ID   DGKI_HUMAN              Reviewed;        1065 AA.
AC   O75912; A4D1Q9; Q9NZ49;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 195.
DE   RecName: Full=Diacylglycerol kinase iota {ECO:0000303|PubMed:9830018};
DE            Short=DAG kinase iota {ECO:0000305|PubMed:9830018};
DE            Short=DGK-iota {ECO:0000303|PubMed:9830018};
DE            EC=2.7.1.107 {ECO:0000269|PubMed:23949095, ECO:0000269|PubMed:9830018};
GN   Name=DGKI {ECO:0000312|HGNC:HGNC:2855};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Retina;
RX   PubMed=9830018; DOI=10.1074/jbc.273.49.32746;
RA   Ding L., Traer E., McIntyre T.M., Zimmerman G.A., Prescott S.M.;
RT   "The cloning and characterization of a novel human diacylglycerol kinase,
RT   DGK-iota.";
RL   J. Biol. Chem. 273:32746-32752(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA   Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA   Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA   Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA   Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA   Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA   Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA   Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 135-1065, AND VARIANT PHE-153.
RX   PubMed=10706894;
RA   Bowne S.J., Sullivan L.S., Ding L., Traer E., Prescott S.M., Birch D.G.,
RA   Kennan A., Humphries P., Daiger S.P.;
RT   "Evaluation of human diacylglycerol kinase iota, DGKI, a homolog of
RT   Drosophila rdgA, in inherited retinopathy mapping to 7q.";
RL   Mol. Vis. 6:6-9(2000).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=15894621; DOI=10.1073/pnas.0500663102;
RA   Regier D.S., Higbee J., Lund K.M., Sakane F., Prescott S.M., Topham M.K.;
RT   "Diacylglycerol kinase iota regulates Ras guanyl-releasing protein 3 and
RT   inhibits Rap1 signaling.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:7595-7600(2005).
RN   [5]
RP   INTERACTION WITH DLG4.
RX   PubMed=21119615; DOI=10.1038/emboj.2010.286;
RA   Yang J., Seo J., Nair R., Han S., Jang S., Kim K., Han K., Paik S.K.,
RA   Choi J., Lee S., Bae Y.C., Topham M.K., Prescott S.M., Rhee J.S.,
RA   Choi S.Y., Kim E.;
RT   "DGKiota regulates presynaptic release during mGluR-dependent LTD.";
RL   EMBO J. 30:165-180(2011).
RN   [6]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=23949095; DOI=10.1159/000351849;
RA   Sato M., Liu K., Sasaki S., Kunii N., Sakai H., Mizuno H., Saga H.,
RA   Sakane F.;
RT   "Evaluations of the selectivities of the diacylglycerol kinase inhibitors
RT   R59022 and R59949 among diacylglycerol kinase isozymes using a new non-
RT   radioactive assay method.";
RL   Pharmacology 92:99-107(2013).
CC   -!- FUNCTION: Diacylglycerol kinase that converts diacylglycerol/DAG into
CC       phosphatidic acid/phosphatidate/PA and regulates the respective levels
CC       of these two bioactive lipids (PubMed:9830018, PubMed:23949095).
CC       Thereby, acts as a central switch between the signaling pathways
CC       activated by these second messengers with different cellular targets
CC       and opposite effects in numerous biological processes (Probable). Has
CC       probably no preference for any of the diacylglycerols in terms of the
CC       acyl chain composition, especially for the acyl chain at the sn-2
CC       position (PubMed:9830018). By controlling the diacylglycerol/DAG-
CC       mediated activation of RASGRP3, negatively regulates the Rap1 signaling
CC       pathway. May play a role in presynaptic diacylglycerol/DAG signaling
CC       and control neurotransmitter release during metabotropic glutamate
CC       receptor-dependent long-term depression (By similarity).
CC       {ECO:0000250|UniProtKB:D3YWQ0, ECO:0000269|PubMed:23949095,
CC       ECO:0000269|PubMed:9830018, ECO:0000305}.
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:0000269|PubMed:23949095, ECO:0000269|PubMed:9830018};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC         Evidence={ECO:0000305|PubMed:9830018};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-
CC         octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+);
CC         Xref=Rhea:RHEA:40327, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:52333, ChEBI:CHEBI:74546, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:23949095, ECO:0000269|PubMed:9830018};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC         Evidence={ECO:0000305|PubMed:9830018};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol
CC         + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC         3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40323, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:75728, ChEBI:CHEBI:77091,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:9830018};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324;
CC         Evidence={ECO:0000305|PubMed:9830018};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycerol + ATP =
CC         1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate +
CC         ADP + H(+); Xref=Rhea:RHEA:40339, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:77097, ChEBI:CHEBI:77098,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:F1MAB7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40340;
CC         Evidence={ECO:0000250|UniProtKB:F1MAB7};
CC   -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC       {ECO:0000269|PubMed:9830018}.
CC   -!- SUBUNIT: Interacts (via PDZ-binding motif) with DLG4; controls the
CC       localization of DGKI to the synapse (PubMed:21119615). Interacts (via
CC       PDZ-binding motif) with DLG1 (By similarity). Interacts (via PDZ-
CC       binding motif) with DLG2 (By similarity). Interacts (via PDZ-binding
CC       motif) with DLG3 (By similarity). May interact with RASGRP3; involved
CC       in the regulation of RASGRP3 activity (By similarity).
CC       {ECO:0000250|UniProtKB:D3YWQ0, ECO:0000250|UniProtKB:F1MAB7,
CC       ECO:0000269|PubMed:21119615}.
CC   -!- INTERACTION:
CC       O75912; P40337-3: VHL; NbExp=3; IntAct=EBI-1765520, EBI-301270;
CC   -!- SUBCELLULAR LOCATION: Cell projection, axon
CC       {ECO:0000250|UniProtKB:F1MAB7}. Cell projection, dendrite
CC       {ECO:0000250|UniProtKB:F1MAB7}. Presynapse
CC       {ECO:0000250|UniProtKB:F1MAB7}. Postsynapse
CC       {ECO:0000250|UniProtKB:F1MAB7}. Postsynaptic density
CC       {ECO:0000250|UniProtKB:F1MAB7}. Synaptic cell membrane
CC       {ECO:0000250|UniProtKB:F1MAB7}. Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane {ECO:0000250|UniProtKB:F1MAB7}. Cytoplasm,
CC       cytosol {ECO:0000269|PubMed:9830018}. Nucleus
CC       {ECO:0000269|PubMed:9830018}. Note=Excluded from inhibitory synapses
CC       (By similarity). Localization between cytoplasm and nucleus is
CC       regulated by protein kinase C (PubMed:9830018). Both in the detergent
CC       soluble and particulate fractions (By similarity).
CC       {ECO:0000250|UniProtKB:F1MAB7, ECO:0000269|PubMed:9830018}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in brain and retina
CC       (PubMed:9830018). In brain, highly expressed in hippocampus, caudate
CC       nucleus, occipital pole, cerebral cortex, and cerebellum
CC       (PubMed:9830018). Also detected in kidney (PubMed:15894621).
CC       {ECO:0000269|PubMed:15894621, ECO:0000269|PubMed:9830018}.
CC   -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC       {ECO:0000305}.
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DR   EMBL; AF061936; AAC62010.1; -; mRNA.
DR   EMBL; CH236950; EAL24051.1; -; Genomic_DNA.
DR   EMBL; AH009185; AAF43006.1; -; Genomic_DNA.
DR   CCDS; CCDS5845.1; -.
DR   RefSeq; NP_001308637.1; NM_001321708.1.
DR   RefSeq; NP_001308638.1; NM_001321709.1.
DR   RefSeq; NP_001308639.1; NM_001321710.1.
DR   RefSeq; NP_004708.1; NM_004717.3.
DR   AlphaFoldDB; O75912; -.
DR   SMR; O75912; -.
DR   BioGRID; 114605; 7.
DR   IntAct; O75912; 3.
DR   STRING; 9606.ENSP00000288490; -.
DR   DrugBank; DB14001; alpha-Tocopherol succinate.
DR   SwissLipids; SLP:000000925; -.
DR   iPTMnet; O75912; -.
DR   PhosphoSitePlus; O75912; -.
DR   BioMuta; DGKI; -.
DR   jPOST; O75912; -.
DR   MassIVE; O75912; -.
DR   MaxQB; O75912; -.
DR   PaxDb; 9606-ENSP00000288490; -.
DR   PeptideAtlas; O75912; -.
DR   ProteomicsDB; 50265; -.
DR   Antibodypedia; 32299; 219 antibodies from 29 providers.
DR   DNASU; 9162; -.
DR   Ensembl; ENST00000288490.9; ENSP00000288490.4; ENSG00000157680.17.
DR   GeneID; 9162; -.
DR   KEGG; hsa:9162; -.
DR   UCSC; uc003vtt.4; human.
DR   AGR; HGNC:2855; -.
DR   CTD; 9162; -.
DR   DisGeNET; 9162; -.
DR   GeneCards; DGKI; -.
DR   HGNC; HGNC:2855; DGKI.
DR   HPA; ENSG00000157680; Tissue enhanced (choroid plexus, retina, thyroid gland).
DR   MIM; 604072; gene.
DR   neXtProt; NX_O75912; -.
DR   OpenTargets; ENSG00000157680; -.
DR   PharmGKB; PA27316; -.
DR   VEuPathDB; HostDB:ENSG00000157680; -.
DR   eggNOG; KOG0782; Eukaryota.
DR   GeneTree; ENSGT00940000158094; -.
DR   InParanoid; O75912; -.
DR   OrthoDB; 4642163at2759; -.
DR   PhylomeDB; O75912; -.
DR   TreeFam; TF312817; -.
DR   BRENDA; 2.7.1.107; 2681.
DR   PathwayCommons; O75912; -.
DR   Reactome; R-HSA-114508; Effects of PIP2 hydrolysis.
DR   SignaLink; O75912; -.
DR   UniPathway; UPA00230; -.
DR   BioGRID-ORCS; 9162; 20 hits in 1160 CRISPR screens.
DR   ChiTaRS; DGKI; human.
DR   GenomeRNAi; 9162; -.
DR   Pharos; O75912; Tbio.
DR   PRO; PR:O75912; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; O75912; Protein.
DR   Bgee; ENSG00000157680; Expressed in cortical plate and 128 other cell types or tissues.
DR   ExpressionAtlas; O75912; baseline and differential.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0043197; C:dendritic spine; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0097060; C:synaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; IDA:BHF-UCL.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IDA:BHF-UCL.
DR   GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR   GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
DR   CDD; cd20850; C1_DGKiota_rpt1; 1.
DR   CDD; cd20896; C1_DGKiota_rpt2; 1.
DR   Gene3D; 2.60.200.40; -; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR047486; C1_DGKiota_rpt1.
DR   InterPro; IPR047487; C1_DGKiota_rpt2.
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; DIACYLGLYCEROL KINASE; 1.
DR   PANTHER; PTHR11255:SF92; DIACYLGLYCEROL KINASE IOTA; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00609; DAGK_acc; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00045; DAGKa; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS50146; DAGK; 1.
PE   1: Evidence at protein level;
KW   ANK repeat; ATP-binding; Cell membrane; Cell projection; Cytoplasm;
KW   Cytoplasmic vesicle; Kinase; Lipid metabolism; Membrane; Metal-binding;
KW   Nucleotide-binding; Nucleus; Reference proteome; Repeat; Synapse;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..1065
FT                   /note="Diacylglycerol kinase iota"
FT                   /id="PRO_0000218466"
FT   DOMAIN          372..507
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   REPEAT          958..987
FT                   /note="ANK 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          994..1023
FT                   /note="ANK 2"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         177..232
FT                   /note="Phorbol-ester/DAG-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT   ZN_FING         250..309
FT                   /note="Phorbol-ester/DAG-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT   REGION          15..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          334..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1022..1041
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1063..1065
FT                   /note="PDZ-binding"
FT                   /evidence="ECO:0000250|UniProtKB:F1MAB7"
FT   COMPBIAS        59..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..349
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         153
FT                   /note="L -> F (in dbSNP:rs61757580)"
FT                   /evidence="ECO:0000269|PubMed:10706894"
FT                   /id="VAR_010190"
FT   CONFLICT        160
FT                   /note="A -> P (in Ref. 3; AAF43006)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1065 AA;  116997 MW;  B84971AA7630A799 CRC64;
     MDAAGRGCHL LPLPAARGPA RAPAAAAAAA ASPPGPCSGA ACAPSAAAGA GAMNPSSSAG
     EEKGATGGSS SSGSGAGSCC LGAEGGADPR GAGSAAAAGA AALDEPAAAG QKEKDEALEE
     KLRNLTFRKQ VSYRKAISRA GLQHLAPAHP LSLPVANGPA KEPRATLDWS ENAVNGEHLW
     LETNVSGDLC YLGEENCQVR FAKSALRRKC AVCKIVVHTA CIEQLEKINF RCKPTFREGG
     SRSPRENFVR HHWVHRRRQE GKCKQCGKGF QQKFSFHSKE IVAISCSWCK QAFHNKVTCF
     MLHHIEEPCS LGAHAAVIVP PTWIIKVKKP QNSLKASNRK KKRTSFKRKA SKRGMEQENK
     GRPFVIKPIS SPLMKPLLVF VNPKSGGNQG TKVLQMFMWY LNPRQVFDLS QEGPKDALEL
     YRKVPNLRIL ACGGDGTVGW ILSILDELQL SPQPPVGVLP LGTGNDLART LNWGGGYTDE
     PVSKILCQVE DGTVVQLDRW NLHVERNPDL PPEELEDGVC KLPLNVFNNY FSLGFDAHVT
     LEFHESREAN PEKFNSRFRN KMFYAGAAFS DFLQRSSRDL SKHVKVVCDG TDLTPKIQEL
     KFQCIVFLNI PRYCAGTMPW GNPGDHHDFE PQRHDDGYIE VIGFTMASLA ALQVGGHGER
     LHQCREVMLL TYKSIPMQVD GEPCRLAPAM IRISLRNQAN MVQKSKRRTS MPLLNDPQSV
     PDRLRIRVNK ISLQDYEGFH YDKEKLREAS ISDWLRTIAG ELVQSFGAIP LGILVVRGDC
     DLETCRMYID RLQEDLQSVS SGSQRVHYQD HETSFPRALS AQRLSPRWCF LDDRSQEHLH
     FVMEISQDEI FILDPDMVVS QPAGTPPGMP DLVVEQASGI SDWWNPALRK RMLSDSGLGM
     IAPYYEDSDL KDLSHSRVLQ SPVSSEDHAI LQAVIAGDLM KLIESYKNGG SLLIQGPDHC
     SLLHYAAKTG NGEIVKYILD HGPSELLDMA DSETGETALH KAACQRNRAV CQLLVDAGAS
     LRKTDSKGKT PQERAQQAGD PDLAAYLESR QNYKVIGHED LETAV
//