HXK4_MOUSE
ID HXK4_MOUSE Reviewed; 465 AA.
AC P52792; P52791;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Hexokinase-4 {ECO:0000305};
DE Short=HK4 {ECO:0000305};
DE EC=2.7.1.1 {ECO:0000269|PubMed:8530440};
DE AltName: Full=Glucokinase {ECO:0000303|PubMed:8575768, ECO:0000303|PubMed:8575769};
DE AltName: Full=Hexokinase type IV {ECO:0000250|UniProtKB:P17712};
DE Short=HK IV {ECO:0000250|UniProtKB:P17712};
DE AltName: Full=Hexokinase-D {ECO:0000250|UniProtKB:P17712};
GN Name=Gck {ECO:0000312|MGI:MGI:1270854};
GN Synonyms=Gk {ECO:0000303|PubMed:8575768, ECO:0000303|PubMed:8575769};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8575769; DOI=10.1006/geno.1995.9942;
RA Ishimura-Oka K., Nakamuta M., Chu M.J., Sullivan M., Chan L., Oka K.;
RT "Partial structure of the mouse glucokinase gene.";
RL Genomics 29:751-754(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RC STRAIN=129/Sv; TISSUE=Liver;
RX PubMed=8575768; DOI=10.1006/geno.1995.9943;
RA Postic C., Niswender K.D., Decaux J.F., Shelton K.D., Gouhot B.,
RA Petterpher C.C., Granner D.K., Girard J., Magnuson M.A.;
RT "Cloning and characterization of the mouse glucokinase gene locus and
RT identification of distal liver-specific DNase I hypersensitive sites.";
RL Genomics 29:740-750(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Liver;
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 1-166 (ISOFORM 1).
RC TISSUE=Pancreas;
RX PubMed=1999433; DOI=10.1016/s0021-9258(20)64354-x;
RA Hughes S.D., Quaade C., Milburn J.L., Cassidy L., Newgard C.B.;
RT "Expression of normal and novel glucokinase mRNAs in anterior pituitary and
RT islet cells.";
RL J. Biol. Chem. 266:4521-4530(1991).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP INDUCTION BY ENDOCANNABINOID ANANDAMIDE.
RX PubMed=21987372; DOI=10.1002/hep.24733;
RA Jourdan T., Demizieux L., Gresti J., Djaouti L., Gaba L., Verges B.,
RA Degrace P.;
RT "Antagonism of peripheral hepatic cannabinoid receptor-1 improves liver
RT lipid metabolism in mice: evidence from cultured explants.";
RL Hepatology 55:790-799(2012).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=24187134; DOI=10.1074/jbc.m113.526632;
RA Hofmeister-Brix A., Kollmann K., Langer S., Schultz J., Lenzen S.,
RA Baltrusch S.;
RT "Identification of the ubiquitin-like domain of midnolin as a new
RT glucokinase interaction partner.";
RL J. Biol. Chem. 288:35824-35839(2013).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=7665557; DOI=10.1074/jbc.270.37.21464;
RA Bali D., Svetlanov A., Lee H.W., Fusco-DeMane D., Leiser M., Li B.,
RA Barzilai N., Surana M., Hou H., Fleischer N.;
RT "Animal model for maturity-onset diabetes of the young generated by
RT disruption of the mouse glucokinase gene.";
RL J. Biol. Chem. 270:21464-21467(1995).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=8530440; DOI=10.1074/jbc.270.51.30253;
RA Terauchi Y., Sakura H., Yasuda K., Iwamoto K., Takahashi N., Ito K.,
RA Kasai H., Suzuki H., Ueda O., Kamada N.;
RT "Pancreatic beta-cell-specific targeted disruption of glucokinase gene.
RT Diabetes mellitus due to defective insulin secretion to glucose.";
RL J. Biol. Chem. 270:30253-30256(1995).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9867845; DOI=10.1074/jbc.274.1.305;
RA Postic C., Shiota M., Niswender K.D., Jetton T.L., Chen Y., Moates J.M.,
RA Shelton K.D., Lindner J., Cherrington A.D., Magnuson M.A.;
RT "Dual roles for glucokinase in glucose homeostasis as determined by liver
RT and pancreatic beta cell-specific gene knock-outs using Cre recombinase.";
RL J. Biol. Chem. 274:305-315(1999).
RN [11]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH GCKR.
RX PubMed=10713097; DOI=10.1074/jbc.275.11.7826;
RA Grimsby J., Coffey J.W., Dvorozniak M.T., Magram J., Li G.,
RA Matschinsky F.M., Shiota C., Kaur S., Magnuson M.A., Grippo J.F.;
RT "Characterization of glucokinase regulatory protein-deficient mice.";
RL J. Biol. Chem. 275:7826-7831(2000).
CC -!- FUNCTION: Catalyzes the phosphorylation of hexose, such as D-glucose,
CC D-fructose and D-mannose, to hexose 6-phosphate (D-glucose 6-phosphate,
CC D-fructose 6-phosphate and D-mannose 6-phosphate, respectively)
CC (PubMed:8530440). Compared to other hexokinases, has a weak affinity
CC for D-glucose, and is effective only when glucose is abundant (By
CC similarity). Mainly expressed in pancreatic beta cells and the liver
CC and constitutes a rate-limiting step in glucose metabolism in these
CC tissues (PubMed:8530440, PubMed:9867845). Since insulin secretion
CC parallels glucose metabolism and the low glucose affinity of GCK
CC ensures that it can change its enzymatic activity within the
CC physiological range of glucose concentrations, GCK acts as a glucose
CC sensor in the pancreatic beta cell (PubMed:8530440, PubMed:9867845). In
CC pancreas, plays an important role in modulating insulin secretion
CC (PubMed:8530440). In liver, helps to facilitate the uptake and
CC conversion of glucose by acting as an insulin-sensitive determinant of
CC hepatic glucose usage (PubMed:9867845). Required to provide D-glucose
CC 6-phosphate for the synthesis of glycogen (PubMed:9867845). Mediates
CC the initial step of glycolysis by catalyzing phosphorylation of D-
CC glucose to D-glucose 6-phosphate (By similarity).
CC {ECO:0000250|UniProtKB:P17712, ECO:0000250|UniProtKB:P35557,
CC ECO:0000269|PubMed:8530440, ECO:0000269|PubMed:9867845}.
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:8530440};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741;
CC Evidence={ECO:0000269|PubMed:8530440};
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:P35557};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126;
CC Evidence={ECO:0000250|UniProtKB:P35557};
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:0000250|UniProtKB:P35557};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826;
CC Evidence={ECO:0000250|UniProtKB:P35557};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-mannose = ADP + D-mannose 6-phosphate + 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:P35557};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11029;
CC Evidence={ECO:0000250|UniProtKB:P35557};
CC -!- ACTIVITY REGULATION: Subject to allosteric regulation. Low glucose and
CC high fructose-6-phosphate triggers association with the inhibitor GCKR
CC followed by sequestration in the nucleus.
CC {ECO:0000250|UniProtKB:P35557}.
CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC {ECO:0000305|PubMed:8530440}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 1/4.
CC {ECO:0000305|PubMed:8530440}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with MIDN; the interaction
CC occurs preferentially at low glucose levels and results in inhibition
CC of hexokinase activity (By similarity). Interacts with GCKR; leading to
CC sequestration in the nucleus (PubMed:10713097).
CC {ECO:0000250|UniProtKB:P35557, ECO:0000269|PubMed:10713097}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24187134}. Nucleus
CC {ECO:0000269|PubMed:10713097}. Mitochondrion
CC {ECO:0000250|UniProtKB:P17712}. Note=Under low glucose concentrations,
CC GCK associates with GCKR and the inactive complex is recruited to the
CC hepatocyte nucleus. {ECO:0000269|PubMed:10713097}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=2;
CC Comment=A number of isoforms are produced by alternative promoter
CC usage. The use of alternative promoters apparently enables the type
CC IV hexokinase gene to be regulated by insulin in the liver and
CC glucose in the beta cell. This may constitute an important feedback
CC loop for maintaining glucose homeostasis.
CC {ECO:0000250|UniProtKB:P35557};
CC Name=1;
CC IsoId=P52792-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P52792-2; Sequence=VSP_002076;
CC -!- INDUCTION: Up-regulated by endocannabinoid anandamide/AEA.
CC {ECO:0000269|PubMed:21987372}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality caused by the absence of
CC hexokinase activity (PubMed:7665557). Conditional deletion in
CC pancreatic beta-cells causes severe diabetes shortly after birth
CC leading to lethality within a week (PubMed:8530440, PubMed:9867845).
CC Deficient islets show defective insulin secretion in response to
CC glucose (PubMed:8530440). Conditional deletion in liver leads to mild
CC hyperglycemia; however, mice display pronounced defects in both
CC glycogen synthesis and glucose turnover rates during a hyperglycemic
CC clamp (PubMed:9867845). {ECO:0000269|PubMed:7665557,
CC ECO:0000269|PubMed:8530440, ECO:0000269|PubMed:9867845}.
CC -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01084, ECO:0000305}.
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DR EMBL; L38990; AAB00360.1; -; mRNA.
DR EMBL; L41631; AAC42074.1; -; Genomic_DNA.
DR EMBL; BC011139; AAH11139.1; -; mRNA.
DR EMBL; M58755; AAA37703.1; -; mRNA.
DR CCDS; CCDS24409.1; -. [P52792-1]
DR CCDS; CCDS70135.1; -. [P52792-2]
DR PIR; I49693; I49693.
DR PIR; I49694; I49694.
DR RefSeq; NP_001274315.1; NM_001287386.1. [P52792-2]
DR RefSeq; NP_034422.2; NM_010292.5. [P52792-1]
DR AlphaFoldDB; P52792; -.
DR SMR; P52792; -.
DR BioGRID; 222262; 4.
DR CORUM; P52792; -.
DR STRING; 10090.ENSMUSP00000099984; -.
DR BindingDB; P52792; -.
DR ChEMBL; CHEMBL3112387; -.
DR iPTMnet; P52792; -.
DR PhosphoSitePlus; P52792; -.
DR SwissPalm; P52792; -.
DR jPOST; P52792; -.
DR PaxDb; P52792; -.
DR PRIDE; P52792; -.
DR ProteomicsDB; 267182; -. [P52792-1]
DR ProteomicsDB; 267183; -. [P52792-2]
DR Antibodypedia; 2045; 539 antibodies from 35 providers.
DR DNASU; 103988; -.
DR Ensembl; ENSMUST00000102920; ENSMUSP00000099984; ENSMUSG00000041798. [P52792-1]
DR Ensembl; ENSMUST00000109822; ENSMUSP00000105447; ENSMUSG00000041798. [P52792-2]
DR Ensembl; ENSMUST00000109823; ENSMUSP00000105448; ENSMUSG00000041798. [P52792-2]
DR GeneID; 103988; -.
DR KEGG; mmu:103988; -.
DR UCSC; uc007hxn.2; mouse. [P52792-1]
DR CTD; 2645; -.
DR MGI; MGI:1270854; Gck.
DR VEuPathDB; HostDB:ENSMUSG00000041798; -.
DR eggNOG; KOG1369; Eukaryota.
DR GeneTree; ENSGT00950000182787; -.
DR HOGENOM; CLU_014393_5_3_1; -.
DR InParanoid; P52792; -.
DR OMA; IAINCEW; -.
DR OrthoDB; 1153545at2759; -.
DR PhylomeDB; P52792; -.
DR TreeFam; TF314238; -.
DR Reactome; R-MMU-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-MMU-70171; Glycolysis.
DR SABIO-RK; P52792; -.
DR UniPathway; UPA00109; UER00180.
DR UniPathway; UPA00242; -.
DR BioGRID-ORCS; 103988; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Gk; mouse.
DR PRO; PR:P52792; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P52792; protein.
DR Bgee; ENSMUSG00000041798; Expressed in left lobe of liver and 68 other tissues.
DR ExpressionAtlas; P52792; baseline and differential.
DR Genevisible; P52792; MM.
DR GO; GO:0005884; C:actin filament; ISO:MGI.
DR GO; GO:0045180; C:basal cortex; ISO:MGI.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0043531; F:ADP binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0008865; F:fructokinase activity; ISS:UniProtKB.
DR GO; GO:0004340; F:glucokinase activity; IDA:MGI.
DR GO; GO:0005536; F:glucose binding; ISS:UniProtKB.
DR GO; GO:0004396; F:hexokinase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISO:MGI.
DR GO; GO:0019158; F:mannokinase activity; ISS:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0070509; P:calcium ion import; IMP:UniProtKB.
DR GO; GO:0046835; P:carbohydrate phosphorylation; IDA:MGI.
DR GO; GO:0001678; P:cellular glucose homeostasis; IMP:UniProtKB.
DR GO; GO:0042149; P:cellular response to glucose starvation; ISO:MGI.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI.
DR GO; GO:0044320; P:cellular response to leptin stimulus; ISO:MGI.
DR GO; GO:0051594; P:detection of glucose; ISS:UniProtKB.
DR GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; ISO:MGI.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; ISS:UniProtKB.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; ISO:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; IDA:MGI.
DR GO; GO:0005978; P:glycogen biosynthetic process; ISO:MGI.
DR GO; GO:0006096; P:glycolytic process; ISO:MGI.
DR GO; GO:0055088; P:lipid homeostasis; ISO:MGI.
DR GO; GO:0006013; P:mannose metabolic process; ISS:UniProtKB.
DR GO; GO:0006739; P:NADP metabolic process; IMP:MGI.
DR GO; GO:0032811; P:negative regulation of epinephrine secretion; ISO:MGI.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; ISS:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; ISS:UniProtKB.
DR GO; GO:0045821; P:positive regulation of glycolytic process; ISO:MGI.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:UniProtKB.
DR GO; GO:0042327; P:positive regulation of phosphorylation; ISO:MGI.
DR GO; GO:0050796; P:regulation of insulin secretion; IMP:MGI.
DR GO; GO:0043266; P:regulation of potassium ion transport; IMP:MGI.
DR GO; GO:0019932; P:second-messenger-mediated signaling; ISO:MGI.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR039073; GCK_chordate.
DR InterPro; IPR001312; Hexokinase.
DR InterPro; IPR019807; Hexokinase_BS.
DR InterPro; IPR022673; Hexokinase_C.
DR InterPro; IPR022672; Hexokinase_N.
DR PANTHER; PTHR19443; PTHR19443; 1.
DR PANTHER; PTHR19443:SF3; PTHR19443:SF3; 1.
DR Pfam; PF00349; Hexokinase_1; 1.
DR Pfam; PF03727; Hexokinase_2; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00378; HEXOKINASE_1; 1.
DR PROSITE; PS51748; HEXOKINASE_2; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Alternative promoter usage; Alternative splicing;
KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Mitochondrion;
KW Nucleotide-binding; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..465
FT /note="Hexokinase-4"
FT /id="PRO_0000197594"
FT DOMAIN 10..454
FT /note="Hexokinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 67..203
FT /note="Hexokinase small subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 204..443
FT /note="Hexokinase large subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT BINDING 78..83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 151..152
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P35557"
FT BINDING 168..169
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P35557"
FT BINDING 204..205
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P35557"
FT BINDING 228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P35557"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P35557"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P35557"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P35557"
FT BINDING 295..296
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P35557"
FT BINDING 332..336
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P35557"
FT BINDING 411..415
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P35557"
FT VAR_SEQ 1..15
FT /note="MLDDRARMEATKKEK -> MAVDTTRRGAQSLTL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_002076"
FT CONFLICT 133
FT /note="F -> L (in Ref. 4; AAA37703)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="I -> L (in Ref. 4; AAA37703)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 465 AA; 52089 MW; 8C85EED079A52D61 CRC64;
MLDDRARMEA TKKEKVEQIL AEFQLQEEDL KKVMSRMQKE MDRGLKLETH QEASVKMLPT
YVRSTPEGSE VGDFLSLDLG GTNFRVMLVK VGEGEAGQWS VKTKHQMYSI PEDAMTGTAE
MLFDYISECI SDFLDKHQMK HKKLPLGFTF SFPVRHEDID KGILLNWTKG FKASGAEGNN
IVGLLRDAIK RRGDFEMDVV AMVNDTVATM ISCYYEDRQC EVGMIVGTGC NACYMEEMQN
VELVEGDEGR MCVNTEWGAF GNSGELDEFL LEYDRMVDES SVNPGQQLYE KIIGGKYMGE
LVRLVLLKLV EENLLFHGEA SEQLRTRGAF ETRFVSQVES DSGDRRQILN ILSTLGLRPS
VADCDIVRRA CESVSTRAAH MCSAGLAGVI NRMRESRSED VMRITVGVDG SVYKLHPSFK
ERFHASVRRL TPNCEITFIE SEEGSGRGAA LVSAVACKKA CMLGQ
