HKDC1_HUMAN
ID HKDC1_HUMAN Reviewed; 917 AA.
AC Q2TB90; B5MDN9; Q2TB91; Q5VTC7; Q7Z373; Q8WU37; Q96EH2; Q9H5Y9;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Hexokinase HKDC1 {ECO:0000305};
DE EC=2.7.1.1 {ECO:0000269|PubMed:30517626};
DE AltName: Full=Hexokinase domain-containing protein 1 {ECO:0000305};
GN Name=HKDC1 {ECO:0000312|HGNC:HGNC:23302};
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-721.
RC TISSUE=Eye, and Kidney;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 196-881 (ISOFORM 3).
RC TISSUE=Ileal mucosa;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 647-917 (ISOFORM 2), AND VARIANT
RP ARG-721.
RC TISSUE=Rectum tumor;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
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 [6]
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 [7]
RP TISSUE SPECIFICITY.
RX PubMed=27459389; DOI=10.1210/en.2016-1288;
RA Ludvik A.E., Pusec C.M., Priyadarshini M., Angueira A.R., Guo C., Lo A.,
RA Hershenhouse K.S., Yang G.Y., Ding X., Reddy T.E., Lowe W.L. Jr.,
RA Layden B.T.;
RT "HKDC1 is a novel hexokinase involved in whole-body glucose use.";
RL Endocrinology 157:3452-3461(2016).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=29401404; DOI=10.1369/0022155418756849;
RA Khan M.W., Ding X., Cotler S.J., Clarke M., Layden B.T.;
RT "Studies on the tissue localization of HKDC1, a putative novel fifth
RT hexokinase, in humans.";
RL J. Histochem. Cytochem. 66:385-392(2018).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=30517626; DOI=10.1210/en.2018-00887;
RA Pusec C.M., De Jesus A., Khan M.W., Terry A.R., Ludvik A.E., Xu K.,
RA Giancola N., Pervaiz H., Daviau Smith E., Ding X., Harrison S.,
RA Chandel N.S., Becker T.C., Hay N., Ardehali H., Cordoba-Chacon J.,
RA Layden B.T.;
RT "Hepatic HKDC1 expression contributes to liver metabolism.";
RL Endocrinology 160:313-330(2019).
RN [10]
RP VARIANT RP92 MET-58, CHARACTERIZATION OF VARIANT RP92 MET-58, INVOLVEMENT
RP IN RP92, AND SUBCELLULAR LOCATION.
RX PubMed=30085091; DOI=10.1093/hmg/ddy281;
RA Zhang L., Sun Z., Zhao P., Huang L., Xu M., Yang Y., Chen X., Lu F.,
RA Zhang X., Wang H., Zhang S., Liu W., Jiang Z., Ma S., Chen R., Zhao C.,
RA Yang Z., Sui R., Zhu X.;
RT "Whole-exome sequencing revealed HKDC1 as a candidate gene associated with
RT autosomal-recessive retinitis pigmentosa.";
RL Hum. Mol. Genet. 27:4157-4168(2018).
CC -!- FUNCTION: Catalyzes the phosphorylation of hexose to hexose 6-
CC phosphate, although at very low level compared to other hexokinases
CC (PubMed:30517626). Has low glucose phosphorylating activity compared to
CC other hexokinases (PubMed:30517626). Involved in glucose homeostasis
CC and hepatic lipid accumulation. Required to maintain whole-body glucose
CC homeostasis during pregnancy; however additional evidences are required
CC to confirm this role (By similarity). {ECO:0000250|UniProtKB:Q91W97,
CC ECO:0000269|PubMed:30517626}.
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:30517626};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741;
CC Evidence={ECO:0000269|PubMed:30517626};
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:30517626};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826;
CC Evidence={ECO:0000269|PubMed:30517626};
CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC {ECO:0000305|PubMed:30517626}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 1/4.
CC {ECO:0000305|PubMed:30517626}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30085091}.
CC Mitochondrion membrane {ECO:0000305|PubMed:30517626}; Peripheral
CC membrane protein {ECO:0000305}. Photoreceptor inner segment
CC {ECO:0000250|UniProtKB:Q91W97}. Note=The mitochondrial-binding peptide
CC (MBP) region promotes association with the mitochondrion.
CC {ECO:0000305|PubMed:30517626}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q2TB90-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2TB90-2; Sequence=VSP_027535, VSP_027536;
CC Name=3;
CC IsoId=Q2TB90-3; Sequence=VSP_027533, VSP_027534;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:27459389,
CC PubMed:29401404). Highly expressed in the brush border, surface
CC epithelium and the myenteric plexus of the small and large intestines;
CC the acinar centrocytes and interlobular ducts of the pancreas; and the
CC alveolar macrophages in the lungs (at protein level) (PubMed:29401404).
CC Present at moderate level in the thyroid follicular epithelium (at
CC protein level) (PubMed:29401404). {ECO:0000269|PubMed:27459389,
CC ECO:0000269|PubMed:29401404}.
CC -!- DISEASE: Retinitis pigmentosa 92 (RP92) [MIM:619614]: 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. RP92 is an autosomal recessive, mild
CC form with onset of night blindness and vision loss in the third to
CC sixth decades of life. {ECO:0000269|PubMed:30085091}. Note=The disease
CC may be caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01084, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH21278.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB15478.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL596223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012337; AAH12337.1; -; mRNA.
DR EMBL; BC021278; AAH21278.1; ALT_FRAME; mRNA.
DR EMBL; BC110504; AAI10505.1; -; mRNA.
DR EMBL; BC110505; AAI10506.2; -; mRNA.
DR EMBL; AK026414; BAB15478.1; ALT_FRAME; mRNA.
DR EMBL; BX538078; CAD98002.1; -; mRNA.
DR CCDS; CCDS7288.1; -. [Q2TB90-1]
DR RefSeq; NP_079406.3; NM_025130.3. [Q2TB90-1]
DR AlphaFoldDB; Q2TB90; -.
DR SMR; Q2TB90; -.
DR BioGRID; 123172; 76.
DR IntAct; Q2TB90; 6.
DR MINT; Q2TB90; -.
DR STRING; 9606.ENSP00000346643; -.
DR ChEMBL; CHEMBL1741200; -.
DR GlyGen; Q2TB90; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q2TB90; -.
DR PhosphoSitePlus; Q2TB90; -.
DR BioMuta; HKDC1; -.
DR DMDM; 311033440; -.
DR EPD; Q2TB90; -.
DR jPOST; Q2TB90; -.
DR MassIVE; Q2TB90; -.
DR MaxQB; Q2TB90; -.
DR PaxDb; Q2TB90; -.
DR PeptideAtlas; Q2TB90; -.
DR PRIDE; Q2TB90; -.
DR ProteomicsDB; 61483; -. [Q2TB90-1]
DR ProteomicsDB; 61484; -. [Q2TB90-2]
DR ProteomicsDB; 61485; -. [Q2TB90-3]
DR Antibodypedia; 2524; 152 antibodies from 25 providers.
DR DNASU; 80201; -.
DR Ensembl; ENST00000354624.6; ENSP00000346643.5; ENSG00000156510.13. [Q2TB90-1]
DR GeneID; 80201; -.
DR KEGG; hsa:80201; -.
DR MANE-Select; ENST00000354624.6; ENSP00000346643.5; NM_025130.4; NP_079406.4.
DR UCSC; uc001jpf.4; human. [Q2TB90-1]
DR CTD; 80201; -.
DR DisGeNET; 80201; -.
DR GeneCards; HKDC1; -.
DR HGNC; HGNC:23302; HKDC1.
DR HPA; ENSG00000156510; Tissue enhanced (intestine, retina).
DR MIM; 617221; gene.
DR MIM; 619614; phenotype.
DR neXtProt; NX_Q2TB90; -.
DR OpenTargets; ENSG00000156510; -.
DR PharmGKB; PA134866195; -.
DR VEuPathDB; HostDB:ENSG00000156510; -.
DR eggNOG; KOG1369; Eukaryota.
DR GeneTree; ENSGT00950000182787; -.
DR HOGENOM; CLU_014393_1_0_1; -.
DR InParanoid; Q2TB90; -.
DR OMA; DQYCEVG; -.
DR OrthoDB; 1153545at2759; -.
DR PhylomeDB; Q2TB90; -.
DR TreeFam; TF314238; -.
DR BRENDA; 2.7.1.1; 2681.
DR PathwayCommons; Q2TB90; -.
DR SignaLink; Q2TB90; -.
DR UniPathway; UPA00109; UER00180.
DR UniPathway; UPA00242; -.
DR BioGRID-ORCS; 80201; 12 hits in 1070 CRISPR screens.
DR GenomeRNAi; 80201; -.
DR Pharos; Q2TB90; Tbio.
DR PRO; PR:Q2TB90; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q2TB90; protein.
DR Bgee; ENSG00000156510; Expressed in jejunal mucosa and 126 other tissues.
DR Genevisible; Q2TB90; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008865; F:fructokinase activity; IBA:GO_Central.
DR GO; GO:0004340; F:glucokinase activity; IDA:UniProtKB.
DR GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR GO; GO:0046835; P:carbohydrate phosphorylation; IBA:GO_Central.
DR GO; GO:0001678; P:cellular glucose homeostasis; IDA:UniProtKB.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IDA:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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; PTHR19443; 2.
DR Pfam; PF00349; Hexokinase_1; 2.
DR Pfam; PF03727; Hexokinase_2; 2.
DR SUPFAM; SSF53067; SSF53067; 4.
DR PROSITE; PS00378; HEXOKINASE_1; 1.
DR PROSITE; PS51748; HEXOKINASE_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Glycolysis; Kinase; Membrane;
KW Mitochondrion; Nucleotide-binding; Reference proteome; Repeat;
KW Retinitis pigmentosa; Transferase.
FT CHAIN 1..917
FT /note="Hexokinase HKDC1"
FT /id="PRO_0000299035"
FT DOMAIN 16..458
FT /note="Hexokinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT DOMAIN 464..905
FT /note="Hexokinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 1..20
FT /note="Mitochondrial-binding peptide (MBP)"
FT /evidence="ECO:0000305|PubMed:30517626"
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..654
FT /note="Hexokinase small subdomain 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 655..894
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:0000250|UniProtKB:P19367"
FT BINDING 84..91
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 84..89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 155
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 172..173
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 208..209
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 209
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 232
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 235
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 260
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 291..294
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 413..415
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 425..426
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 449
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 532..537
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 532..536
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 602..603
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 619..620
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 655..656
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 656
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 679
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 679
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 681..682
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 707
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 741
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 746..747
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 783..787
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 860..862
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 862..866
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 896
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT VAR_SEQ 705..736
FT /note="NTEWGGFGDNGCIDDIWTRYDTEVDEGSLNPG -> CFSFCLWFVLQVLIVV
FT LRIVRYRKSSKLIKKF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_027533"
FT VAR_SEQ 737..917
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_027534"
FT VAR_SEQ 791..806
FT /note="SDRLALLQVRRILQQL -> RMLSVIDAYCLDLLFH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_027535"
FT VAR_SEQ 807..917
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_027536"
FT VARIANT 54
FT /note="D -> G (in dbSNP:rs10823320)"
FT /id="VAR_034776"
FT VARIANT 58
FT /note="T -> M (in RP92; unknown pathological significance;
FT slightly decreased hexokinase activity)"
FT /evidence="ECO:0000269|PubMed:30085091"
FT /id="VAR_086465"
FT VARIANT 124
FT /note="T -> I (in dbSNP:rs874556)"
FT /id="VAR_034777"
FT VARIANT 204
FT /note="L -> P (in dbSNP:rs7899445)"
FT /id="VAR_034778"
FT VARIANT 721
FT /note="W -> R (in dbSNP:rs1111335)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_034779"
FT VARIANT 917
FT /note="N -> K (in dbSNP:rs906219)"
FT /id="VAR_034780"
SQ SEQUENCE 917 AA; 102545 MW; F7E32F3F2B4118B6 CRC64;
MFAVHLMAFY FSKLKEDQIK KVDRFLYHMR LSDDTLLDIM RRFRAEMEKG LAKDTNPTAA
VKMLPTFVRA IPDGSENGEF LSLDLGGSKF RVLKVQVAEE GKRHVQMESQ FYPTPNEIIR
GNGTELFEYV ADCLADFMKT KDLKHKKLPL GLTFSFPCRQ TKLEEGVLLS WTKKFKARGV
QDTDVVSRLT KAMRRHKDMD VDILALVNDT VGTMMTCAYD DPYCEVGVII GTGTNACYME
DMSNIDLVEG DEGRMCINTE WGAFGDDGAL EDIRTEFDRE LDLGSLNPGK QLFEKMISGL
YLGELVRLIL LKMAKAGLLF GGEKSSALHT KGKIETRHVA AMEKYKEGLA NTREILVDLG
LEPSEADCIA VQHVCTIVSF RSANLCAAAL AAILTRLREN KKVERLRTTV GMDGTLYKIH
PQYPKRLHKV VRKLVPSCDV RFLLSESGST KGAAMVTAVA SRVQAQRKQI DRVLALFQLT
REQLVDVQAK MRAELEYGLK KKSHGLATVR MLPTYVCGLP DGTEKGKFLA LDLGGTNFRV
LLVKIRSGRR SVRMYNKIFA IPLEIMQGTG EELFDHIVQC IADFLDYMGL KGASLPLGFT
FSFPCRQMSI DKGTLIGWTK GFKATDCEGE DVVDMLREAI KRRNEFDLDI VAVVNDTVGT
MMTCGYEDPN CEIGLIAGTG SNMCYMEDMR NIEMVEGGEG KMCINTEWGG FGDNGCIDDI
WTRYDTEVDE GSLNPGKQRY EKMTSGMYLG EIVRQILIDL TKQGLLFRGQ ISERLRTRGI
FETKFLSQIE SDRLALLQVR RILQQLGLDS TCEDSIVVKE VCGAVSRRAA QLCGAGLAAI
VEKRREDQGL EHLRITVGVD GTLYKLHPHF SRILQETVKE LAPRCDVTFM LSEDGSGKGA
ALITAVAKRL QQAQKEN
