HXK2_MOUSE
ID HXK2_MOUSE Reviewed; 917 AA.
AC O08528;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Hexokinase-2 {ECO:0000305};
DE EC=2.7.1.1 {ECO:0000250|UniProtKB:P52789};
DE AltName: Full=Hexokinase type II {ECO:0000303|PubMed:15489334};
DE Short=HK II {ECO:0000303|PubMed:15489334};
GN Name=Hk2 {ECO:0000312|MGI:MGI:1315197};
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 [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ; TISSUE=Liver;
RX PubMed=10656921; DOI=10.1007/s003350010019;
RA Heikkinen S., Suppola S., Malkki M., Deeb S.S., Janne J., Laakso M.;
RT "Mouse hexokinase II gene: structure, cDNA, promoter analysis, and
RT expression pattern.";
RL Mamm. Genome 11:91-96(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 FUNCTION.
RX PubMed=18350175; DOI=10.1371/journal.pone.0001852;
RA Chiara F., Castellaro D., Marin O., Petronilli V., Brusilow W.S.,
RA Juhaszova M., Sollott S.J., Forte M., Bernardi P., Rasola A.;
RT "Hexokinase II detachment from mitochondria triggers apoptosis through the
RT permeability transition pore independent of voltage-dependent anion
RT channels.";
RL PLoS ONE 3:E1852-E1852(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen, and
RC Testis;
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 [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=10428828; DOI=10.1074/jbc.274.32.22517;
RA Heikkinen S., Pietilae M., Halmekytoe M., Suppola S., Pirinen E.,
RA Deeb S.S., Jaenne J., Laakso M.;
RT "Hexokinase II-deficient mice. Prenatal death of homozygotes without
RT disturbances in glucose tolerance in heterozygotes.";
RL J. Biol. Chem. 274:22517-22523(1999).
CC -!- FUNCTION: Catalyzes the phosphorylation of hexose, such as D-glucose
CC and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D-
CC fructose 6-phosphate, respectively) (By similarity). Mediates the
CC initial step of glycolysis by catalyzing phosphorylation of D-glucose
CC to D-glucose 6-phosphate (By similarity). Plays a key role in
CC maintaining the integrity of the outer mitochondrial membrane by
CC preventing the release of apoptogenic molecules from the intermembrane
CC space and subsequent apoptosis (PubMed:18350175).
CC {ECO:0000250|UniProtKB:P27881, ECO:0000269|PubMed:18350175}.
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:0000250|UniProtKB:P52789};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741;
CC Evidence={ECO:0000250|UniProtKB:P52789};
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:P27881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126;
CC Evidence={ECO:0000250|UniProtKB:P27881};
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:P52789};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826;
CC Evidence={ECO:0000250|UniProtKB:P52789};
CC -!- ACTIVITY REGULATION: Hexokinase activity is specifically inhibited by
CC 2,6-disubstituted glucosamines. {ECO:0000250|UniProtKB:P52789}.
CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC {ECO:0000250|UniProtKB:P52789}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 1/4.
CC {ECO:0000250|UniProtKB:P52789}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with TIGAR; the interaction
CC increases hexokinase activity in a hypoxia- and HIF1A-dependent manner
CC (By similarity). {ECO:0000250|UniProtKB:P19367,
CC ECO:0000250|UniProtKB:P52789}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:P52789}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P52789}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P52789}. Note=The mitochondrial-binding peptide
CC (MBP) region promotes association with the mitochondrial outer
CC membrane. The interaction with the mitochondrial outer membrane via the
CC mitochondrial-binding peptide (MBP) region promotes higher stability of
CC the protein. Release from the mitochondrial outer membrane into the
CC cytosol induces permeability transition pore (PTP) opening and
CC apoptosis. {ECO:0000250|UniProtKB:P52789}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle, heart
CC and adipose tissues. {ECO:0000269|PubMed:10656921}.
CC -!- DOMAIN: The N- and C-terminal halves of the protein contain a
CC hexokinase domain. In contrast to hexokinase-1 and -3 (HK1 and HK3,
CC respectively), both hexokinase domains display catalytic activity. The
CC region connecting the two hexokinase domains is required for the
CC catalytic activity of the N-terminal hexokinase domain. The N-terminal
CC half regulates stability of the whole enzyme.
CC {ECO:0000250|UniProtKB:P52789}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality around E7.5 stage probably
CC caused by the absence of hexokinase activity.
CC {ECO:0000269|PubMed:10428828}.
CC -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01084, ECO:0000305}.
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DR EMBL; Y11666; CAA72366.1; -; Genomic_DNA.
DR EMBL; Y11667; CAA72366.1; JOINED; Genomic_DNA.
DR EMBL; Y11668; CAA72366.1; JOINED; Genomic_DNA.
DR EMBL; AJ238540; CAB72257.1; -; mRNA.
DR EMBL; BC054472; AAH54472.1; -; mRNA.
DR CCDS; CCDS20263.1; -.
DR RefSeq; NP_038848.1; NM_013820.3.
DR AlphaFoldDB; O08528; -.
DR SMR; O08528; -.
DR BioGRID; 200316; 7.
DR DIP; DIP-41484N; -.
DR IntAct; O08528; 5.
DR MINT; O08528; -.
DR STRING; 10090.ENSMUSP00000000642; -.
DR ChEMBL; CHEMBL4105980; -.
DR iPTMnet; O08528; -.
DR PhosphoSitePlus; O08528; -.
DR SwissPalm; O08528; -.
DR EPD; O08528; -.
DR jPOST; O08528; -.
DR MaxQB; O08528; -.
DR PaxDb; O08528; -.
DR PeptideAtlas; O08528; -.
DR PRIDE; O08528; -.
DR ProteomicsDB; 273237; -.
DR Antibodypedia; 31617; 710 antibodies from 38 providers.
DR DNASU; 15277; -.
DR Ensembl; ENSMUST00000000642; ENSMUSP00000000642; ENSMUSG00000000628.
DR GeneID; 15277; -.
DR KEGG; mmu:15277; -.
DR UCSC; uc009cll.2; mouse.
DR CTD; 3099; -.
DR MGI; MGI:1315197; Hk2.
DR VEuPathDB; HostDB:ENSMUSG00000000628; -.
DR eggNOG; KOG1369; Eukaryota.
DR GeneTree; ENSGT00950000182787; -.
DR InParanoid; O08528; -.
DR OMA; MEEMRYI; -.
DR OrthoDB; 1153545at2759; -.
DR PhylomeDB; O08528; -.
DR TreeFam; TF314238; -.
DR BRENDA; 2.7.1.1; 3474.
DR Reactome; R-MMU-70171; Glycolysis.
DR SABIO-RK; O08528; -.
DR UniPathway; UPA00109; UER00180.
DR UniPathway; UPA00242; -.
DR BioGRID-ORCS; 15277; 8 hits in 76 CRISPR screens.
DR ChiTaRS; Hk2; mouse.
DR PRO; PR:O08528; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; O08528; protein.
DR Bgee; ENSMUSG00000000628; Expressed in plantaris and 246 other tissues.
DR ExpressionAtlas; O08528; baseline and differential.
DR Genevisible; O08528; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0016529; C:sarcoplasmic reticulum; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0008865; F:fructokinase activity; ISS:UniProtKB.
DR GO; GO:0004340; F:glucokinase activity; ISS:UniProtKB.
DR GO; GO:0005536; F:glucose binding; ISO:MGI.
DR GO; GO:0004396; F:hexokinase activity; IDA:MGI.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IGI:MGI.
DR GO; GO:0046835; P:carbohydrate phosphorylation; IMP:MGI.
DR GO; GO:0001678; P:cellular glucose homeostasis; IBA:GO_Central.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0072655; P:establishment of protein localization to mitochondrion; ISO:MGI.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; ISS:UniProtKB.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; ISS:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; IMP:MGI.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0007595; P:lactation; IEA:Ensembl.
DR GO; GO:0072656; P:maintenance of protein location in mitochondrion; ISO:MGI.
DR GO; GO:0035795; P:negative regulation of mitochondrial membrane permeability; IMP:CACAO.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IMP:CACAO.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:1904925; P:positive regulation of autophagy of mitochondrion in response to mitochondrial depolarization; ISO:MGI.
DR GO; GO:0046324; P:regulation of glucose import; IMP:MGI.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0002931; P:response to ischemia; ISO:MGI.
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; 2.
DR PROSITE; PS51748; HEXOKINASE_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Allosteric enzyme; ATP-binding; Cytoplasm; Glycolysis; Kinase;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transferase.
FT CHAIN 1..917
FT /note="Hexokinase-2"
FT /id="PRO_0000197588"
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..16
FT /note="Mitochondrial-binding peptide (MBP)"
FT /evidence="ECO:0000250|UniProtKB:P52789"
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: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 84..88
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P52789"
FT BINDING 155..156
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P52789"
FT BINDING 172..173
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P52789"
FT BINDING 208..209
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P52789"
FT BINDING 209
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P52789"
FT BINDING 232
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P52789"
FT BINDING 235
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P52789"
FT BINDING 260
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P52789"
FT BINDING 291..294
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P52789"
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:P52789"
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:P52789"
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:P52789"
FT BINDING 603..604
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P52789"
FT BINDING 620..621
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P52789"
FT BINDING 656..657
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P52789"
FT BINDING 657
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P52789"
FT BINDING 680
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 680
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P52789"
FT BINDING 682..683
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P52789"
FT BINDING 708
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P52789"
FT BINDING 739..742
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P52789"
FT BINDING 747..748
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 784..788
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 861..863
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P52789"
FT BINDING 863..867
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 897
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P52789"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P52789"
SQ SEQUENCE 917 AA; 102535 MW; 44293E7A92D724B3 CRC64;
MIASHMIACL FTELNQNQVQ KVDQYLYHMR LSDETLLEIS RRFRKEMEKG LGATTHPTAA
VKMLPTFVRS TPDGTEHGEF LALDLGGTNF RVLRVRVTDN GLQRVEMENQ IYAIPEDIMR
GSGTQLFDHI AECLANFMDK LQIKEKKLPL GFTFSFPCHQ TKLDESFLVS WTKGFKSSGV
EGRDVVDLIR KAIQRRGDFD IDIVAVVNDT VGTMMTCGYD DQNCEIGLIV GTGSNACYME
EMRHIDMVEG DEGRMCINME WGAFGDDGTL NDIRTEFDRE IDMGSLNPGK QLFEKMISGM
YMGELVRLIL VKMAKAELLF QGKLSPELLT TGSFETKDVS DIEDDKDGIQ KAYQILVRLG
LSPLQEDCVA THRICQIVST RSASLCAATL AAVLWRIKEN KGEERLRSTI GVDGSVYKKH
PHFAKRLHKA VRRLVPDCDV RFLRSEDGSG KGAAMVTAVA YRLADQHRAR QKTLESLKLS
HEQLLEVKRR MKVEMEQGLS KETHEAAPVK MLPTYVCATP DGTEKGDFLA LDLGGTNFRV
LLVRVRNGKR RGVEMHNKIY SIPQEVMHGT GEELFDHIVQ CIADFLEYMG MKGVSLPLGF
TFSFPCQQNS LDQSILLKWT KGFKASGCEG EDVVTLLKEA IRRREEFDLD VVAVVNDTVG
TMMTCGYEDP HCEVGLIVGT GSNACYMEEM RNVELVDGEE GRMCVNMEWG AFGDNGCLDD
LRTVFDVAVD ELSLNPGKQR FEKMISGMYL GEIVRNILID FTKRGLLFRG RISERLKTRG
IFETKFLSQI ESDCLALLQV RAILRHLGLE STCDDSIIVK EVCTVVARRA AQLCGAGMAA
VVDKIRENRG LDNLKVTVGV DGTLYKLHPH FAKVMHETVR DLAPKCDVSF LESEDGSGKG
AALITAVACR IREAGQR
