GenomeNet

Database: UniProt
Entry: Q9VCF2_DROME
LinkDB: Q9VCF2_DROME
Original site: Q9VCF2_DROME 
ID   Q9VCF2_DROME            Unreviewed;      1564 AA.
AC   Q9VCF2;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 2.
DT   27-MAR-2024, entry version 177.
DE   RecName: Full=Diacylglycerol kinase {ECO:0000256|RuleBase:RU361128};
DE            Short=DAG kinase {ECO:0000256|RuleBase:RU361128};
DE            EC=2.7.1.107 {ECO:0000256|RuleBase:RU361128};
GN   Name=CG5875 {ECO:0000313|EMBL:AAF56214.2};
GN   Synonyms=CG13600 {ECO:0000313|EMBL:AAF56214.2}, CG31452
GN   {ECO:0000313|EMBL:AAF56214.2}, DGKt {ECO:0000313|EMBL:AAF56214.2},
GN   Dmel\CG31140 {ECO:0000313|EMBL:AAF56214.2};
GN   ORFNames=CG31140 {ECO:0000313|EMBL:AAF56214.2,
GN   ECO:0000313|FlyBase:FBgn0051140}, Dmel_CG31140
GN   {ECO:0000313|EMBL:AAF56214.2};
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 {ECO:0000313|EMBL:AAF56214.2, ECO:0000313|Proteomes:UP000000803};
RN   [1] {ECO:0000313|EMBL:AAF56214.2, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J., 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., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA   Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA   Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA   Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA   Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA   Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA   Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2] {ECO:0000313|EMBL:AAF56214.2, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537568;
RA   Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA   Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA   George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA   Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA   Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA   Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT   "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT   euchromatic genome sequence.";
RL   Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN   [3] {ECO:0000313|EMBL:AAF56214.2, ECO:0000313|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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] {ECO:0000313|EMBL:AAF56214.2, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537573;
RA   Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA   Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA   Celniker S.E.;
RT   "The transposable elements of the Drosophila melanogaster euchromatin: a
RT   genomics perspective.";
RL   Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN   [5] {ECO:0000313|EMBL:AAF56214.2, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537574;
RA   Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA   Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA   Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA   Karpen G.H.;
RT   "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL   Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN   [6] {ECO:0000313|EMBL:AAF56214.2, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA   Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA   Ashburner M., Anxolabehere D.;
RT   "Combined evidence annotation of transposable elements in genome
RT   sequences.";
RL   PLoS Comput. Biol. 1:166-175(2005).
RN   [7] {ECO:0000313|EMBL:AAF56214.2, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569856; DOI=10.1126/science.1139815;
RA   Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT   "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL   Science 316:1586-1591(2007).
RN   [8] {ECO:0000313|EMBL:AAF56214.2, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569867; DOI=10.1126/science.1139816;
RA   Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA   Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA   Dimitri P., Karpen G.H., Celniker S.E.;
RT   "Sequence finishing and mapping of Drosophila melanogaster
RT   heterochromatin.";
RL   Science 316:1625-1628(2007).
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         Evidence={ECO:0000256|ARBA:ARBA00001383,
CC         ECO:0000256|RuleBase:RU361128};
CC   -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC       {ECO:0000256|ARBA:ARBA00009280, ECO:0000256|RuleBase:RU361128}.
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DR   EMBL; AE014297; AAF56214.2; -; Genomic_DNA.
DR   RefSeq; NP_651199.2; NM_142942.6.
DR   SMR; Q9VCF2; -.
DR   PaxDb; 7227-FBpp0083885; -.
DR   DNASU; 42836; -.
DR   EnsemblMetazoa; FBtr0084497; FBpp0083885; FBgn0051140.
DR   GeneID; 42836; -.
DR   UCSC; CG31140-RA; d. melanogaster.
DR   AGR; FB:FBgn0051140; -.
DR   FlyBase; FBgn0051140; CG31140.
DR   VEuPathDB; VectorBase:FBgn0051140; -.
DR   eggNOG; KOG1169; Eukaryota.
DR   GeneTree; ENSGT00940000159492; -.
DR   OrthoDB; 4642163at2759; -.
DR   PhylomeDB; Q9VCF2; -.
DR   BioGRID-ORCS; 42836; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; CG31140; fly.
DR   GenomeRNAi; 42836; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0051140; Expressed in brain and 17 other cell types or tissues.
DR   ExpressionAtlas; Q9VCF2; baseline and differential.
DR   Genevisible; Q9VCF2; DM.
DR   GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR   GO; GO:0005634; C:nucleus; ISS:FlyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; ISS:FlyBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0046339; P:diacylglycerol metabolic process; IBA:GO_Central.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:FlyBase.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0046834; P:lipid phosphorylation; IBA:GO_Central.
DR   GO; GO:0070528; P:protein kinase C signaling; ISS:FlyBase.
DR   GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR   CDD; cd20803; C1_DGKtheta_typeV_rpt1; 1.
DR   CDD; cd20804; C1_DGKtheta_typeV_rpt2; 1.
DR   CDD; cd20854; C1_DGKtheta_typeV_rpt3; 1.
DR   CDD; cd17111; RA1_DAGK-theta; 1.
DR   CDD; cd01783; RA2_DAGK-theta; 1.
DR   Gene3D; 2.60.200.40; -; 1.
DR   Gene3D; 3.30.60.20; -; 2.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR020454; DAG/PE-bd.
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   InterPro; IPR000159; RA_dom.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR   PANTHER; PTHR11255:SF54; DIACYLGLYCEROL KINASE THETA; 1.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF00609; DAGK_acc; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   Pfam; PF00788; RA; 2.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 3.
DR   SMART; SM00045; DAGKa; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SMART; SM00314; RA; 2.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 3.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 2.
DR   PROSITE; PS50146; DAGK; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 3.
PE   1: Evidence at protein level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361128};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361128};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361128};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:Q9VCF2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          5..55
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          68..116
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          134..185
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          923..1024
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          1115..1273
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
FT   REGION          268..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          367..399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          417..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          476..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          686..710
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          732..828
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1274..1321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..300
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..324
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..445
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..463
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        494..523
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        549..571
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        738..763
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        807..828
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1299..1321
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1564 AA;  171673 MW;  9A9B143D69B048D4 CRC64;
     MADGGHSFVK KTFHKPTYCH HCSDLLWGLI QQGYICEVCN FIIHERCVSS VVTPCSGIAP
     CIIKNPVAHC WSEPTHHKRK FCTVCRKRLD ETPAVHCLVC EYFAHIECQD FAVPDCTENA
     TYVPGKELLN VKHQHHWREG NLPSTSKCAY CKKTCWSSEC LTGYRCEWCG MTTHAGCRMY
     LPTECNFGIL QPIYLPPHSV SIPRTEVPIE AIIGVQVKSK TSLVRDYSCP SPDLSCPIPG
     AGSGSLTSLG LKELLELHRQ RLEQSKQHFL LSTPPTPTSC GSISLCHSPT PSSLTVGETS
     NEAEQDRERD QDQPEEEPEE ENTEQDSALQ LTTSTSNVIG NLQKWPSANS SLHLLYTNLF
     RKLGQGKRRR KRGISSGGLS PSEDEDDVDG GVCDISGGDL SDDYDHCDVA LRRRSLRSRQ
     PRDVSETDYH GDAEAEAEGE TVPRESCYET SDTGGELTNT DDLDSSLNLI SNLSYNSSNN
     SNACNVPGGA TAPDARNTAT TSTTAPGKSG HALSVQGGRQ QPKTGALAQI KPKPKPILMP
     KHKAQGKGGS LSSPLSNSNS SDCSSASPSA PATLLQLSPV GRSKSFQESA AITAVSRYKK
     YGRGLFQRRR SKRSPKNAVG VGGKSNYSLD RLSQNIEITI QDEDGNFHPY DDNYHMLAGR
     LDATDVDDDV GFDDLYLDDR PSGASDDVAF AGDISDGGAS SRSRASDASD GHVLGRLLRQ
     VRQGLSVGWR KPRYQKRRAR SISEEFSSGD TPRFKDEESA SKAESGHGPS SGGAGGGGGS
     GGAGGSSAAG ASASAAGGSS GHYRPDSGSG HKSDKSEKDR EKKEKEREEK DIEMIKVFDG
     NNSFRRQQYR VIIVQRTYTL EQLLTTALRA FHITRDPQAF YLTDLYAPAG MEDTPMLDPT
     PVLNLVHLEG KRPAIYLRFH DRDRGHVRVY PGKLQCSMLE DPYVSVPVDN STVIKDLIRD
     ALDKFGLQDN QIQDYRCSEV LLDRGVTERI LSWNERPWDI MKQLGKDSIR QMELMRFYMQ
     HKQDPHGPNI ALFVGNLPTG LSQRNYEQIL NKYVTDENKF ISIGPIYYEY GSVVLTFEDS
     MKAVRAFYNL RETIIEDKKL LVLLLPNIEP SMVPSDVRPL LVFVNVKSGG CQGLELISSF
     RKLLNPYQVF DLDNGGPLPG YVQPITVFVI RPLIFDSIIS LYVFRQITNY KILVCGGDGT
     IGWVLQCLDN VGQDSECSSP PCAIVPLGTG NDLARVLCWG SGYTGGEDPL NLLRDVIEAE
     EIRLDRWTVV FHPEDKPEEP AMKAPSQTTG KKKKAHQAHL SQSQQTNQHH QLPALTSSDI
     SGGAQNEDNS QIFVMNNYFG IGIDADLCLD FHNAREENPN QFNSRLRNKG YYVKMGLRKI
     VGRKAVKDLQ KELRLEVDGK IVELPPVDGI IILNILSWGS GANPWGPDKD DQFSTPNHYD
     GMLEVVGVTG VVHLGQIQSG IRTAMRIAQG GHIKIHLNTD MPVQVDGEPW IQSPGDVVVL
     KSALKATMLK KNKLKMKRRN TEPTMMVAGS AAPPLSLALP PSVGEVGVAG EGAEGDGGTN
     NTDF
//
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