DGKD_HUMAN
ID DGKD_HUMAN Reviewed; 1214 AA.
AC Q16760; Q14158; Q6PK55; Q8NG53;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 4.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=Diacylglycerol kinase delta {ECO:0000305};
DE Short=DAG kinase delta;
DE EC=2.7.1.107 {ECO:0000269|PubMed:12200442, ECO:0000269|PubMed:17880279, ECO:0000269|PubMed:23949095};
DE AltName: Full=130 kDa diacylglycerol kinase;
DE AltName: Full=Diglyceride kinase delta;
DE Short=DGK-delta;
GN Name=DGKD {ECO:0000312|HGNC:HGNC:2851};
GN Synonyms=KIAA0145 {ECO:0000312|EMBL:BAC11809.1};
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] (ISOFORMS 1 AND 2), FUNCTION, CATALYTIC
RP ACTIVITY, PATHWAY, SUBCELLULAR LOCATION (ISOFORM 1), SUBUNIT, INDUCTION BY
RP PHORBOL ESTERS (ISOFORMS 1 AND 2), DOMAIN, TISSUE SPECIFICITY (ISOFORMS 1
RP AND 2), AND REGION.
RC TISSUE=Brain;
RX PubMed=12200442; DOI=10.1074/jbc.m206895200;
RA Sakane F., Imai S., Yamada K., Murakami T., Tsushima S., Kanoh H.;
RT "Alternative splicing of the human diacylglycerol kinase delta gene
RT generates two isoforms differing in their expression patterns and in
RT regulatory functions.";
RL J. Biol. Chem. 277:43519-43526(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-1214 (ISOFORM 2).
RC TISSUE=Bone marrow;
RX PubMed=8590280; DOI=10.1093/dnares/2.4.167;
RA Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. IV. The
RT coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:167-174(1995).
RN [3]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R., Nomura N.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 45-1214 (ISOFORM 1).
RC TISSUE=Hepatoma, and Testis;
RX PubMed=8626538; DOI=10.1074/jbc.271.14.8394;
RA Sakane F., Imai S., Kai M., Wada I., Kanoh H.;
RT "Molecular cloning of a novel diacylglycerol kinase isozyme with a
RT pleckstrin homology domain and a C-terminal tail similar to those of the
RT EPH family of protein-tyrosine kinases.";
RL J. Biol. Chem. 271:8394-8401(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1068-1214.
RC TISSUE=Lymph;
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 [6]
RP SUBUNIT, SUBCELLULAR LOCATION (ISOFORM 1), PHOSPHORYLATION (ISOFORM 1),
RP DOMAIN, AND MUTAGENESIS OF TRP-1145.
RX PubMed=12084710; DOI=10.1074/jbc.m202035200;
RA Imai S., Sakane F., Kanoh H.;
RT "Phorbol ester-regulated oligomerization of diacylglycerol kinase delta
RT linked to its phosphorylation and translocation.";
RL J. Biol. Chem. 277:35323-35332(2002).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH AP2A2, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF PHE-369; PHE-372 AND PHE-748.
RX PubMed=17880279; DOI=10.1042/bj20070755;
RA Kawasaki T., Kobayashi T., Ueyama T., Shirai Y., Saito N.;
RT "Regulation of clathrin-dependent endocytosis by diacylglycerol kinase
RT delta: importance of kinase activity and binding to AP2alpha.";
RL Biochem. J. 409:471-479(2008).
RN [8]
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).
RN [9]
RP STRUCTURE BY NMR OF 216-286.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the C1 domain of the human diacylglycerol kinase
RT delta.";
RL Submitted (APR-2004) to the PDB data bank.
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:12200442, 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). By
CC controlling the levels of diacylglycerol, regulates for instance the
CC PKC and EGF receptor signaling pathways and plays a crucial role during
CC development (By similarity). May also regulate clathrin-dependent
CC endocytosis (PubMed:17880279). {ECO:0000250|UniProtKB:E9PUQ8,
CC ECO:0000269|PubMed:12200442, ECO:0000269|PubMed:17880279,
CC ECO:0000269|PubMed:23949095, 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:12200442, ECO:0000269|PubMed:17880279,
CC ECO:0000269|PubMed:23949095};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC Evidence={ECO:0000305|PubMed:12200442};
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:12200442, ECO:0000269|PubMed:23949095};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC Evidence={ECO:0000305|PubMed:12200442};
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:17880279};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324;
CC Evidence={ECO:0000305|PubMed:17880279};
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC {ECO:0000305|PubMed:12200442}.
CC -!- SUBUNIT: Homooligomer (PubMed:12200442, PubMed:12084710). Monomer
CC (PubMed:12084710). Interacts with AP2A2; regulates clathrin-dependent
CC endocytosis (PubMed:17880279). {ECO:0000269|PubMed:12084710,
CC ECO:0000269|PubMed:12200442, ECO:0000269|PubMed:17880279}.
CC -!- INTERACTION:
CC Q16760-2; Q16760-2: DGKD; NbExp=5; IntAct=EBI-11147675, EBI-11147675;
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit
CC {ECO:0000269|PubMed:17880279}. Cytoplasm {ECO:0000269|PubMed:12200442}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:12200442}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12200442}. Cytoplasm {ECO:0000269|PubMed:12200442}.
CC Note=Isoform 1 translocation from cytoplasm to the plasma membrane is
CC induced by phorbol esters (PubMed:12200442). Phorbol esters induce the
CC conversion into the monomeric form which can translocate to the plasma
CC membrane (PubMed:12084710). {ECO:0000269|PubMed:12084710,
CC ECO:0000269|PubMed:12200442}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2; Synonyms=DGKdelta2 {ECO:0000303|PubMed:12200442};
CC IsoId=Q16760-1; Sequence=Displayed;
CC Name=1; Synonyms=DGKdelta1 {ECO:0000303|PubMed:12200442};
CC IsoId=Q16760-2; Sequence=VSP_012891;
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Widely expressed.
CC {ECO:0000269|PubMed:12200442}.
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Only detected in ovary, and to a
CC lesser extent in spleen. {ECO:0000269|PubMed:12200442}.
CC -!- INDUCTION: [Isoform 2]: Up-regulated by phorbol esters and EGF.
CC {ECO:0000269|PubMed:12200442}.
CC -!- INDUCTION: [Isoform 1]: Down-regulated by phorbol esters.
CC {ECO:0000269|PubMed:12200442}.
CC -!- DOMAIN: The SAM domain mediates homooligomerization.
CC {ECO:0000269|PubMed:12084710}.
CC -!- DOMAIN: The PH domain mediates association with membranes.
CC {ECO:0000269|PubMed:12200442}.
CC -!- PTM: [Isoform 1]: Phosphorylated (PubMed:12084710). Phosphorylation by
CC PKC induced by phorbol esters prevents homooligomerization and promotes
CC association with membranes (PubMed:12084710).
CC {ECO:0000269|PubMed:12084710}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000305}.
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DR EMBL; AB078966; BAC11809.1; -; mRNA.
DR EMBL; D63479; BAA09766.3; -; mRNA.
DR EMBL; D73409; BAA11134.1; -; mRNA.
DR EMBL; BC006561; AAH06561.1; -; mRNA.
DR CCDS; CCDS2504.1; -. [Q16760-1]
DR CCDS; CCDS46546.1; -. [Q16760-2]
DR RefSeq; NP_003639.2; NM_003648.2. [Q16760-2]
DR RefSeq; NP_690618.2; NM_152879.2. [Q16760-1]
DR PDB; 1R79; NMR; -; A=216-286.
DR PDB; 3BQ7; X-ray; 2.90 A; A/B/C/D/E/F=1141-1208.
DR PDBsum; 1R79; -.
DR PDBsum; 3BQ7; -.
DR AlphaFoldDB; Q16760; -.
DR BMRB; Q16760; -.
DR SMR; Q16760; -.
DR BioGRID; 114097; 26.
DR DIP; DIP-29646N; -.
DR IntAct; Q16760; 16.
DR MINT; Q16760; -.
DR STRING; 9606.ENSP00000264057; -.
DR ChEMBL; CHEMBL1075120; -.
DR DrugBank; DB14001; alpha-Tocopherol succinate.
DR DrugBank; DB00144; Phosphatidyl serine.
DR SwissLipids; SLP:000000939; -. [Q16760-2]
DR iPTMnet; Q16760; -.
DR PhosphoSitePlus; Q16760; -.
DR BioMuta; DGKD; -.
DR DMDM; 116241328; -.
DR EPD; Q16760; -.
DR jPOST; Q16760; -.
DR MassIVE; Q16760; -.
DR MaxQB; Q16760; -.
DR PaxDb; Q16760; -.
DR PeptideAtlas; Q16760; -.
DR PRIDE; Q16760; -.
DR ProteomicsDB; 61052; -. [Q16760-1]
DR ProteomicsDB; 61053; -. [Q16760-2]
DR Antibodypedia; 34452; 172 antibodies from 28 providers.
DR DNASU; 8527; -.
DR Ensembl; ENST00000264057.7; ENSP00000264057.2; ENSG00000077044.11. [Q16760-1]
DR Ensembl; ENST00000409813.7; ENSP00000386455.3; ENSG00000077044.11. [Q16760-2]
DR Ensembl; ENST00000628356.4; ENSP00000487220.1; ENSG00000280873.5. [Q16760-1]
DR Ensembl; ENST00000628527.2; ENSP00000487423.1; ENSG00000280873.5. [Q16760-2]
DR GeneID; 8527; -.
DR KEGG; hsa:8527; -.
DR MANE-Select; ENST00000264057.7; ENSP00000264057.2; NM_152879.3; NP_690618.2.
DR UCSC; uc002vui.2; human. [Q16760-1]
DR CTD; 8527; -.
DR DisGeNET; 8527; -.
DR GeneCards; DGKD; -.
DR HGNC; HGNC:2851; DGKD.
DR HPA; ENSG00000077044; Tissue enhanced (skeletal).
DR MIM; 601826; gene.
DR neXtProt; NX_Q16760; -.
DR OpenTargets; ENSG00000077044; -.
DR PharmGKB; PA27312; -.
DR VEuPathDB; HostDB:ENSG00000077044; -.
DR eggNOG; KOG1170; Eukaryota.
DR GeneTree; ENSGT00940000159041; -.
DR HOGENOM; CLU_001799_3_0_1; -.
DR InParanoid; Q16760; -.
DR OMA; SKAPCEK; -.
DR OrthoDB; 43384at2759; -.
DR PhylomeDB; Q16760; -.
DR TreeFam; TF313104; -.
DR BRENDA; 2.7.1.107; 2681.
DR PathwayCommons; Q16760; -.
DR Reactome; R-HSA-114508; Effects of PIP2 hydrolysis.
DR SignaLink; Q16760; -.
DR SIGNOR; Q16760; -.
DR UniPathway; UPA00230; -.
DR BioGRID-ORCS; 8527; 39 hits in 1093 CRISPR screens.
DR ChiTaRS; DGKD; human.
DR EvolutionaryTrace; Q16760; -.
DR GeneWiki; DGKD; -.
DR GenomeRNAi; 8527; -.
DR Pharos; Q16760; Tbio.
DR PRO; PR:Q16760; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q16760; protein.
DR Bgee; ENSG00000077044; Expressed in body of stomach and 95 other tissues.
DR ExpressionAtlas; Q16760; baseline and differential.
DR Genevisible; Q16760; HS.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; TAS:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019992; F:diacylglycerol binding; NAS:UniProtKB.
DR GO; GO:0004143; F:diacylglycerol kinase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:MGI.
DR GO; GO:0046339; P:diacylglycerol metabolic process; IDA:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; NAS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0046834; P:lipid phosphorylation; IDA:UniProtKB.
DR GO; GO:0090038; P:negative regulation of protein kinase C signaling; ISS:UniProtKB.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; IMP:UniProtKB.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; NAS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0010033; P:response to organic substance; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
DR CDD; cd00029; C1; 2.
DR CDD; cd09575; SAM_DGK-delta; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.50.10330; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR037607; DGK.
DR InterPro; IPR037606; DGK-delta_SAM.
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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR11255; PTHR11255; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF57889; SSF57889; 2.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cell membrane; Coated pit;
KW Cytoplasm; Endocytosis; Kinase; Lipid metabolism; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Protein transport; Reference proteome;
KW Repeat; Transferase; Transport; Zinc; Zinc-finger.
FT CHAIN 1..1214
FT /note="Diacylglycerol kinase delta"
FT /id="PRO_0000218462"
FT DOMAIN 53..146
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 317..451
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT DOMAIN 1145..1208
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT ZN_FING 163..213
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 235..286
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..52
FT /note="Regulates association with membranes"
FT /evidence="ECO:0000269|PubMed:12200442"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..52
FT /note="MAAAAGAPPPGPPQPPPPPPPEESSDSEPEAEPGSPQKLIRKVSTSGQIRQK
FT -> MNMFLYFQ (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:12200442,
FT ECO:0000303|PubMed:8626538"
FT /id="VSP_012891"
FT MUTAGEN 369
FT /note="F->A: Decreased interaction with AP2A2; when
FT associated with A-372."
FT /evidence="ECO:0000269|PubMed:17880279"
FT MUTAGEN 372
FT /note="F->A: Decreased interaction with AP2A2; when
FT associated with A-369."
FT /evidence="ECO:0000269|PubMed:17880279"
FT MUTAGEN 748
FT /note="F->A: Decreased interaction with AP2A2."
FT /evidence="ECO:0000269|PubMed:17880279"
FT MUTAGEN 1145
FT /note="W->G: Loss of homooligomerization."
FT /evidence="ECO:0000269|PubMed:12084710"
FT CONFLICT 511
FT /note="V -> P (in Ref. 4; BAA11134)"
FT /evidence="ECO:0000305"
FT CONFLICT 828..834
FT /note="RPIPLPS -> DPSHSPV (in Ref. 4; BAA11134)"
FT /evidence="ECO:0000305"
FT CONFLICT 960
FT /note="L -> V (in Ref. 1; BAC11809 and 4; BAA11134)"
FT /evidence="ECO:0000305"
FT CONFLICT 1054
FT /note="Missing (in Ref. 4; BAA11134)"
FT /evidence="ECO:0000305"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:1R79"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:1R79"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:1R79"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:1R79"
FT HELIX 276..281
FT /evidence="ECO:0007829|PDB:1R79"
FT HELIX 1142..1144
FT /evidence="ECO:0007829|PDB:3BQ7"
FT HELIX 1147..1156
FT /evidence="ECO:0007829|PDB:3BQ7"
FT HELIX 1160..1162
FT /evidence="ECO:0007829|PDB:3BQ7"
FT HELIX 1163..1168
FT /evidence="ECO:0007829|PDB:3BQ7"
FT HELIX 1173..1176
FT /evidence="ECO:0007829|PDB:3BQ7"
FT HELIX 1181..1186
FT /evidence="ECO:0007829|PDB:3BQ7"
FT HELIX 1192..1206
FT /evidence="ECO:0007829|PDB:3BQ7"
SQ SEQUENCE 1214 AA; 134525 MW; ED114429096D2112 CRC64;
MAAAAGAPPP GPPQPPPPPP PEESSDSEPE AEPGSPQKLI RKVSTSGQIR QKTIIKEGML
TKQNNSFQRS KRRYFKLRGR TLYYAKTAKS IIFDEVDLTD ASVAESSTKN VNNSFTVITP
CRKLILCADN RKEMEDWIAA LKTVQNREHF EPTQYSMDHF SGMHNWYACS HARPTYCNVC
REALSGVTSH GLSCEVCKFK AHKRCAVRAT NNCKWTTLAS IGKDIIEDAD GIAMPHQWLE
GNLPVSAKCT VCDKTCGSVL RLQDWRCLWC KAMVHTSCKE SLLTKCPLGL CKVSVIPPTA
LNSIDSDGFW KASCPPSCTS PLLVFVNSKS GDNQGVKFLR RFKQLLNPAQ VFDLMNGGPH
LGLRLFQKFD TFRILVCGGD GSVGWVLSEI DSLNLHKQCQ LGVLPLGTGN DLARVLGWGS
ACDDDTQLPQ ILEKLERAST KMLDRWSVMA YEAKLPRQAS SSTVTEDFSE DSEVQQILFY
EDSVAAHLSK ILTSDQHSVV ISSAKVLCET VKDFVARVGK AYEKTTESSE ESEVMAKKCS
VLKEKLDSLL KTLDDESQAS SSLPNPPPTI AEEAEDGDGS GSICGSTGDR LVASACPARP
QIFRPREQLM LRANSLKKAI RQIIEHTEKA VDEQNAQTQE QEGFVLGLSE SEEKMDHRVC
PPLSHSESFG VPKGRSQRKV SKSPCEKLIS KGSLSLGSSA SLPPQPGSRD GLPALNTKIL
YPNVRAGMSG SLPGGSVISR LLINADPFNS EPETLEYYTE KCVMNNYFGI GLDAKISLDF
NNKRDEHPEK CRSRTKNMMW YGVLGTKELL HRTYKNLEQK VLLECDGRPI PLPSLQGIAV
LNIPSYAGGT NFWGGTKEDD TFAAPSFDDK ILEVVAVFGS MQMAVSRVIR LQHHRIAQCR
TVKISILGDE GVPVQVDGEA WVQPPGYIRI VHKNRAQTLT RDRAFESTLK SWEDKQKCEL
PRPPSCSLHP EMLSEEEATQ MDQFGQAAGV LIHSIREIAQ SHRDMEQELA HAVNASSKSM
DRVYGKPRTT EGLNCSFVLE MVNNFRALRS ETELLLSGKM ALQLDPPQKE QLGSALAEMD
RQLRRLADTP WLCQSAEPGD EESVMLDLAK RSRSGKFRLV TKFKKEKNNK NKEAHSSLGA
PVHLWGTEEV AAWLEHLSLC EYKDIFTRHD IRGSELLHLE RRDLKDLGVT KVGHMKRILC
GIKELSRSAP AVEA
