DGK1_DROME
ID DGK1_DROME Reviewed; 1211 AA.
AC Q01583; A8DY60; A8DY61; Q53YF9; Q7KQR7; Q8MKP0; Q9V327;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 5.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Diacylglycerol kinase 1;
DE Short=DAG kinase 1;
DE Short=DGK 1;
DE Short=Diglyceride kinase 1;
DE EC=2.7.1.107;
GN Name=Dgk; Synonyms=DGK1; ORFNames=CG34361;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM G), FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R;
RX PubMed=1321433; DOI=10.1073/pnas.89.13.6030;
RA Masai I., Hosoya T., Kojima S., Hotta Y.;
RT "Molecular cloning of a Drosophila diacylglycerol kinase gene that is
RT expressed in the nervous system and muscle.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:6030-6034(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S; TISSUE=Embryo;
RX PubMed=8380995; DOI=10.1042/bj2890439;
RA Harden N., Yap S.F., Chiam M.-A., Lim L.;
RT "A Drosophila gene encoding a protein with similarity to diacylglycerol
RT kinase is expressed in specific neurons.";
RL Biochem. J. 289:439-444(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM G).
RC STRAIN=Berkeley; TISSUE=Testis;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Upon cell stimulation converts the second messenger
CC diacylglycerol into phosphatidate, initiating the resynthesis of
CC phosphatidylinositols and attenuating protein kinase C activity (By
CC similarity). May have a role in the development of the embryonic
CC nervous system and the function of the adult nervous system and muscle;
CC regulating signal transduction in neurons. {ECO:0000250,
CC ECO:0000269|PubMed:1321433, ECO:0000269|PubMed:8380995}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-
CC phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608,
CC ChEBI:CHEBI:456216; EC=2.7.1.107;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=E;
CC IsoId=Q01583-4; Sequence=Displayed;
CC Name=C;
CC IsoId=Q01583-3; Sequence=VSP_017884;
CC Name=F;
CC IsoId=Q01583-1; Sequence=VSP_033247;
CC Name=G;
CC IsoId=Q01583-2; Sequence=VSP_017885, VSP_017886, VSP_017887;
CC -!- TISSUE SPECIFICITY: In 10-11 hours embryos, expression is abundant in a
CC limited number of cells in the procephalic region and in the ventral
CC nerve cord. Predominantly expressed in the adult nervous system and
CC muscle: including compound eyes, brain cortex, fibrillar muscle, and
CC tubular muscle. {ECO:0000269|PubMed:1321433,
CC ECO:0000269|PubMed:8380995}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the embryonic, pupal and adult
CC stages, with little expression during the larval stages.
CC {ECO:0000269|PubMed:1321433, ECO:0000269|PubMed:8380995}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000305}.
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DR EMBL; D11120; BAA01894.1; -; mRNA.
DR EMBL; X67335; CAA47750.1; -; mRNA.
DR EMBL; AE013599; AAF59180.1; -; Genomic_DNA.
DR EMBL; AE013599; AAS64897.1; -; Genomic_DNA.
DR EMBL; AE013599; ABV53719.1; -; Genomic_DNA.
DR EMBL; AE013599; ABV53720.1; -; Genomic_DNA.
DR EMBL; BT003323; AAO25083.1; -; mRNA.
DR PIR; A46140; A46140.
DR PIR; B46140; B46140.
DR RefSeq; NP_001097219.1; NM_001103749.2. [Q01583-4]
DR RefSeq; NP_001097220.1; NM_001103750.3. [Q01583-1]
DR RefSeq; NP_523654.2; NM_078930.4. [Q01583-2]
DR RefSeq; NP_995775.2; NM_206053.2.
DR AlphaFoldDB; Q01583; -.
DR IntAct; Q01583; 1.
DR STRING; 7227.FBpp0300813; -.
DR BindingDB; Q01583; -.
DR ChEMBL; CHEMBL1075068; -.
DR PaxDb; Q01583; -.
DR PRIDE; Q01583; -.
DR DNASU; 35738; -.
DR EnsemblMetazoa; FBtr0112579; FBpp0111491; FBgn0085390. [Q01583-2]
DR EnsemblMetazoa; FBtr0112580; FBpp0111492; FBgn0085390. [Q01583-4]
DR EnsemblMetazoa; FBtr0112581; FBpp0111493; FBgn0085390. [Q01583-1]
DR GeneID; 35738; -.
DR KEGG; dme:Dmel_CG34361; -.
DR CTD; 35738; -.
DR FlyBase; FBgn0085390; Dgk.
DR VEuPathDB; VectorBase:FBgn0085390; -.
DR eggNOG; KOG0696; Eukaryota.
DR eggNOG; KOG1169; Eukaryota.
DR GeneTree; ENSGT00940000168305; -.
DR InParanoid; Q01583; -.
DR PhylomeDB; Q01583; -.
DR BRENDA; 2.7.1.107; 1994.
DR Reactome; R-DME-114508; Effects of PIP2 hydrolysis.
DR BioGRID-ORCS; 35738; 0 hits in 3 CRISPR screens.
DR ChiTaRS; rdgA; fly.
DR GenomeRNAi; 35738; -.
DR PRO; PR:Q01583; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0085390; Expressed in embryonic Malpighian tubule (Drosophila) and 36 other tissues.
DR ExpressionAtlas; Q01583; baseline and differential.
DR Genevisible; Q01583; DM.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004143; F:diacylglycerol kinase activity; IDA:FlyBase.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0046339; P:diacylglycerol metabolic process; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0046834; P:lipid phosphorylation; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IDA:FlyBase.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR CDD; cd00029; C1; 2.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 1.10.238.110; -; 2.
DR Gene3D; 3.40.50.10330; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR029477; DAG_kinase_typeI_N.
DR InterPro; IPR037607; DGK.
DR InterPro; IPR038199; DGK_typeI_N_sf.
DR InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR PANTHER; PTHR11255; PTHR11255; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF14513; DAG_kinase_N; 1.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF111331; SSF111331; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR SUPFAM; SSF57889; SSF57889; 2.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Calcium; Kinase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Repeat; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..1211
FT /note="Diacylglycerol kinase 1"
FT /id="PRO_0000218473"
FT DOMAIN 286..321
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 331..366
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 548..682
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT ZN_FING 382..432
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 449..498
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 174..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..841
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..958
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 299
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 301
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 303
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 310
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 344
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 346
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 348
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 350
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 355
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VAR_SEQ 1..698
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:8380995"
FT /id="VSP_017884"
FT VAR_SEQ 2..73
FT /note="NIGIAAPKWDKLSPREFLQLQELASYSTRKLQDVLREFSSPSAASTPKCIPD
FT GDIDFDGFRRFLDAFLDCEA -> RWELRYGWQIVTFRTNCATAAAVACHQLLCPVSLT
FT SAVEIMPNSFPPEGRRRERRSGNLVLRAGCCCIGKYF (in isoform G)"
FT /evidence="ECO:0000303|PubMed:1321433, ECO:0000303|Ref.5"
FT /id="VSP_017885"
FT VAR_SEQ 74..485
FT /note="Missing (in isoform G)"
FT /evidence="ECO:0000303|PubMed:1321433, ECO:0000303|Ref.5"
FT /id="VSP_017886"
FT VAR_SEQ 121..250
FT /note="GSIPNINSIAELMPQCSGGGGGIGGTGGVAGAEGHAQARSSFVDKIHGITDK
FT LHHSLGGHLSHDPSKTGSVHPMLTVTPSPLASGPSMFQASNPARRSVDSSPSHSATNHS
FT QMSRNSSKKSSNSVNCKID -> AVSRILPAIGRHCPGSLESGSAQAEKR (in
FT isoform F)"
FT /evidence="ECO:0000305"
FT /id="VSP_033247"
FT VAR_SEQ 530..537
FT /note="Missing (in isoform G)"
FT /evidence="ECO:0000303|PubMed:1321433, ECO:0000303|Ref.5"
FT /id="VSP_017887"
FT CONFLICT 794
FT /note="M -> T (in Ref. 1; BAA01894)"
FT /evidence="ECO:0000305"
FT CONFLICT 863
FT /note="Q -> QQQQQ (in Ref. 2; CAA47750)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1211 AA; 132960 MW; CC58412EE1E8F762 CRC64;
MNIGIAAPKW DKLSPREFLQ LQELASYSTR KLQDVLREFS SPSAASTPKC IPDGDIDFDG
FRRFLDAFLD CEAPLDLAKH LFVSFLKPNV TQAQLHGRAL NQMAAISSTA ACAPVTSHTK
GSIPNINSIA ELMPQCSGGG GGIGGTGGVA GAEGHAQARS SFVDKIHGIT DKLHHSLGGH
LSHDPSKTGS VHPMLTVTPS PLASGPSMFQ ASNPARRSVD SSPSHSATNH SQMSRNSSKK
SSNSVNCKID ADIKLLARKL SHFDPLTLKV PLKDVVCYLS LLEAGRPEDK LEFMFRLYDT
DSNGVLDTAE MDAIVNQMMA VAEYLGWDVS ELRPILQEMM VEIDYDADGT VSLDEWQRGG
MTTIPLLVLL GVDSTTLKED GIHVWRLKHF SKPAYCNLCL NMLVGLGKKG LCCVLCKYTV
HERCVQHAPA SCITTYVKSK KPKCGGDLLH HWVEGNCYGR CSKCRKRIKA YHGITGLTCR
WCHMMLHNRC ASSVKKECTL GEYSELIVPP TAICPAVLDR QRSVNQAHKK SQMHHHQATH
FQITPPDELS CPLLVFVNPK SGGRQGDRIL RKFQYMLNPR QVYDLSKGGP KEGLTLFKDL
PRFRVICCGG DGTVGWVLEA MDSIELASQP AIGVIPLGTG NDLARCLRWG GGYEGENIPK
LMDKFRRAST VMLDRWSIEV TNTPHSDDMR PKVTLHSNMQ KVIELSQSVV VDKSLMERFE
EIQRQSKQVA TSMGTAASST SIMMASKTET EMETMATMEF GSSTTTTNRT TTTKSISMST
FETQCLQQTL RTAMSSSSSN TSSGSPCNGN QDAETEVDSH AAAAADVREK SVPRRSGETE
KQSLETLLLQ HKQQMQQQQQ QQQQGVTSLA VEEAATATPV GSNQSDNSSQ RNKQNNILKQ
QITLSLDLSD HEDEPKDDGG GAGDGTKSNG NSIPATPATP ITPTTPNAAS SVLQQQQQQH
LQFEQQQKPI KVQSDKDCTV PYNIINNYFS VGVDAAICVK FHLEREKNPH KFNSRMKNKL
WYFEYATSET FAASCKNLHE SIEIVCDGVA LDLANGPHLQ GVALLNIPYT HGGSNLWGEH
LSQKRIRKSA GPFGKSKKLR AGDKEFSATS FNSVDLSVAI QDFGDRLIEV IGLENCLHMG
QVRTGLRASG RRLAQCSEVI IKTKKTFPMQ IDGEPWMQMP CTIKVTHKNQ VPMLMAPRSE
KGRGFFNLLC S
