ID HKDC1_MOUSE Reviewed; 915 AA.
AC Q91W97; Q3UKJ9;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 24-JAN-2024, entry version 139.
DE RecName: Full=Hexokinase HKDC1 {ECO:0000305};
DE EC=2.7.1.1 {ECO:0000250|UniProtKB:Q2TB90};
DE AltName: Full=Hexokinase domain-containing protein 1 {ECO:0000305};
GN Name=Hkdc1 {ECO:0000312|MGI:MGI:2384910};
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; TISSUE=Placenta;
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 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=25648650; DOI=10.1038/ncomms7069;
RA Guo C., Ludvik A.E., Arlotto M.E., Hayes M.G., Armstrong L.L.,
RA Scholtens D.M., Brown C.D., Newgard C.B., Becker T.C., Layden B.T.,
RA Lowe W.L., Reddy T.E.;
RT "Coordinated regulatory variation associated with gestational
RT hyperglycaemia regulates expression of the novel hexokinase HKDC1.";
RL Nat. Commun. 6:6069-6069(2015).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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 [5]
RP FUNCTION.
RX PubMed=30543855; DOI=10.1016/j.bbadis.2018.11.022;
RA Khan M.W., Priyadarshini M., Cordoba-Chacon J., Becker T.C., Layden B.T.;
RT "Hepatic hexokinase domain containing 1 (HKDC1) improves whole body glucose
RT tolerance and insulin sensitivity in pregnant mice.";
RL Biochim. Biophys. Acta 1865:678-687(2019).
RN [6]
RP TISSUE SPECIFICITY, 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 (By
CC similarity). Has low glucose phosphorylating activity compared to other
CC hexokinases (By similarity). Involved in glucose homeostasis and
CC hepatic lipid accumulation (PubMed:30543855). Required to maintain
CC whole-body glucose homeostasis during pregnancy; however additional
CC evidences are required to confirm this role (PubMed:25648650,
CC PubMed:27459389). {ECO:0000250|UniProtKB:Q2TB90,
CC ECO:0000269|PubMed:25648650, ECO:0000269|PubMed:27459389,
CC ECO:0000269|PubMed:30543855}.
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:Q2TB90};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741;
CC Evidence={ECO:0000250|UniProtKB:Q2TB90};
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:Q2TB90};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826;
CC Evidence={ECO:0000250|UniProtKB:Q2TB90};
CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC {ECO:0000250|UniProtKB:Q2TB90}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 1/4.
CC {ECO:0000250|UniProtKB:Q2TB90}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q2TB90}.
CC Mitochondrion membrane {ECO:0000250|UniProtKB:Q2TB90}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:Q2TB90}. Photoreceptor inner
CC segment {ECO:0000269|PubMed:30085091}. Note=The mitochondrial-binding
CC peptide (MBP) region promotes association with the mitochondrion.
CC {ECO:0000250|UniProtKB:Q2TB90}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Detected in retina, brain,
CC cerebellum, liver, lung, kidney, spleen, pancreas and intestine
CC (PubMed:30085091). {ECO:0000269|PubMed:27459389,
CC ECO:0000269|PubMed:30085091}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality.
CC {ECO:0000269|PubMed:27459389}.
CC -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01084, ECO:0000305}.
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DR EMBL; AK145980; BAE26802.1; -; mRNA.
DR EMBL; BC016235; AAH16235.1; -; mRNA.
DR CCDS; CCDS23888.1; -.
DR RefSeq; NP_663394.1; NM_145419.1.
DR AlphaFoldDB; Q91W97; -.
DR SMR; Q91W97; -.
DR BioGRID; 229687; 7.
DR IntAct; Q91W97; 1.
DR STRING; 10090.ENSMUSP00000020277; -.
DR iPTMnet; Q91W97; -.
DR PhosphoSitePlus; Q91W97; -.
DR EPD; Q91W97; -.
DR jPOST; Q91W97; -.
DR MaxQB; Q91W97; -.
DR PaxDb; 10090-ENSMUSP00000020277; -.
DR PeptideAtlas; Q91W97; -.
DR ProteomicsDB; 273146; -.
DR Pumba; Q91W97; -.
DR Antibodypedia; 2524; 178 antibodies from 26 providers.
DR DNASU; 216019; -.
DR Ensembl; ENSMUST00000020277.9; ENSMUSP00000020277.9; ENSMUSG00000020080.9.
DR GeneID; 216019; -.
DR KEGG; mmu:216019; -.
DR UCSC; uc007fhc.1; mouse.
DR AGR; MGI:2384910; -.
DR CTD; 80201; -.
DR MGI; MGI:2384910; Hkdc1.
DR VEuPathDB; HostDB:ENSMUSG00000020080; -.
DR eggNOG; KOG1369; Eukaryota.
DR GeneTree; ENSGT00950000182787; -.
DR HOGENOM; CLU_014393_1_0_1; -.
DR InParanoid; Q91W97; -.
DR OMA; PNEITRG; -.
DR OrthoDB; 5481886at2759; -.
DR PhylomeDB; Q91W97; -.
DR TreeFam; TF314238; -.
DR Reactome; R-MMU-70171; Glycolysis.
DR UniPathway; UPA00109; UER00180.
DR UniPathway; UPA00242; -.
DR BioGRID-ORCS; 216019; 2 hits in 79 CRISPR screens.
DR PRO; PR:Q91W97; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q91W97; Protein.
DR Bgee; ENSMUSG00000020080; Expressed in kidney calyx and 90 other cell types or tissues.
DR Genevisible; Q91W97; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; 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; ISS:UniProtKB.
DR GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR GO; GO:0046835; P:carbohydrate phosphorylation; IBA:GO_Central.
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; IMP:UniProtKB.
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:SF28; HEXOKINASE HKDC1; 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; 1.
DR PROSITE; PS51748; HEXOKINASE_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Membrane; Mitochondrion;
KW Nucleotide-binding; Reference proteome; Repeat; Transferase.
FT CHAIN 1..915
FT /note="Hexokinase HKDC1"
FT /id="PRO_0000299036"
FT DOMAIN 16..458
FT /note="Hexokinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT DOMAIN 464..903
FT /note="Hexokinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 1..20
FT /note="Mitochondrial-binding peptide (MBP)"
FT /evidence="ECO:0000250|UniProtKB:Q2TB90"
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..652
FT /note="Hexokinase small subdomain 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 653..892
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 600..601
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 617..618
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 653..654
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 654
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 677
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 677
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..680
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 705
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 739
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 744..745
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 781..785
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 858..860
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 860..864
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 894
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT CONFLICT 208
FT /note="N -> D (in Ref. 1; BAE26802)"
FT /evidence="ECO:0000305"
FT CONFLICT 745
FT /note="M -> T (in Ref. 1; BAE26802)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 915 AA; 102259 MW; 1AE1506A9AC0228A CRC64;
MFAVHLVAFY FTKLKEDQIK KVDRFLYHMR LSDETLVDIM ARFQAEMEKG LGKDTNPTAS
VKMLPTFVRA IPDGSENGEF LSLDLGGSKF RVLKVQVSQE GQQNVQMESQ FYPMPNEITR
GNGTELFDYV ADCLADFMKT KNLTHKKLPL GFTFSFPCRQ NKLEEGVLLS WTKKFKARGV
QDTDVVNRLA TAMKKHKDLD VDILALVNDT VGTMMTCAYD DPNCEVGVII GTGTNACYME
DMSNIDLVEG DEGRMCINTE WGAFGDDGAL EDIRTEFDRE LDLGSLNPGK QLFEKMISGL
YMGELVRLIL LKMAKVGLLF GGAKSSALHT KGKIETQHVA AMEMSKEGLA NTREILVDLG
LEPSESDCIA VQHVCTIVSF RSANLCAAAL ATILTRLREN KKLARLRTTV GMDGTLYKTH
PQYPKRLHKV VRRLVPNCDV RFLLSESGST KGAAMVTAVA SRVQAQRKQI DKVLALFQLT
REQLLGVRDK MRAELEYGLK KKTHSLATVK MLPTYVYGMP DGTEKGKFLA LDLGGTNFRV
LLVKIRRRSV RMYNKIFAIP LEIMQGTGEE LFDHIVQCIA DFLDYMGLKG AQLPLGFTFS
FPCRQTCIDK GTLVGWTKGF KATDCEGEDV VDMLREAIKR RNEFDLDIVA IVNDTVGTMM
TCGYEDPRCE IGLIAGTGSN VCYMEEMRNI ELVDGDEGRM CVNTEWGGFG DNGCIDDIRT
QYDKEVDEGS LNAGKQRYEK MTSGMYLGEI VRRILIDLTR QGLLFRGQIS ERLRTRGIFE
TKFLSQIESD RLALLQVRRI LQQLGLDSTC EDSIVVKEVC GAVSRRAAQM CGAGMAAIVE
KRREDQGLQH FKVTVGVDGT LYKLHPHFSR ILQETVKELA PQCDVTFMLS EDGSGKGAAL
ITAVAKRLQQ PRKDI
//
