ID   HXK3_MOUSE              Reviewed;         922 AA.
AC   Q3TRM8; Q3TAX6; Q3UDP1; Q3UEA4;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   24-JAN-2024, entry version 138.
DE   RecName: Full=Hexokinase-3 {ECO:0000305};
DE            EC=2.7.1.1 {ECO:0000250|UniProtKB:P27926};
DE   AltName: Full=Hexokinase type III {ECO:0000250|UniProtKB:P27926};
DE            Short=HK III {ECO:0000250|UniProtKB:P27926};
DE   AltName: Full=Hexokinase-C {ECO:0000250|UniProtKB:P27926};
GN   Name=Hk3 {ECO:0000312|MGI:MGI:2670962};
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone, and Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver, and Spleen;
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).
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). Mediates the initial step of
CC       glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-
CC       phosphate. {ECO:0000250|UniProtKB:P27926}.
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:P27926};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741;
CC         Evidence={ECO:0000250|UniProtKB:P27926};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+);
CC         Xref=Rhea:RHEA:16125, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:37721, ChEBI:CHEBI:61527, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC         Evidence={ECO:0000250|UniProtKB:P27926};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126;
CC         Evidence={ECO:0000250|UniProtKB:P27926};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+);
CC         Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC         Evidence={ECO:0000250|UniProtKB:P27926};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826;
CC         Evidence={ECO:0000250|UniProtKB:P27926};
CC   -!- ACTIVITY REGULATION: Hexokinase is an allosteric enzyme inhibited by
CC       its product D-glucose 6-phosphate. {ECO:0000250|UniProtKB:P52790}.
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC       {ECO:0000250|UniProtKB:P27926}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 1/4.
CC       {ECO:0000250|UniProtKB:P27926}.
CC   -!- DOMAIN: The N- and C-terminal halves of this hexokinase contain a
CC       hexokinase domain. The catalytic activity is associated with the C-
CC       terminus while regulatory function is associated with the N-terminus.
CC       {ECO:0000250|UniProtKB:P19367}.
CC   -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01084, ECO:0000305}.
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DR   EMBL; AK149651; BAE29007.1; -; mRNA.
DR   EMBL; AK149992; BAE29220.1; -; mRNA.
DR   EMBL; AK154603; BAE32706.1; -; mRNA.
DR   EMBL; AK162637; BAE37000.1; -; mRNA.
DR   EMBL; AK171580; BAE42538.1; -; mRNA.
DR   CCDS; CCDS26538.1; -.
DR   RefSeq; NP_001028417.1; NM_001033245.4.
DR   RefSeq; NP_001193319.1; NM_001206390.1.
DR   AlphaFoldDB; Q3TRM8; -.
DR   SMR; Q3TRM8; -.
DR   BioGRID; 229281; 1.
DR   STRING; 10090.ENSMUSP00000051215; -.
DR   iPTMnet; Q3TRM8; -.
DR   PhosphoSitePlus; Q3TRM8; -.
DR   SwissPalm; Q3TRM8; -.
DR   MaxQB; Q3TRM8; -.
DR   PaxDb; 10090-ENSMUSP00000051215; -.
DR   ProteomicsDB; 273332; -.
DR   Antibodypedia; 29158; 483 antibodies from 35 providers.
DR   DNASU; 212032; -.
DR   Ensembl; ENSMUST00000052949.13; ENSMUSP00000051215.7; ENSMUSG00000025877.15.
DR   Ensembl; ENSMUST00000126234.8; ENSMUSP00000123233.2; ENSMUSG00000025877.15.
DR   GeneID; 212032; -.
DR   KEGG; mmu:212032; -.
DR   UCSC; uc007qpr.2; mouse.
DR   AGR; MGI:2670962; -.
DR   CTD; 3101; -.
DR   MGI; MGI:2670962; Hk3.
DR   VEuPathDB; HostDB:ENSMUSG00000025877; -.
DR   eggNOG; KOG1369; Eukaryota.
DR   GeneTree; ENSGT00950000182787; -.
DR   InParanoid; Q3TRM8; -.
DR   OMA; VRPCEVG; -.
DR   OrthoDB; 5481886at2759; -.
DR   PhylomeDB; Q3TRM8; -.
DR   TreeFam; TF314238; -.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-70171; Glycolysis.
DR   SABIO-RK; Q3TRM8; -.
DR   UniPathway; UPA00109; UER00180.
DR   UniPathway; UPA00242; -.
DR   BioGRID-ORCS; 212032; 3 hits in 80 CRISPR screens.
DR   PRO; PR:Q3TRM8; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q3TRM8; Protein.
DR   Bgee; ENSMUSG00000025877; Expressed in granulocyte and 86 other cell types or tissues.
DR   ExpressionAtlas; Q3TRM8; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019899; F:enzyme 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; IEA:InterPro.
DR   GO; GO:0004396; F:hexokinase activity; ISO:MGI.
DR   GO; GO:0042562; F:hormone binding; ISO:MGI.
DR   GO; GO:0046835; P:carbohydrate phosphorylation; IBA:GO_Central.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; ISS:UniProtKB.
DR   GO; GO:0051156; P:glucose 6-phosphate metabolic process; ISS:UniProtKB.
DR   GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR   GO; GO:0001678; P:intracellular glucose homeostasis; IBA:GO_Central.
DR   GO; GO:1901299; P:negative regulation of hydrogen peroxide-mediated programmed cell death; ISO:MGI.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 2.
DR   Gene3D; 3.30.420.40; -; 2.
DR   Gene3D; 3.40.367.20; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR001312; Hexokinase.
DR   InterPro; IPR019807; Hexokinase_BS.
DR   InterPro; IPR022673; Hexokinase_C.
DR   InterPro; IPR022672; Hexokinase_N.
DR   PANTHER; PTHR19443; HEXOKINASE; 1.
DR   PANTHER; PTHR19443:SF1; HEXOKINASE-3; 1.
DR   Pfam; PF00349; Hexokinase_1; 2.
DR   Pfam; PF03727; Hexokinase_2; 2.
DR   PRINTS; PR00475; HEXOKINASE.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 4.
DR   PROSITE; PS00378; HEXOKINASE_1; 2.
DR   PROSITE; PS51748; HEXOKINASE_2; 2.
DR   Genevisible; Q3TRM8; MM.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; ATP-binding; Glycolysis; Kinase; Nucleotide-binding;
KW   Reference proteome; Repeat; Transferase.
FT   CHAIN           1..922
FT                   /note="Hexokinase-3"
FT                   /id="PRO_0000197591"
FT   DOMAIN          25..469
FT                   /note="Hexokinase 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   DOMAIN          475..911
FT                   /note="Hexokinase 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          82..218
FT                   /note="Hexokinase small subdomain 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          219..458
FT                   /note="Hexokinase large subdomain 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          529..660
FT                   /note="Hexokinase small subdomain 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          661..900
FT                   /note="Hexokinase large subdomain 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   BINDING         93..102
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         93..100
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         166
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         183..184
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         219..220
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         220
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         243
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         246
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         271
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         302..305
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         424..426
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         436..437
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         540..545
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         540..544
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         608..609
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         625..626
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P52790"
FT   BINDING         661..662
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P52790"
FT   BINDING         662
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         685
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         685
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         687..688
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P52790"
FT   BINDING         713
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P52790"
FT   BINDING         747
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P52790"
FT   BINDING         752..753
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         789..793
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         866..868
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         868..872
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         902
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   CONFLICT        203
FT                   /note="A -> S (in Ref. 1; BAE37000)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        384
FT                   /note="Y -> C (in Ref. 1; BAE29220)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        439
FT                   /note="K -> E (in Ref. 1; BAE29220)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        442
FT                   /note="V -> I (in Ref. 1; BAE29007)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        509
FT                   /note="G -> E (in Ref. 1; BAE29007)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        860
FT                   /note="T -> A (in Ref. 1; BAE29007)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   922 AA;  100101 MW;  38F4E024630C45E5 CRC64;
     MATIGPSGLH PGERASVCPH EGVPRPSGSL ELECLQQFKV TRTQLQQIQA SLLCSMEQAL
     KGQDSPAPSV RMLPTYVRST PHGTEQGDFL VLELGATGAS LRVLWVTLTG TKECRVEPRS
     REFVIPQEVI LGAGQQLFDF AARCLSEFLD AYPVENQGLK LGFNFSFPCH QTGLDRSTLI
     SWTKGFRCSG VEGQDVVQLL RDAIQRQGTY RIDVVAMVND TVGTMMGCEL GTRPCEVGLI
     VDTGTNACYM EEARHVAALD EDRGRTCVSI EWGSFYDEDA LGPVLTTFDS ALDRESLTPG
     AQRFEKMIGG LYLGELVRLV LVHLTQHGVL FDGCASPALL SQGCILLDHV AEMEDTATGT
     ARVHTILQDL GLSPRASDAE LVQYVCVAVC TRAAQLCAAA LAAVLSRLQH SREQQTLQVA
     VATGGRVFER HPRFLRILKE TVTLLAPNCD VSFIPSVDGG GRGVAMVTAV AARLAAHRRI
     LEETLAPFQL TLEQMTVVQA QMREAMIRGL QGEASSLRML PTYVRATPDG SERGDFLALD
     LGGTNFRVLL VRVAEGSVQI INQVYSIPEC RAQGSGQKLF DHIVDCIVDF QKRQGLSGQS
     LPLGFTFSFP CKQLGLDQGI LLNWTKGFNA SGCEGQDVVY LLREAIRRRQ AVELNVVAIV
     NDTVGTMMSC GYDDPRCEMG LIVGTGTNAC YMEELRNVAS VPGDSGLMCI NMEWGAFGDD
     GSLGTLSTRF DTSVDQASIN PGKQRFEKMI SGMYLGEIVR HILLHLTNLG VLFRGQKTQC
     LQARDIFKTK FLSEIESDSL ALRQVRAILE DLGLTLTSDD ALMVLEVCQA VSRRAAQLCG
     AGVAAVVEKI RENRGLQELT VSVGVDGTLY KLHPHFSKLV SATVRKLAPQ CTVTFLQSED
     GSGKGAALVT AVACRLTQMA HV
//