DGKQ_MOUSE
ID DGKQ_MOUSE Reviewed; 934 AA.
AC Q6P5E8; Q3UYE8;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Diacylglycerol kinase theta;
DE Short=DAG kinase theta;
DE EC=2.7.1.107 {ECO:0000269|PubMed:26748701};
DE AltName: Full=Diglyceride kinase theta;
DE Short=DGK-theta;
GN Name=Dgkq;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-26, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
RC Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=26748701; DOI=10.1016/j.celrep.2015.12.022;
RA Goldschmidt H.L., Tu-Sekine B., Volk L., Anggono V., Huganir R.L.,
RA Raben D.M.;
RT "DGKtheta Catalytic Activity Is Required for Efficient Recycling of
RT Presynaptic Vesicles at Excitatory Synapses.";
RL Cell Rep. 14:200-207(2016).
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:26748701). Thereby, acts as a
CC central switch between the signaling pathways activated by these second
CC messengers with different cellular targets and opposite effects in
CC numerous biological processes (PubMed:26748701). Within the
CC adrenocorticotropic hormone signaling pathway, produces phosphatidic
CC acid which in turn activates NR5A1 and subsequent steroidogenic gene
CC transcription (By similarity). Also functions downstream of the nerve
CC growth factor signaling pathway being specifically activated in the
CC nucleus by the growth factor (By similarity). Through its
CC diacylglycerol activity also regulates synaptic vesicle endocytosis
CC (PubMed:26748701). {ECO:0000250|UniProtKB:D3ZEY4,
CC ECO:0000250|UniProtKB:P52824, ECO:0000269|PubMed:26748701}.
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:26748701};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC Evidence={ECO:0000269|PubMed:26748701};
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:0000250|UniProtKB:P52824};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC Evidence={ECO:0000250|UniProtKB:P52824};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-sn-glycerol + ATP = 1-O-hexadecyl-sn-glycero-3-
CC phosphate + ADP + H(+); Xref=Rhea:RHEA:41672, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:34115, ChEBI:CHEBI:77580,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P52824};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41673;
CC Evidence={ECO:0000250|UniProtKB:P52824};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-acetyl-sn-glycerol + ATP = 1-O-hexadecyl-2-
CC acetyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:41676,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:75936,
CC ChEBI:CHEBI:78385, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P52824};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41677;
CC Evidence={ECO:0000250|UniProtKB:P52824};
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:0000250|UniProtKB:P52824};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324;
CC Evidence={ECO:0000250|UniProtKB:P52824};
CC -!- ACTIVITY REGULATION: Activated by phosphatidylserine.
CC {ECO:0000250|UniProtKB:P52824}.
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC {ECO:0000269|PubMed:26748701}.
CC -!- SUBUNIT: Interacts with RHOA (constitutively activated, GTP-bound); the
CC interaction inhibits DGKQ. Interacts with PRKCE. Interacts with PRKCH.
CC Interacts with PLCB1. Interacts with NR5A1; the interaction requires
CC both LXXLL motifs in DGKQ and is required for full phosphatidic acid-
CC mediated activation of NR5A1. {ECO:0000250|UniProtKB:P52824}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P52824}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:26748701}. Cell membrane
CC {ECO:0000250|UniProtKB:P52824}. Synapse {ECO:0000269|PubMed:26748701}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P52824}. Nucleus
CC {ECO:0000250|UniProtKB:P52824}. Nucleus speckle
CC {ECO:0000250|UniProtKB:P52824}. Nucleus matrix
CC {ECO:0000250|UniProtKB:D3ZEY4}. Note=Translocates to the plasma
CC membrane in response to steroid hormone receptor stimulation.
CC Translocation to the plasma membrane is dependent on G-protein coupled
CC receptor stimulation and subsequent activation of PRKCE and probably
CC PRKCH. Translocates to the nucleus in response to thrombin stimulation
CC (By similarity). Association with the nuclear matrix is regulated by
CC nerve growth factor (By similarity). {ECO:0000250|UniProtKB:D3ZEY4,
CC ECO:0000250|UniProtKB:P52824}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P5E8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P5E8-2; Sequence=VSP_037832;
CC -!- TISSUE SPECIFICITY: Widely expressed in all brain regions, including
CC the cortex and hippocampus with a specific expression in neuronal cells
CC (at protein level). {ECO:0000269|PubMed:26748701}.
CC -!- DEVELOPMENTAL STAGE: Expression increases through development and peaks
CC at postnatal day 14. {ECO:0000269|PubMed:26748701}.
CC -!- DOMAIN: The L-X-X-L-L repeats are both required for binding and
CC phosphatidic acid-mediated activation of the nuclear receptor NR5A1.
CC {ECO:0000250|UniProtKB:P52824}.
CC -!- PTM: Phosphorylated by PRKCE and PRKCH in vitro.
CC {ECO:0000250|UniProtKB:P52824}.
CC -!- DISRUPTION PHENOTYPE: Homozygous knockout mice display no overt
CC phenotype with respect to body size, mating, and lifespan.
CC {ECO:0000269|PubMed:26748701}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000305}.
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DR EMBL; AK134745; BAE22264.1; -; mRNA.
DR EMBL; BC062929; AAH62929.1; -; mRNA.
DR CCDS; CCDS19515.1; -. [Q6P5E8-1]
DR RefSeq; NP_950176.1; NM_199011.1. [Q6P5E8-1]
DR AlphaFoldDB; Q6P5E8; -.
DR SMR; Q6P5E8; -.
DR BioGRID; 225672; 2.
DR STRING; 10090.ENSMUSP00000057859; -.
DR iPTMnet; Q6P5E8; -.
DR PhosphoSitePlus; Q6P5E8; -.
DR EPD; Q6P5E8; -.
DR jPOST; Q6P5E8; -.
DR MaxQB; Q6P5E8; -.
DR PaxDb; Q6P5E8; -.
DR PeptideAtlas; Q6P5E8; -.
DR PRIDE; Q6P5E8; -.
DR ProteomicsDB; 279411; -. [Q6P5E8-1]
DR ProteomicsDB; 279412; -. [Q6P5E8-2]
DR Antibodypedia; 22185; 219 antibodies from 31 providers.
DR DNASU; 110524; -.
DR Ensembl; ENSMUST00000053913; ENSMUSP00000057859; ENSMUSG00000004815. [Q6P5E8-1]
DR GeneID; 110524; -.
DR KEGG; mmu:110524; -.
DR UCSC; uc008yot.1; mouse. [Q6P5E8-1]
DR UCSC; uc012eau.1; mouse. [Q6P5E8-2]
DR CTD; 1609; -.
DR MGI; MGI:102918; Dgkq.
DR VEuPathDB; HostDB:ENSMUSG00000004815; -.
DR eggNOG; KOG1169; Eukaryota.
DR GeneTree; ENSGT00940000159492; -.
DR HOGENOM; CLU_003770_0_0_1; -.
DR InParanoid; Q6P5E8; -.
DR OMA; EDYRCSE; -.
DR OrthoDB; 1275907at2759; -.
DR PhylomeDB; Q6P5E8; -.
DR TreeFam; TF312817; -.
DR BRENDA; 2.7.1.107; 3474.
DR Reactome; R-MMU-114508; Effects of PIP2 hydrolysis.
DR UniPathway; UPA00230; -.
DR BioGRID-ORCS; 110524; 6 hits in 75 CRISPR screens.
DR ChiTaRS; Dgkq; mouse.
DR PRO; PR:Q6P5E8; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q6P5E8; protein.
DR Bgee; ENSMUSG00000004815; Expressed in primary visual cortex and 124 other tissues.
DR ExpressionAtlas; Q6P5E8; baseline and differential.
DR Genevisible; Q6P5E8; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016363; C:nuclear matrix; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0012506; C:vesicle membrane; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004143; F:diacylglycerol kinase activity; ISS:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0043274; F:phospholipase binding; ISO:MGI.
DR GO; GO:0030297; F:transmembrane receptor protein tyrosine kinase activator activity; ISO:MGI.
DR GO; GO:0019933; P:cAMP-mediated signaling; ISO:MGI.
DR GO; GO:0046339; P:diacylglycerol metabolic process; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0046486; P:glycerolipid metabolic process; ISO:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0046834; P:lipid phosphorylation; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; ISO:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:0070528; P:protein kinase C signaling; ISO:MGI.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0090181; P:regulation of cholesterol metabolic process; ISO:MGI.
DR GO; GO:2000064; P:regulation of cortisol biosynthetic process; ISO:MGI.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0006111; P:regulation of gluconeogenesis; ISO:MGI.
DR GO; GO:2000182; P:regulation of progesterone biosynthetic process; ISO:MGI.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; IDA:SynGO.
DR GO; GO:1903432; P:regulation of TORC1 signaling; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0033198; P:response to ATP; ISO:MGI.
DR GO; GO:0051591; P:response to cAMP; ISO:MGI.
DR GO; GO:0070493; P:thrombin-activated receptor signaling pathway; ISO:MGI.
DR CDD; cd00029; C1; 2.
DR Gene3D; 3.40.50.10330; -; 1.
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; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR11255; PTHR11255; 2.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF00788; RA; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 3.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00314; RA; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
DR SUPFAM; SSF54236; SSF54236; 2.
DR SUPFAM; SSF57889; SSF57889; 3.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 3.
DR PROSITE; PS50081; ZF_DAG_PE_2; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Cytoplasm; Cytoskeleton;
KW Kinase; Lipid metabolism; Membrane; Metal-binding; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Synapse; Transferase;
KW Zinc; Zinc-finger.
FT CHAIN 1..934
FT /note="Diacylglycerol kinase theta"
FT /id="PRO_0000381763"
FT DOMAIN 387..486
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 576..713
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT ZN_FING 54..102
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 115..162
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 177..228
FT /note="Phorbol-ester/DAG-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 547..551
FT /note="LXXLL motif 1"
FT /evidence="ECO:0000250|UniProtKB:P52824"
FT MOTIF 566..570
FT /note="LXXLL motif 2"
FT /evidence="ECO:0000250|UniProtKB:P52824"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..548
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_037832"
SQ SEQUENCE 934 AA; 102254 MW; C7FA90936443818E CRC64;
MAAAAEPGAR TWPGSGSPRL GSPAGSPVLG ISGRTRPGSG PERTSRAIGS AAPGHSFRKV
TLTKPTFCHL CSDFIWGLAG FLCDVCNFMS HEKCLKQVKT PCTSIAPSLV RVPVAHCFGS
LGLYKRKFCV VCRKSLEVPA FRCEVCELHV HPDCVPFACS DCRQCHQDGQ QDYDTYHHHW
REGNLPSGAR CEVCRKTCGS SDVLAGVRCE WCGVQAHSVC STALAPECTF GRLRSMVLPP
SCVRLLSRNF SKMHCFRIPE TMVLELGDGD DGVDGSAAIG TGREVLTATE STKQTLKIFD
GNDSMRKNQF RLVTVSRLAR NEEVMEAALR AYYISEDPKD FQLQALPLSG NAQALGKAGT
TEEEASKGSC PRDSVPEAWV IRSLPRTQEI LKIYPGWLKV GVAYVSIRVN SQSTARSVVQ
EVLPLFGQQV EDKERFQLIE VLMSSRQVQR TVLADEEPLL DRLWDIRQTS VRQVSQTRFY
VAETRATAPR VSLFVGGLPP GLSPQDYSNL LHEAMATKAA VVSVSHVYSL QGAVILDVTC
FAEAERLYML ARDTAVHGRP LTALVLPDVL HTKLPPDCCP LLVFVNPKSG GLKGRELLCS
FRKLLNPHQV FELTNGGPLP GFHLFSQVPS FRVLVCGGDG TVGWVLAALE ETRRHLACPE
PSVAILPLGT GNDLGRVLRW GAGYSGEDPF SVLVSVDEAD AVLMDRWTIL LDAHEIDSTE
NNVVETEPPK IVQMNNYCGI GIDAELSLDF HQAREEEPGK FTSRFHNKGV YVRVGLQKIS
HSRSLHKEIR LQVEQQEVEL PSIEGLIFIN IPSWGSGADL WGSDNDSRFE KPRIDDGLLE
VVGVTGVVHM GQVQGGLRSG IRIAQGSYFR VTLLKATPVQ VDGEPWVQAP GHMIISATAP
KVHMLRKAKQ KPRKAGANRD TRVDTLPAPE GNPL
