|PubMed:10978502, ECO:0000269|Ref.6}. CC -!- DOMAIN: The N- and C-terminal halves of this hexokinase contain a CC hexokinase domain (PubMed:10574795, PubMed:9493266, PubMed:9735292). CC The catalytic activity is associated with the C-terminus while CC regulatory function is associated with the N-terminus (PubMed:10574795, CC PubMed:9493266, PubMed:9735292). Each domain can bind a single D- CC glucose and D-glucose 6-phosphate molecule (PubMed:9493266). CC {ECO:0000269|PubMed:10574795, ECO:0000269|PubMed:9493266, CC ECO:0000269|PubMed:9735292}. CC -!- DISEASE: Anemia, congenital, non-spherocytic hemolytic, 5 (CNSHA5) CC [MIM:235700]: An autosomal recessive disorder characterized by CC hemolytic anemia as the predominant clinical feature, and decreased red CC cell hexokinase activity. {ECO:0000269|PubMed:12393545, CC ECO:0000269|PubMed:7655856}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Neuropathy, hereditary motor and sensory, Russe type (HMSNR) CC [MIM:605285]: An autosomal recessive progressive complex peripheral CC neuropathy characterized by onset in the first decade of distal lower CC limb weakness and muscle atrophy resulting in walking difficulties. CC Distal impairment of the upper limbs usually occurs later, as does CC proximal lower limb weakness. There is distal sensory impairment, with CC pes cavus and areflexia. Laboratory studies suggest that it is a CC myelinopathy resulting in reduced nerve conduction velocities in the CC demyelinating range as well as a length-dependent axonopathy. CC {ECO:0000269|PubMed:19536174, ECO:0000269|PubMed:34193129}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Retinitis pigmentosa 79 (RP79) [MIM:617460]: A form of CC retinitis pigmentosa, a retinal dystrophy belonging to the group of CC pigmentary retinopathies. Retinitis pigmentosa is characterized by CC retinal pigment deposits visible on fundus examination and primary loss CC of rod photoreceptor cells followed by secondary loss of cone CC photoreceptors. Patients typically have night vision blindness and loss CC of midperipheral visual field. As their condition progresses, they lose CC their far peripheral visual field and eventually central vision as CC well. RP79 inheritance is autosomal dominant. CC {ECO:0000269|PubMed:25190649, ECO:0000269|PubMed:25316723}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Neurodevelopmental disorder with visual defects and brain CC anomalies (NEDVIBA) [MIM:618547]: A disorder characterized by global CC developmental delay, speech delay, intellectual disability, structural CC brain abnormalities, and visual impairments including retinitis CC pigmentosa and optic atrophy. {ECO:0000269|PubMed:30778173}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE- CC ProRule:PRU01084, ECO:0000305}. CC -!- CAUTION: Hexokinase is known to act as a monomer (PubMed:10686099). It CC however homodimerizes at elevated protein concentrations used for CC crystallizations (PubMed:10574795, PubMed:9493266). CC {ECO:0000269|PubMed:10574795, ECO:0000269|PubMed:10686099, CC ECO:0000269|PubMed:9493266}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Hexokinase entry; CC URL="https://en.wikipedia.org/wiki/Hexokinase"; 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; M75126; AAA52646.1; -; mRNA. DR EMBL; AF016365; AAC15862.1; -; Genomic_DNA. DR EMBL; AF016349; AAC15862.1; JOINED; Genomic_DNA. DR EMBL; AF016351; AAC15862.1; JOINED; Genomic_DNA. DR EMBL; AF016352; AAC15862.1; JOINED; Genomic_DNA. DR EMBL; AF016353; AAC15862.1; JOINED; Genomic_DNA. DR EMBL; AF016354; AAC15862.1; JOINED; Genomic_DNA. DR EMBL; AF016355; AAC15862.1; JOINED; Genomic_DNA. DR EMBL; AF016356; AAC15862.1; JOINED; Genomic_DNA. DR EMBL; AF016357; AAC15862.1; JOINED; Genomic_DNA. DR EMBL; AF016358; AAC15862.1; JOINED; Genomic_DNA. DR EMBL; AF016359; AAC15862.1; JOINED; Genomic_DNA. DR EMBL; AF016360; AAC15862.1; JOINED; Genomic_DNA. DR EMBL; AF016361; AAC15862.1; JOINED; Genomic_DNA. DR EMBL; AF016362; AAC15862.1; JOINED; Genomic_DNA. DR EMBL; AF016363; AAC15862.1; JOINED; Genomic_DNA. DR EMBL; AF016364; AAC15862.1; JOINED; Genomic_DNA. DR EMBL; AF016365; AAC15863.1; -; Genomic_DNA. DR EMBL; AF016349; AAC15863.1; JOINED; Genomic_DNA. DR EMBL; AF016351; AAC15863.1; JOINED; Genomic_DNA. DR EMBL; AF016352; AAC15863.1; JOINED; Genomic_DNA. DR EMBL; AF016353; AAC15863.1; JOINED; Genomic_DNA. DR EMBL; AF016354; AAC15863.1; JOINED; Genomic_DNA. DR EMBL; AF016355; AAC15863.1; JOINED; Genomic_DNA. DR EMBL; AF016356; AAC15863.1; JOINED; Genomic_DNA. DR EMBL; AF016357; AAC15863.1; JOINED; Genomic_DNA. DR EMBL; AF016358; AAC15863.1; JOINED; Genomic_DNA. DR EMBL; AF016359; AAC15863.1; JOINED; Genomic_DNA. DR EMBL; AF016360; AAC15863.1; JOINED; Genomic_DNA. DR EMBL; AF016361; AAC15863.1; JOINED; Genomic_DNA. DR EMBL; AF016362; AAC15863.1; JOINED; Genomic_DNA. DR EMBL; AF016363; AAC15863.1; JOINED; Genomic_DNA. DR EMBL; AF016364; AAC15863.1; JOINED; Genomic_DNA. DR EMBL; AF016365; AAF82319.1; -; Genomic_DNA. DR EMBL; AF163910; AAF82319.1; JOINED; Genomic_DNA. DR EMBL; AF163911; AAF82319.1; JOINED; Genomic_DNA. DR EMBL; AF016351; AAF82319.1; JOINED; Genomic_DNA. DR EMBL; AF016352; AAF82319.1; JOINED; Genomic_DNA. DR EMBL; AF016353; AAF82319.1; JOINED; Genomic_DNA. DR EMBL; AF016354; AAF82319.1; JOINED; Genomic_DNA. DR EMBL; AF016355; AAF82319.1; JOINED; Genomic_DNA. DR EMBL; AF016356; AAF82319.1; JOINED; Genomic_DNA. DR EMBL; AF016357; AAF82319.1; JOINED; Genomic_DNA. DR EMBL; AF016358; AAF82319.1; JOINED; Genomic_DNA. DR EMBL; AF016359; AAF82319.1; JOINED; Genomic_DNA. DR EMBL; AF016360; AAF82319.1; JOINED; Genomic_DNA. DR EMBL; AF016361; AAF82319.1; JOINED; Genomic_DNA. DR EMBL; AF016362; AAF82319.1; JOINED; Genomic_DNA. DR EMBL; AF016363; AAF82319.1; JOINED; Genomic_DNA. DR EMBL; AF016364; AAF82319.1; JOINED; Genomic_DNA. DR EMBL; AF016365; AAF82320.1; -; Genomic_DNA. DR EMBL; AF163912; AAF82320.1; JOINED; Genomic_DNA. DR EMBL; AF016351; AAF82320.1; JOINED; Genomic_DNA. DR EMBL; AF016352; AAF82320.1; JOINED; Genomic_DNA. DR EMBL; AF016353; AAF82320.1; JOINED; Genomic_DNA. DR EMBL; AF016354; AAF82320.1; JOINED; Genomic_DNA. DR EMBL; AF016355; AAF82320.1; JOINED; Genomic_DNA. DR EMBL; AF016356; AAF82320.1; JOINED; Genomic_DNA. DR EMBL; AF016357; AAF82320.1; JOINED; Genomic_DNA. DR EMBL; AF016358; AAF82320.1; JOINED; Genomic_DNA. DR EMBL; AF016359; AAF82320.1; JOINED; Genomic_DNA. DR EMBL; AF016360; AAF82320.1; JOINED; Genomic_DNA. DR EMBL; AF016361; AAF82320.1; JOINED; Genomic_DNA. DR EMBL; AF016362; AAF82320.1; JOINED; Genomic_DNA. DR EMBL; AF016363; AAF82320.1; JOINED; Genomic_DNA. DR EMBL; AF016364; AAF82320.1; JOINED; Genomic_DNA. DR EMBL; AC016821; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL596223; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL672126; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC008730; AAH08730.1; -; mRNA. DR EMBL; AF073786; AAC25424.1; -; mRNA. DR EMBL; AF029306; AAC00172.1; -; Genomic_DNA. DR EMBL; X66957; CAA47379.1; -; mRNA. DR CCDS; CCDS7289.1; -. [P19367-3] DR CCDS; CCDS7291.1; -. [P19367-2] DR CCDS; CCDS7292.1; -. [P19367-1] DR PIR; A31869; A31869. DR RefSeq; NP_000179.2; NM_000188.3. [P19367-1] DR RefSeq; NP_001309293.1; NM_001322364.2. [P19367-3] DR RefSeq; NP_001345192.1; NM_001358263.1. [P19367-3] DR RefSeq; NP_277031.1; NM_033496.3. [P19367-2] DR RefSeq; NP_277032.1; NM_033497.3. [P19367-3] DR RefSeq; NP_277033.1; NM_033498.3. [P19367-3] DR RefSeq; NP_277035.2; NM_033500.2. [P19367-4] DR RefSeq; XP_024303737.1; XM_024447969.2. [P19367-3] DR RefSeq; XP_047281092.1; XM_047425136.1. [P19367-3] DR RefSeq; XP_047281093.1; XM_047425137.1. [P19367-3] DR RefSeq; XP_054221661.1; XM_054365686.1. [P19367-3] DR RefSeq; XP_054221662.1; XM_054365687.1. [P19367-3] DR RefSeq; XP_054221663.1; XM_054365688.1. [P19367-3] DR PDB; 1CZA; X-ray; 1.90 A; N=1-917. DR PDB; 1DGK; X-ray; 2.80 A; N=1-917. DR PDB; 1HKB; X-ray; 2.80 A; A/B=1-917. DR PDB; 1HKC; X-ray; 2.80 A; A=1-917. DR PDB; 1QHA; X-ray; 2.25 A; A/B=1-917. DR PDB; 4F9O; X-ray; 2.65 A; A/B=1-914. DR PDB; 4FOE; X-ray; 2.70 A; A/B=1-917. DR PDB; 4FOI; X-ray; 2.40 A; A/B=1-917. DR PDB; 4FPA; X-ray; 2.48 A; A/B=1-917. DR PDB; 4FPB; X-ray; 3.00 A; A/B=1-917. DR AlphaFoldDB; P19367; -. DR SMR; P19367; -. DR BioGRID; 109345; 241. DR CORUM; P19367; -. DR DIP; DIP-56245N; -. DR FunCoup; P19367; 1667. DR IntAct; P19367; 105. DR MINT; P19367; -. DR NDEx; IQUERY-CP-HK1; 15 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000494664; -. DR BindingDB; P19367; -. DR ChEMBL; CHEMBL2688; -. DR DrugBank; DB02007; alpha-D-glucose 6-phosphate. DR DrugBank; DB02379; Beta-D-Glucose. DR DrugBank; DB01914; D-glucose. DR DrugBank; DB09341; Dextrose, unspecified form. DR DrugBank; DB09502; Fludeoxyglucose (18F). DR DrugBank; DB06266; Lonidamine. DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester. DR CarbonylDB; P19367; -. DR GlyGen; P19367; 3 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (2 sites). DR iPTMnet; P19367; -. DR MetOSite; P19367; -. DR PhosphoSitePlus; P19367; -. DR SwissPalm; P19367; -. DR BioMuta; HK1; -. DR DMDM; 116242516; -. DR CPTAC; CPTAC-80; -. DR CPTAC; CPTAC-81; -. DR jPOST; P19367; -. DR MassIVE; P19367; -. DR PaxDb; 9606-ENSP00000494664; -. DR PeptideAtlas; P19367; -. DR PRIDE; P19367; -. DR ProteomicsDB; 53648; -. [P19367-1] DR ProteomicsDB; 53649; -. [P19367-2] DR ProteomicsDB; 53650; -. [P19367-3] DR ProteomicsDB; 53651; -. [P19367-4] DR Pumba; P19367; -. DR Antibodypedia; 2057; 888 antibodies from 45 providers. DR DNASU; 3098; -. DR Ensembl; ENST00000298649.8; ENSP00000298649.3; ENSG00000156515.26. [P19367-2] DR Ensembl; ENST00000359426.7; ENSP00000352398.6; ENSG00000156515.26. [P19367-1] DR Ensembl; ENST00000436817.6; ENSP00000415949.2; ENSG00000156515.26. [P19367-3] DR Ensembl; ENST00000643399.2; ENSP00000494664.1; ENSG00000156515.26. [P19367-3] DR GeneID; 3098; -. DR KEGG; hsa:3098; -. DR MANE-Select; ENST00000359426.7; ENSP00000352398.6; NM_000188.3; NP_000179.2. DR UCSC; uc001jpg.5; human. [P19367-1] DR AGR; HGNC:4922; -. DR ClinPGx; PA29300; -. DR CTD; 3098; -. DR DisGeNET; 3098; -. DR GeneCards; HK1; -. DR HGNC; HGNC:4922; HK1. DR HPA; ENSG00000156515; Low tissue specificity. DR MalaCards; HK1; -. DR MIM; 142600; gene. DR MIM; 235700; phenotype. DR MIM; 605285; phenotype. DR MIM; 617460; phenotype. DR MIM; 618547; phenotype. DR OpenTargets; ENSG00000156515; -. DR Orphanet; 99953; Charcot-Marie-Tooth disease type 4G. DR Orphanet; 90031; Non-spherocytic hemolytic anemia due to hexokinase deficiency. DR VEuPathDB; HostDB:ENSG00000156515; -. DR eggNOG; KOG1369; Eukaryota. DR GeneTree; ENSGT00950000182787; -. DR HOGENOM; CLU_014393_1_0_1; -. DR InParanoid; P19367; -. DR OMA; XGILITW; -. DR OrthoDB; 419537at2759; -. DR PAN-GO; P19367; 9 GO annotations based on evolutionary models. DR PhylomeDB; P19367; -. DR BioCyc; MetaCyc:HS08136-MONOMER; -. DR BRENDA; 2.7.1.1; 2681. DR PathwayCommons; P19367; -. DR Reactome; R-HSA-446205; Synthesis of GDP-mannose. DR Reactome; R-HSA-5619056; Defective HK1 causes hexokinase deficiency (HK deficiency). DR Reactome; R-HSA-70171; Glycolysis. DR SABIO-RK; P19367; -. DR SignaLink; P19367; -. DR SIGNOR; P19367; -. DR UniPathway; UPA00109; UER00180. DR UniPathway; UPA00242; -. DR Agora; ENSG00000156515; -. DR BioGRID-ORCS; 3098; 16 hits in 1175 CRISPR screens. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; HK1; human. DR EvolutionaryTrace; P19367; -. DR GenomeRNAi; 3098; -. DR Pharos; P19367; Tchem. DR PRO; PR:P19367; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; P19367; protein. DR Bgee; ENSG00000156515; Expressed in cerebellar vermis and 205 other cell types or tissues. DR ExpressionAtlas; P19367; baseline and differential. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0045121; C:membrane raft; IEA:Ensembl. DR GO; GO:0005741; C:mitochondrial outer membrane; EXP:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0005536; F:D-glucose binding; IEA:InterPro. DR GO; GO:0008865; F:fructokinase activity; ISS:UniProtKB. DR GO; GO:0004340; F:glucokinase activity; ISS:UniProtKB. DR GO; GO:0047931; F:glucosamine kinase activity; EXP:UniProtKB. DR GO; GO:0004396; F:hexokinase activity; IMP:CAFA. DR GO; GO:0019158; F:mannokinase activity; EXP:Reactome. DR GO; GO:0042834; F:peptidoglycan binding; IDA:CAFA. DR GO; GO:0061621; P:canonical glycolysis; TAS:Reactome. DR GO; GO:0046835; P:carbohydrate phosphorylation; IMP:CAFA. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; ISS:UniProtKB. DR GO; GO:0009298; P:GDP-mannose biosynthetic process; TAS:Reactome. 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; IEA:InterPro. DR GO; GO:0072656; P:maintenance of protein location in mitochondrion; IMP:ParkinsonsUK-UCL. DR GO; GO:0006013; P:mannose metabolic process; ISS:UniProtKB. DR GO; GO:0002720; P:positive regulation of cytokine production involved in immune response; IEA:Ensembl. DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IEA:Ensembl. DR GO; GO:0070585; P:protein localization to mitochondrion; IMP:ParkinsonsUK-UCL. DR CDD; cd24124; ASKHA_NBD_HK1_meta_rpt1; 1. DR CDD; cd24127; ASKHA_NBD_HK1_meta_rpt2; 1. DR FunFam; 3.30.420.40:FF:000015; Hexokinase 1; 1. DR FunFam; 3.40.367.20:FF:000001; Hexokinase 1; 1. DR FunFam; 3.30.420.40:FF:000555; Hexokinase-1; 1. DR FunFam; 3.40.367.20:FF:000020; Hexokinase-1; 1. 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:SF10; HEXOKINASE-1; 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; 2. DR PROSITE; PS51748; HEXOKINASE_2; 2. DR PDBsum; 1CZA; -. DR PDBsum; 1DGK; -. DR PDBsum; 1HKB; -. DR PDBsum; 1HKC; -. DR PDBsum; 1QHA; -. DR PDBsum; 4F9O; -. DR PDBsum; 4FOE; -. DR PDBsum; 4FOI; -. DR PDBsum; 4FPA; -. DR PDBsum; 4FPB; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Allosteric enzyme; Alternative splicing; KW ATP-binding; Charcot-Marie-Tooth disease; Cytoplasm; KW Direct protein sequencing; Disease variant; Glycolysis; KW Hereditary hemolytic anemia; Immunity; Inflammatory response; KW Innate immunity; Intellectual disability; Kinase; Membrane; Mitochondrion; KW Mitochondrion outer membrane; Neurodegeneration; Neuropathy; KW Nucleotide-binding; Phosphoprotein; Proteomics identification; KW Reference proteome; Repeat; Retinitis pigmentosa; Transferase. FT CHAIN 1..917 FT /note="Hexokinase-1" FT /id="PRO_0000197585" FT DOMAIN 16..458 FT /note="Hexokinase 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084" FT DOMAIN 464..906 FT /note="Hexokinase 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084" FT REGION 1..10 FT /note="Mitochondrial-binding peptide (MBP)" FT /evidence="ECO:0000305|PubMed:1985912" FT REGION 73..207 FT /note="Hexokinase small subdomain 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084" FT REGION 208..447 FT /note="Hexokinase large subdomain 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084" FT REGION 521..655 FT /note="Hexokinase small subdomain 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084" FT REGION 656..895 FT /note="Hexokinase large subdomain 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084" FT BINDING 30 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:10574795, FT ECO:0000269|PubMed:10686099, ECO:0007744|PDB:1CZA, FT ECO:0007744|PDB:1DGK, ECO:0007744|PDB:1QHA" FT BINDING 84..91 FT /ligand="D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61548" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:10574795, FT ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:9493266, FT ECO:0007744|PDB:1CZA, ECO:0007744|PDB:1HKB, FT ECO:0007744|PDB:1QHA, ECO:0007744|PDB:4FOE, FT ECO:0007744|PDB:4FOI, ECO:0007744|PDB:4FPA" FT BINDING 84..89 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:10686099, FT ECO:0000269|PubMed:9735292, ECO:0007744|PDB:1DGK, FT ECO:0007744|PDB:1HKC" FT BINDING 155 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:10686099, FT ECO:0000269|PubMed:9493266, ECO:0000269|PubMed:9735292, FT ECO:0007744|PDB:1DGK, ECO:0007744|PDB:1HKB, FT ECO:0007744|PDB:1HKC, ECO:0007744|PDB:4F9O, FT ECO:0007744|PDB:4FOE, ECO:0007744|PDB:4FOI, FT ECO:0007744|PDB:4FPA" FT BINDING 172..173 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:10574795, FT ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:9493266, FT ECO:0000269|PubMed:9735292, ECO:0007744|PDB:1CZA, FT ECO:0007744|PDB:1DGK, ECO:0007744|PDB:1HKB, FT ECO:0007744|PDB:1HKC, ECO:0007744|PDB:1QHA, FT ECO:0007744|PDB:4F9O, ECO:0007744|PDB:4FOE, FT ECO:0007744|PDB:4FOI, ECO:0007744|PDB:4FPA, FT ECO:0007744|PDB:4FPB" FT BINDING 208..209 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:10574795, FT ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:9493266, FT ECO:0000269|PubMed:9735292, ECO:0007744|PDB:1CZA, FT ECO:0007744|PDB:1DGK, ECO:0007744|PDB:1HKB, FT ECO:0007744|PDB:1HKC, ECO:0007744|PDB:1QHA, FT ECO:0007744|PDB:4F9O, ECO:0007744|PDB:4FOE, FT ECO:0007744|PDB:4FOI, ECO:0007744|PDB:4FPA, FT ECO:0007744|PDB:4FPB" FT BINDING 209 FT /ligand="D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61548" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:10574795, FT ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:9493266, FT ECO:0007744|PDB:1CZA, ECO:0007744|PDB:1HKB, FT ECO:0007744|PDB:1QHA, ECO:0007744|PDB:4FOE, FT ECO:0007744|PDB:4FOI, ECO:0007744|PDB:4FPA" FT BINDING 232 FT /ligand="D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61548" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:10574795, FT ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:9493266, FT ECO:0007744|PDB:1CZA, ECO:0007744|PDB:1HKB, FT ECO:0007744|PDB:1QHA, ECO:0007744|PDB:4F9O, FT ECO:0007744|PDB:4FOE, ECO:0007744|PDB:4FOI, FT ECO:0007744|PDB:4FPA, ECO:0007744|PDB:4FPB" FT BINDING 235 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:10574795, FT ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:9493266, FT ECO:0000269|PubMed:9735292, ECO:0007744|PDB:1CZA, FT ECO:0007744|PDB:1DGK, ECO:0007744|PDB:1HKB, FT ECO:0007744|PDB:1HKC, ECO:0007744|PDB:1QHA, FT ECO:0007744|PDB:4F9O, ECO:0007744|PDB:4FOE, FT ECO:0007744|PDB:4FOI, ECO:0007744|PDB:4FPA, FT ECO:0007744|PDB:4FPB" FT BINDING 260 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:10574795, FT ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:9493266, FT ECO:0000269|PubMed:9735292, ECO:0007744|PDB:1CZA, FT ECO:0007744|PDB:1DGK, ECO:0007744|PDB:1HKB, FT ECO:0007744|PDB:1HKC, ECO:0007744|PDB:1QHA, FT ECO:0007744|PDB:4F9O, ECO:0007744|PDB:4FOE, FT ECO:0007744|PDB:4FOI, ECO:0007744|PDB:4FPA, FT ECO:0007744|PDB:4FPB" FT BINDING 291..294 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:10574795, FT ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:9493266, FT ECO:0000269|PubMed:9735292, ECO:0007744|PDB:1CZA, FT ECO:0007744|PDB:1DGK, ECO:0007744|PDB:1HKB, FT ECO:0007744|PDB:1HKC, ECO:0007744|PDB:1QHA, FT ECO:0007744|PDB:4F9O, ECO:0007744|PDB:4FOE, FT ECO:0007744|PDB:4FOI, ECO:0007744|PDB:4FPA, FT ECO:0007744|PDB:4FPB" FT BINDING 345 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:10574795, FT ECO:0007744|PDB:1QHA" FT BINDING 413..415 FT /ligand="D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61548" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:10574795, FT ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:9493266, FT ECO:0007744|PDB:1CZA, ECO:0007744|PDB:1HKB, FT ECO:0007744|PDB:1QHA, ECO:0007744|PDB:4F9O, FT ECO:0007744|PDB:4FOE, ECO:0007744|PDB:4FOI, FT ECO:0007744|PDB:4FPA, ECO:0007744|PDB:4FPB" FT BINDING 425..426 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:10574795, FT ECO:0000269|PubMed:10686099, ECO:0007744|PDB:1CZA, FT ECO:0007744|PDB:1DGK, ECO:0007744|PDB:1QHA" FT BINDING 449 FT /ligand="D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61548" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:10574795, FT ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:9493266, FT ECO:0007744|PDB:1CZA, ECO:0007744|PDB:1HKB, FT ECO:0007744|PDB:1QHA, ECO:0007744|PDB:4F9O, FT ECO:0007744|PDB:4FOE, ECO:0007744|PDB:4FOI, FT ECO:0007744|PDB:4FPA, ECO:0007744|PDB:4FPB" FT BINDING 532..537 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:10686099, FT ECO:0007744|PDB:1DGK" FT BINDING 532..536 FT /ligand="D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61548" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:10574795, FT ECO:0000269|PubMed:10686099, ECO:0007744|PDB:1CZA, FT ECO:0007744|PDB:1QHA, ECO:0007744|PDB:4FOE, FT ECO:0007744|PDB:4FOI, ECO:0007744|PDB:4FPA" FT BINDING 603..604 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:10686099, FT ECO:0000269|PubMed:9493266, ECO:0007744|PDB:1DGK, FT ECO:0007744|PDB:1HKB, ECO:0007744|PDB:4F9O, FT ECO:0007744|PDB:4FOE, ECO:0007744|PDB:4FOI, FT ECO:0007744|PDB:4FPA, ECO:0007744|PDB:4FPB" FT BINDING 620..621 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:10574795, FT ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:9493266, FT ECO:0007744|PDB:1CZA, ECO:0007744|PDB:1DGK, FT ECO:0007744|PDB:1HKB, ECO:0007744|PDB:1QHA, FT ECO:0007744|PDB:4F9O, ECO:0007744|PDB:4FOE, FT ECO:0007744|PDB:4FOI, ECO:0007744|PDB:4FPA, FT ECO:0007744|PDB:4FPB" FT BINDING 656..657 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:10574795, FT ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:9493266, FT ECO:0007744|PDB:1CZA, ECO:0007744|PDB:1DGK, FT ECO:0007744|PDB:1HKB, ECO:0007744|PDB:1QHA, FT ECO:0007744|PDB:4F9O, ECO:0007744|PDB:4FOE, FT ECO:0007744|PDB:4FOI, ECO:0007744|PDB:4FPA, FT ECO:0007744|PDB:4FPB" FT BINDING 657 FT /ligand="D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61548" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:10574795, FT ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:9493266, FT ECO:0007744|PDB:1CZA, ECO:0007744|PDB:1HKB, FT ECO:0007744|PDB:1QHA, ECO:0007744|PDB:4FOI, FT ECO:0007744|PDB:4FPA" FT BINDING 680 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:10686099, FT ECO:0000269|PubMed:9735292, ECO:0007744|PDB:1DGK, FT ECO:0007744|PDB:1HKC" FT BINDING 680 FT /ligand="D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61548" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:10574795, FT ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:9493266, FT ECO:0007744|PDB:1CZA, ECO:0007744|PDB:1HKB, FT ECO:0007744|PDB:1QHA, ECO:0007744|PDB:4F9O, FT ECO:0007744|PDB:4FOE, ECO:0007744|PDB:4FOI, FT ECO:0007744|PDB:4FPA, ECO:0007744|PDB:4FPB" FT BINDING 682..683 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:10574795, FT ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:9493266, FT ECO:0007744|PDB:1CZA, ECO:0007744|PDB:1DGK, FT ECO:0007744|PDB:1HKB, ECO:0007744|PDB:1QHA, FT ECO:0007744|PDB:4F9O, ECO:0007744|PDB:4FOE, FT ECO:0007744|PDB:4FOI, ECO:0007744|PDB:4FPA, FT ECO:0007744|PDB:4FPB" FT BINDING 708 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:10574795, FT ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:9493266, FT ECO:0007744|PDB:1CZA, ECO:0007744|PDB:1DGK, FT ECO:0007744|PDB:1HKB, ECO:0007744|PDB:1QHA, FT ECO:0007744|PDB:4F9O, ECO:0007744|PDB:4FOE, FT ECO:0007744|PDB:4FOI, ECO:0007744|PDB:4FPA, FT ECO:0007744|PDB:4FPB" FT BINDING 742 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:10574795, FT ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:9493266, FT ECO:0007744|PDB:1CZA, ECO:0007744|PDB:1DGK, FT ECO:0007744|PDB:1HKB, ECO:0007744|PDB:1QHA, FT ECO:0007744|PDB:4F9O, ECO:0007744|PDB:4FOE, FT ECO:0007744|PDB:4FOI, ECO:0007744|PDB:4FPA, FT ECO:0007744|PDB:4FPB" FT BINDING 747..748 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:10686099, FT ECO:0007744|PDB:1DGK" FT BINDING 784..788 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:10686099, FT ECO:0007744|PDB:1DGK" FT BINDING 861..863 FT /ligand="D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61548" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:10574795, FT ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:9493266, FT ECO:0007744|PDB:1CZA, ECO:0007744|PDB:1HKB, FT ECO:0007744|PDB:1QHA, ECO:0007744|PDB:4F9O, FT ECO:0007744|PDB:4FOE, ECO:0007744|PDB:4FOI, FT ECO:0007744|PDB:4FPA, ECO:0007744|PDB:4FPB" FT BINDING 863..867 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:10686099, FT ECO:0000269|PubMed:9735292, ECO:0007744|PDB:1DGK, FT ECO:0007744|PDB:1HKC" FT BINDING 897 FT /ligand="D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61548" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:10574795, FT ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:9493266, FT ECO:0007744|PDB:1CZA, ECO:0007744|PDB:1HKB, FT ECO:0007744|PDB:1QHA, ECO:0007744|PDB:4F9O, FT ECO:0007744|PDB:4FOI, ECO:0007744|PDB:4FPA, FT ECO:0007744|PDB:4FPB" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:25944712" FT MOD_RES 337 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P05708" FT VAR_SEQ 1..21 FT /note="MIAAQLLAYYFTELKDDQVKK -> MDCEHSLSLPCRGAEAWEIG (in FT isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_002071" FT VAR_SEQ 1..21 FT /note="MIAAQLLAYYFTELKDDQVKK -> MGQICQRESATAAEKPKLHLLAESE FT (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_002072" FT VAR_SEQ 1..21 FT /note="MIAAQLLAYYFTELKDDQVKK -> MAKRALHDF (in isoform 4)" FT /evidence="ECO:0000303|PubMed:10978502" FT /id="VSP_002073" FT VARIANT 414 FT /note="G -> E (in NEDVIBA; dbSNP:rs1064795154)" FT /evidence="ECO:0000269|PubMed:30778173" FT /id="VAR_083222" FT VARIANT 418 FT /note="K -> E (in NEDVIBA; no effect on the affinity for FT glucose or ATP; no effect on thermal stability; FT dbSNP:rs1564557037)" FT /evidence="ECO:0000269|PubMed:30778173" FT /id="VAR_083223" FT VARIANT 445 FT /note="S -> L (in NEDVIBA; no effect on the affinity for FT glucose or ATP; no effect on thermal stability; FT dbSNP:rs1064794848)" FT /evidence="ECO:0000269|PubMed:30778173" FT /id="VAR_083224" FT VARIANT 457 FT /note="T -> M (in NEDVIBA; dbSNP:rs1057517928)" FT /evidence="ECO:0000269|PubMed:30778173" FT /id="VAR_083225" FT VARIANT 529 FT /note="L -> S (in CNSHA5; dbSNP:rs137853249)" FT /evidence="ECO:0000269|PubMed:7655856" FT /id="VAR_009878" FT VARIANT 680 FT /note="T -> S (in CNSHA5; HKUtrecht; dbSNP:rs398122379)" FT /evidence="ECO:0000269|PubMed:12393545" FT /id="VAR_023780" FT VARIANT 776 FT /note="L -> M (in dbSNP:rs1054203)" FT /evidence="ECO:0000269|PubMed:1637300, FT ECO:0000269|PubMed:3207429" FT /id="VAR_023781" FT VARIANT 847 FT /note="E -> K (in RP79; uncertain significance; no effect FT on hexokinase activity; no effect on protein abundance; FT dbSNP:rs777849213)" FT /evidence="ECO:0000269|PubMed:25190649, FT ECO:0000269|PubMed:25316723" FT /id="VAR_078923" FT CONFLICT 730 FT /note="D -> N (in Ref. 1; AAA52646 and 9; CAA47379)" FT /evidence="ECO:0000305" FT HELIX 14..16 FT /evidence="ECO:0007829|PDB:1QHA" FT HELIX 17..25 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 27..29 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 33..51 FT /evidence="ECO:0007829|PDB:1CZA" FT TURN 53..55 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 56..58 FT /evidence="ECO:0007829|PDB:1CZA" FT STRAND 78..100 FT /evidence="ECO:0007829|PDB:1CZA" FT STRAND 103..112 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 116..119 FT /evidence="ECO:0007829|PDB:1CZA" FT STRAND 120..122 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 123..141 FT /evidence="ECO:0007829|PDB:1CZA" FT STRAND 144..146 FT /evidence="ECO:0007829|PDB:4FOI" FT STRAND 150..154 FT /evidence="ECO:0007829|PDB:1CZA" FT STRAND 161..164 FT /evidence="ECO:0007829|PDB:4FPB" FT TURN 179..182 FT /evidence="ECO:0007829|PDB:4FPA" FT HELIX 185..196 FT /evidence="ECO:0007829|PDB:1CZA" FT STRAND 203..207 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 209..220 FT /evidence="ECO:0007829|PDB:1CZA" FT STRAND 224..241 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 242..244 FT /evidence="ECO:0007829|PDB:1CZA" FT STRAND 252..258 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 261..263 FT /evidence="ECO:0007829|PDB:1CZA" FT TURN 264..273 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 276..283 FT /evidence="ECO:0007829|PDB:1CZA" FT STRAND 285..287 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 294..297 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 299..315 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 320..322 FT /evidence="ECO:0007829|PDB:1CZA" FT TURN 326..329 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 336..342 FT /evidence="ECO:0007829|PDB:1CZA" FT TURN 345..347 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 348..358 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 365..401 FT /evidence="ECO:0007829|PDB:1CZA" FT STRAND 404..413 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 415..419 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 423..434 FT /evidence="ECO:0007829|PDB:1CZA" FT STRAND 438..444 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 449..475 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 481..499 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 501..504 FT /evidence="ECO:0007829|PDB:1CZA" FT STRAND 526..546 FT /evidence="ECO:0007829|PDB:1CZA" FT STRAND 548..550 FT /evidence="ECO:0007829|PDB:1QHA" FT STRAND 552..560 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 564..567 FT /evidence="ECO:0007829|PDB:1CZA" FT STRAND 568..570 FT /evidence="ECO:0007829|PDB:4F9O" FT HELIX 571..589 FT /evidence="ECO:0007829|PDB:1CZA" FT STRAND 597..602 FT /evidence="ECO:0007829|PDB:1CZA" FT STRAND 606..610 FT /evidence="ECO:0007829|PDB:1CZA" FT STRAND 613..616 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 633..644 FT /evidence="ECO:0007829|PDB:1CZA" FT STRAND 650..655 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 657..666 FT /evidence="ECO:0007829|PDB:1CZA" FT STRAND 672..689 FT /evidence="ECO:0007829|PDB:1CZA" FT TURN 690..692 FT /evidence="ECO:0007829|PDB:1CZA" FT STRAND 700..706 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 709..711 FT /evidence="ECO:0007829|PDB:1CZA" FT TURN 712..715 FT /evidence="ECO:0007829|PDB:1CZA" FT TURN 717..721 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 724..731 FT /evidence="ECO:0007829|PDB:1CZA" FT TURN 734..737 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 742..744 FT /evidence="ECO:0007829|PDB:1CZA" FT TURN 747..749 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 750..763 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 768..770 FT /evidence="ECO:0007829|PDB:1CZA" FT TURN 774..777 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 784..790 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 797..807 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 813..848 FT /evidence="ECO:0007829|PDB:1CZA" FT STRAND 852..861 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 863..867 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 871..882 FT /evidence="ECO:0007829|PDB:1CZA" FT STRAND 886..892 FT /evidence="ECO:0007829|PDB:1CZA" FT HELIX 898..912 FT /evidence="ECO:0007829|PDB:1CZA" FT VARIANT P19367-3:7..917 FT /note="Missing (in HMSNR)" FT /evidence="ECO:0000269|PubMed:34193129" FT /id="VAR_087589" SQ SEQUENCE 917 AA; 102486 MW; F29A6837531C0594 CRC64; MIAAQLLAYY FTELKDDQVK KIDKYLYAMR LSDETLIDIM TRFRKEMKNG LSRDFNPTAT VKMLPTFVRS IPDGSEKGDF IALDLGGSSF RILRVQVNHE KNQNVHMESE VYDTPENIVH GSGSQLFDHV AECLGDFMEK RKIKDKKLPV GFTFSFPCQQ SKIDEAILIT WTKRFKASGV EGADVVKLLN KAIKKRGDYD ANIVAVVNDT VGTMMTCGYD DQHCEVGLII GTGTNACYME ELRHIDLVEG DEGRMCINTE WGAFGDDGSL EDIRTEFDRE IDRGSLNPGK QLFEKMVSGM YLGELVRLIL VKMAKEGLLF EGRITPELLT RGKFNTSDVS AIEKNKEGLH NAKEILTRLG VEPSDDDCVS VQHVCTIVSF RSANLVAATL GAILNRLRDN KGTPRLRTTV GVDGSLYKTH PQYSRRFHKT LRRLVPDSDV RFLLSESGSG KGAAMVTAVA YRLAEQHRQI EETLAHFHLT KDMLLEVKKR MRAEMELGLR KQTHNNAVVK MLPSFVRRTP DGTENGDFLA LDLGGTNFRV LLVKIRSGKK RTVEMHNKIY AIPIEIMQGT GEELFDHIVS CISDFLDYMG IKGPRMPLGF TFSFPCQQTS LDAGILITWT KGFKATDCVG HDVVTLLRDA IKRREEFDLD VVAVVNDTVG TMMTCAYEEP TCEVGLIVGT GSNACYMEEM KNVEMVEGDQ GQMCINMEWG AFGDNGCLDD IRTHYDRLVD EYSLNAGKQR YEKMISGMYL GEIVRNILID FTKKGFLFRG QISETLKTRG IFETKFLSQI ESDRLALLQV RAILQQLGLN STCDDSILVK TVCGVVSRRA AQLCGAGMAA VVDKIRENRG LDRLNVTVGV DGTLYKLHPH FSRIMHQTVK ELSPKCNVSF LLSEDGSGKG AALITAVGVR LRTEASS //