DGK2_DROME
ID DGK2_DROME Reviewed; 1457 AA.
AC Q09103; A8JV38; A8JV40; Q0KHU7; Q7YU71; Q8SY47; Q9W3A4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Eye-specific diacylglycerol kinase;
DE Short=DAG kinase 2;
DE Short=DGK 2;
DE Short=Diglyceride kinase 2;
DE EC=2.7.1.107;
DE AltName: Full=Retinal degeneration A protein;
GN Name=rdgA; Synonyms=DGK2; ORFNames=CG34344;
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 A), FUNCTION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=Canton-S; TISSUE=Head;
RX PubMed=8248222; DOI=10.1073/pnas.90.23.11157;
RA Masai I., Okazaki A., Hosoya T., Hotta Y.;
RT "Drosophila retinal degeneration A gene encodes an eye-specific
RT diacylglycerol kinase with cysteine-rich zinc-finger motifs and ankyrin
RT repeats.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:11157-11161(1993).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Head;
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 (AUG-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for the maintenance of phospholipid turnover within
CC the photoreceptor. {ECO:0000269|PubMed:8248222}.
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 -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A;
CC IsoId=Q09103-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q09103-3; Sequence=VSP_030264, VSP_030266, VSP_028732,
CC VSP_028733;
CC Name=C;
CC IsoId=Q09103-2; Sequence=VSP_030265, VSP_030267;
CC -!- TISSUE SPECIFICITY: Expressed specifically in adult eye.
CC {ECO:0000269|PubMed:8248222}.
CC -!- DISRUPTION PHENOTYPE: Flies exhibit photoreceptor cells that degenerate
CC within a week after eclosion. {ECO:0000269|PubMed:8248222}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ22428.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; D17315; BAA04135.1; -; mRNA.
DR EMBL; AE014298; AAF46430.2; -; Genomic_DNA.
DR EMBL; AE014298; ABW09364.1; -; Genomic_DNA.
DR EMBL; AE014298; ABW09365.1; -; Genomic_DNA.
DR EMBL; AY075349; AAL68208.1; -; mRNA.
DR EMBL; BT009959; AAQ22428.1; ALT_SEQ; mRNA.
DR PIR; T13709; T13709.
DR RefSeq; NP_001096916.1; NM_001103446.2. [Q09103-3]
DR RefSeq; NP_001096917.1; NM_001103447.4. [Q09103-2]
DR RefSeq; NP_511092.2; NM_078537.3. [Q09103-1]
DR AlphaFoldDB; Q09103; -.
DR SMR; Q09103; -.
DR BioGRID; 58282; 21.
DR IntAct; Q09103; 4.
DR STRING; 7227.FBpp0305778; -.
DR PaxDb; Q09103; -.
DR PRIDE; Q09103; -.
DR DNASU; 31826; -.
DR EnsemblMetazoa; FBtr0302660; FBpp0291800; FBgn0261549. [Q09103-1]
DR EnsemblMetazoa; FBtr0302661; FBpp0291801; FBgn0261549. [Q09103-3]
DR EnsemblMetazoa; FBtr0302662; FBpp0291802; FBgn0261549. [Q09103-2]
DR GeneID; 31826; -.
DR KEGG; dme:Dmel_CG42667; -.
DR CTD; 31826; -.
DR FlyBase; FBgn0261549; rdgA.
DR VEuPathDB; VectorBase:FBgn0261549; -.
DR eggNOG; KOG0782; Eukaryota.
DR GeneTree; ENSGT00940000167477; -.
DR InParanoid; Q09103; -.
DR PhylomeDB; Q09103; -.
DR BRENDA; 2.7.1.107; 1994.
DR Reactome; R-DME-114508; Effects of PIP2 hydrolysis.
DR SABIO-RK; Q09103; -.
DR SignaLink; Q09103; -.
DR BioGRID-ORCS; 31826; 0 hits in 3 CRISPR screens.
DR ChiTaRS; rdgA; fly.
DR GenomeRNAi; 31826; -.
DR PRO; PR:Q09103; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0261549; Expressed in brain and 21 other tissues.
DR ExpressionAtlas; Q09103; baseline and differential.
DR Genevisible; Q09103; DM.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004143; F:diacylglycerol kinase activity; ISS:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0016059; P:deactivation of rhodopsin mediated signaling; IGI:FlyBase.
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:0006654; P:phosphatidic acid biosynthetic process; TAS:FlyBase.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:FlyBase.
DR GO; GO:0045494; P:photoreceptor cell maintenance; TAS:FlyBase.
DR GO; GO:0007602; P:phototransduction; IMP:FlyBase.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; IMP:FlyBase.
DR GO; GO:0007608; P:sensory perception of smell; IMP:FlyBase.
DR GO; GO:0007605; P:sensory perception of sound; IMP:FlyBase.
DR GO; GO:0043052; P:thermotaxis; IDA:FlyBase.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd00029; C1; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.40.50.10330; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR037607; DGK.
DR InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR PANTHER; PTHR11255; PTHR11255; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR SMART; SM00248; ANK; 4.
DR SMART; SM00109; C1; 1.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50146; DAGK; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ANK repeat; ATP-binding; Kinase; Membrane;
KW Metal-binding; Nucleotide-binding; Reference proteome; Repeat;
KW Sensory transduction; Transferase; Vision; Zinc; Zinc-finger.
FT CHAIN 1..1457
FT /note="Eye-specific diacylglycerol kinase"
FT /id="PRO_0000218474"
FT DOMAIN 808..944
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT REPEAT 1320..1349
FT /note="ANK 1"
FT REPEAT 1353..1382
FT /note="ANK 2"
FT REPEAT 1389..1418
FT /note="ANK 3"
FT REPEAT 1422..1451
FT /note="ANK 4"
FT ZN_FING 591..641
FT /note="Phorbol-ester/DAG-type 1"
FT ZN_FING 661..724
FT /note="Phorbol-ester/DAG-type 2"
FT REGION 1..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1264..1302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..257
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..132
FT /note="MQQQQQPSIDQLPEPTASTSNSATTKPTIATATTSTTTTSGNNFHQQLQATT
FT AATMQRLRTTFTRSRTPTGAEMKMQNSLEVPKQVRSASFDEMQLESQRASSSLLKQQSS
FT SSASADERSSEAGFLQVPLAA -> MERLLHAVREEFQTEDEYETEVDDEGNVLHRSSI
FT SSCSSSSSSSNTSSSSDGSNSTASQPLSPSLPQPRRRLQRSDSFGSVGGGVAGGVAGSG
FT ATGAGGVRRFRRSSIGMQRKSAFRQRKLDSLGAWRRKRR (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_030265"
FT VAR_SEQ 1..116
FT /note="MQQQQQPSIDQLPEPTASTSNSATTKPTIATATTSTTTTSGNNFHQQLQATT
FT AATMQRLRTTFTRSRTPTGAEMKMQNSLEVPKQVRSASFDEMQLESQRASSSLLKQQSS
FT SSASA -> MPERSISQRDLDEIEIESDEEEEELEQGVGLSTRSRRNRRGASDSPAASR
FT ARNATNGIQNRGRERERERERERSRERFGGTNAADEARFYDDEEQRMEDDGEEDSDEDI
FT EMLDYDT (in isoform B)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_030264"
FT VAR_SEQ 117..564
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_030266"
FT VAR_SEQ 133..565
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_030267"
FT VAR_SEQ 1315
FT /note="S -> SNKDRLFSFNEDVFGCGFS (in isoform B)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_028732"
FT VAR_SEQ 1445..1457
FT /note="KQGTQPVDGWLDD -> QERFMHLEKQTRI (in isoform B)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_028733"
FT CONFLICT 32
FT /note="A -> V (in Ref. 1; BAA04135)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="S -> T (in Ref. 1; BAA04135)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="N -> K (in Ref. 1; BAA04135)"
FT /evidence="ECO:0000305"
FT CONFLICT 565
FT /note="R -> RR (in Ref. 1; BAA04135)"
FT /evidence="ECO:0000305"
FT CONFLICT 667
FT /note="K -> N (in Ref. 1; BAA04135)"
FT /evidence="ECO:0000305"
FT CONFLICT 679..684
FT /note="Missing (in Ref. 1; BAA04135)"
FT /evidence="ECO:0000305"
FT CONFLICT 778
FT /note="G -> GGG (in Ref. 1; BAA04135)"
FT /evidence="ECO:0000305"
FT CONFLICT 924
FT /note="L -> M (in Ref. 5; AAQ22428)"
FT /evidence="ECO:0000305"
FT CONFLICT 983
FT /note="E -> G (in Ref. 5; AAQ22428)"
FT /evidence="ECO:0000305"
FT CONFLICT 1128
FT /note="I -> N (in Ref. 5; AAQ22428)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1457 AA; 160142 MW; 8F4E33E9C1B665D1 CRC64;
MQQQQQPSID QLPEPTASTS NSATTKPTIA TATTSTTTTS GNNFHQQLQA TTAATMQRLR
TTFTRSRTPT GAEMKMQNSL EVPKQVRSAS FDEMQLESQR ASSSLLKQQS SSSASADERS
SEAGFLQVPL AAHQQRSHSF DSATASAGSD DSGTFLEVPR RLKARRSSST KTPPPCIHCH
YLEEYERRMT AEQRYFIDHR ELTALSYSNT SSEASEDEDE VEGHNAEEEE EGSAAIEDAE
EETTEAATEE ADEDPRTEVE SEHDHDPDDD AALEMDIRIG NMSQGSSIEE SRARLPRQMR
RHTIGSSSVT SASEDEGLEG SDNGSPHFGN TLLPPQPTTP CGITFTLSPT NGDYPSPPHL
PLDPGSPPIS PCSSNSGRLP ALAPIISTPC SSADADDAGA AMGLPVRARR RSISRQEAIF
VEPTGNSLEN VSHEEVDNSN TKSSVDTADS LDEASTMATC GSPGAAGGSG ASSSHHNAFV
VRDIYLMVPD LKRDRAASVD SCFSKLSSNA KTEELQPSAD GCFLTVPNIN ATRSRSVDIV
LPTDEQARYK ALSMTGSTVT YADGRTASAS NSRRPIRIVP DWTENAVQGE HYWKPTSASG
DLCCLNEECI KSGQRMKCSA CQLVAHHNCI PFVNEKSTLA CKPTYRDVGI RQYREQTTTH
HHWVHRKLEK GKCKQCGKFF PMKQAVQSKL FGSKEIVALA CAWCHEIYHN KEACFNQAKI
GEECRLGNYA PIIVPPSWIV KLPTKGNFKS SIRVSNKNNA ASGSGGGGAG GGAGGGGGKS
KKQTQRRQKG KEEKKEPRAF IVKPIPSPEV IPVIVFINPK SGGNQGHKLL GKFQHLLNPR
QVFDLTQGGP KMGLDMFRKA PNLRVLACGG DGTVGWVLSV LDQIQPPLQP APAVGVLPLG
TGNDLARALG WGGGYTDEPI GKILREIGMS QCVLMDRWRV KVTPNDDVTD DHVDRSKPNV
PLNVINNYFS FGVDAHIALE FHEAREAHPE RFNSRLRNKM YYGQMGGKDL ILRQYRNLSQ
WVTLECDGQD FTGKLRDAGC HAVLFLNIPS YGGGTHPWND SFGASKPSID DGLMEVVGLT
TYQLPMLQAG MHGTCICQCR KARIITKRTI PMQVDGEACR VKPSVIEIEL LNKALMLSKR
KHGRGDVQVN PLEKMQLHIL RVTMQQYEQY HYDKEMLRKL ANKLGQIEIE SQCDLEHVRN
MLNTKFEESI SYPKVSQDWC FIDSCTAEHY FRIDRAQEHL HYICDIAIDE LYILDHEAAT
MPQTPDQERS FAAFSQRQAQ NERRQMDQAQ GRGPGSTDED LQIGSKPIKV MKWKSPILEQ
TSDAILLAAQ SGDLNMLRAL HEQGYSLQSV NKNGQTALHF ACKYNHRDIV KYIIASATRR
LINMADKELG QTALHIAAEQ NRRDICVMLV AAGAHLDTLD SGGNTPMMVA FNKNANEIAT
YLESKQGTQP VDGWLDD
