DGKQ_RAT
ID DGKQ_RAT Reviewed; 937 AA.
AC D3ZEY4;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Diacylglycerol kinase theta {ECO:0000305};
DE Short=DAG kinase theta;
DE Short=DGKtheta {ECO:0000303|PubMed:9099683};
DE EC=2.7.1.107 {ECO:0000269|PubMed:15337525};
GN Name=Dgkq {ECO:0000312|RGD:2320722};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=9099683; DOI=10.1074/jbc.272.16.10422;
RA Houssa B., Schaap D., van der Wal J., Goto K., Kondo H., Yamakawa A.,
RA Shibata M., Takenawa T., van Blitterswijk W.J.;
RT "Cloning of a novel human diacylglycerol kinase (DGKtheta) containing three
RT cysteine-rich domains, a proline-rich region, and a pleckstrin homology
RT domain with an overlapping Ras-associating domain.";
RL J. Biol. Chem. 272:10422-10428(1997).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15337525; DOI=10.1016/j.cellsig.2004.03.018;
RA Tabellini G., Billi A.M., Fala F., Cappellini A., Evagelisti C.,
RA Manzoli L., Cocco L., Martelli A.M.;
RT "Nuclear diacylglycerol kinase-theta is activated in response to nerve
RT growth factor stimulation of PC12 cells.";
RL Cell. Signal. 16:1263-1271(2004).
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:15337525). 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:15337525). 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 (PubMed:15337525). Through its
CC diacylglycerol activity also regulates synaptic vesicle endocytosis (By
CC similarity). {ECO:0000250|UniProtKB:P52824,
CC ECO:0000269|PubMed:15337525}.
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:15337525};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC Evidence={ECO:0000305|PubMed:15337525};
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:15337525};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC Evidence={ECO:0000305|PubMed:15337525};
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:0000269|PubMed:15337525}.
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC {ECO:0000269|PubMed:15337525}.
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:0000250|UniProtKB:Q6P5E8}. Cell membrane
CC {ECO:0000250|UniProtKB:P52824}. Synapse {ECO:0000250|UniProtKB:Q6P5E8}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P52824}. Nucleus
CC {ECO:0000269|PubMed:15337525}. Nucleus speckle
CC {ECO:0000269|PubMed:15337525}. Nucleus matrix
CC {ECO:0000269|PubMed:15337525}. Note=Translocates to the plasma membrane
CC in response to steroid hormone receptor stimulation. Translocation to
CC the plasma membrane is dependent on G-protein coupled receptor
CC stimulation and subsequent activation of PRKCE and probably PRKCH.
CC Translocates to the nucleus in response to thrombin stimulation (By
CC similarity). Association with the nuclear matrix is regulated by nerve
CC growth factor (PubMed:15337525). {ECO:0000250|UniProtKB:P52824,
CC ECO:0000269|PubMed:15337525}.
CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in the
CC brain and, to a lesser extent, in the small intestine, duodenum, and
CC liver (PubMed:9099683). In brain, expressed in gray matter
CC (PubMed:9099683). Expression is most intense in the cerebellar cortex
CC and hippocampus, while moderate expression is seen in the olfactory
CC bulb neuronal layers and brain stem nuclei (PubMed:9099683). In the
CC cerebellar cortex, equally expressed in both the Purkinje cell somata
CC and the granule cells (PubMed:9099683). {ECO:0000269|PubMed:9099683}.
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 -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000305}.
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DR EMBL; AC117047; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474079; EDL84024.1; -; Genomic_DNA.
DR RefSeq; NP_001185733.1; NM_001198804.1.
DR AlphaFoldDB; D3ZEY4; -.
DR SMR; D3ZEY4; -.
DR IntAct; D3ZEY4; 1.
DR STRING; 10116.ENSRNOP00000036466; -.
DR PhosphoSitePlus; D3ZEY4; -.
DR PaxDb; D3ZEY4; -.
DR PeptideAtlas; D3ZEY4; -.
DR Ensembl; ENSRNOT00000032056; ENSRNOP00000036466; ENSRNOG00000024112.
DR GeneID; 100361138; -.
DR KEGG; rno:100361138; -.
DR UCSC; RGD:2320722; rat.
DR CTD; 1609; -.
DR RGD; 2320722; Dgkq.
DR eggNOG; KOG1169; Eukaryota.
DR GeneTree; ENSGT00940000159492; -.
DR HOGENOM; CLU_003770_0_0_1; -.
DR InParanoid; D3ZEY4; -.
DR OMA; EDYRCSE; -.
DR OrthoDB; 1275907at2759; -.
DR PhylomeDB; D3ZEY4; -.
DR TreeFam; TF312817; -.
DR Reactome; R-RNO-114508; Effects of PIP2 hydrolysis.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Proteomes; UP000234681; Chromosome 14.
DR Bgee; ENSRNOG00000024112; Expressed in jejunum and 20 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005768; C:endosome; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0016363; C:nuclear matrix; IMP:ParkinsonsUK-UCL.
DR GO; GO:0016607; C:nuclear speck; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; ISO:RGD.
DR GO; GO:0098793; C:presynapse; ISO:RGD.
DR GO; GO:0012506; C:vesicle membrane; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004143; F:diacylglycerol kinase activity; IMP:ParkinsonsUK-UCL.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0019900; F:kinase binding; ISO:RGD.
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:RGD.
DR GO; GO:0030297; F:transmembrane receptor protein tyrosine kinase activator activity; ISO:RGD.
DR GO; GO:0019933; P:cAMP-mediated signaling; ISO:RGD.
DR GO; GO:0046339; P:diacylglycerol metabolic process; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0046486; P:glycerolipid metabolic process; ISO:RGD.
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:RGD.
DR GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; ISO:RGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0070528; P:protein kinase C signaling; ISO:RGD.
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:RGD.
DR GO; GO:2000064; P:regulation of cortisol biosynthetic process; ISO:RGD.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0006111; P:regulation of gluconeogenesis; ISO:RGD.
DR GO; GO:2000182; P:regulation of progesterone biosynthetic process; ISO:RGD.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; ISO:RGD.
DR GO; GO:1903432; P:regulation of TORC1 signaling; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0033198; P:response to ATP; ISO:RGD.
DR GO; GO:0051591; P:response to cAMP; ISO:RGD.
DR GO; GO:0070493; P:thrombin-activated receptor signaling pathway; ISO:RGD.
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 ATP-binding; Cell membrane; Cytoplasm; Cytoskeleton; Kinase;
KW Lipid metabolism; Membrane; Metal-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Synapse; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..937
FT /note="Diacylglycerol kinase theta"
FT /id="PRO_0000450756"
FT DOMAIN 390..489
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 579..716
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..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 550..554
FT /note="LXXLL motif 1"
FT /evidence="ECO:0000250|UniProtKB:P52824"
FT MOTIF 569..573
FT /note="LXXLL motif 2"
FT /evidence="ECO:0000250|UniProtKB:P52824"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P5E8"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P5E8"
SQ SEQUENCE 937 AA; 102545 MW; 9E0EAEAFD5A99716 CRC64;
MATAAESGAR TWPGSGSPRL GSPAGSPVLG ISGRARPGSG PERTGRAIGS VAPGHSFRKV
TLTKPTFCHL CSDFIWGLAG FLCDVCNFMS HEKCLKQVKT PCTSIAPSLV RVPVAHCFGS
LGLYKRKFCV VCRKSLEVPA FRCEVCELHV HPDCVPFACS DCRQCHQDGQ HDYDTYHHHW
REGNLPSGAR CEVCRKTCGS SDVLAGVRCE WCGVQAHSVC STALTPECTF GRLRSMVLPP
SCVRLLSRNF SKMHCFRIPE TMVLELGDGD DGLDGSAAVG TGREVSAATE STKQTLKIFD
GNDSMRKNQF RLVTVSRLAR NEEVMEAALR AYYINEDPKD FQLQALPLTL LSGNAQALGK
AGTTEEETSK DSGPGDSVPE AWVIRSLPRT QEILKIYPDW LKVGVAYVSI RVNSQSTARS
VVQEVLPLFG RQVEDQERFQ LIEVLMSSRQ VQRTVLVDEE PLLDRLRDIR QTSVRQASQT
RFYVAEARAV TPHVSLFVGG LPPGLSPQDY SNLLHEAMAT KAAVVSVSHV YSLQGAVVLD
VTCFAEAERL YMLARDTAVH GRPLTALVLP DVLHTKLPPD CCPLLVFVNP KSGGLKGREL
LCSFRKLLNP HQVFELTNGG PLPGFHLFSQ VPCFRVLVCG GDGTVGWVLA ALEETRRHLA
CPEPSVAILP LGTGNDLGRV LRWGAGYSGE DPFSVLVSVD EADAVLMDRW TILLDAHEID
STENNVVETE PPKIVQMNNY CGIGIDAELS LDFHQAREEE PGKFTSRFHN KGVYVRVGLQ
KISHSRSLHK EIRLQVEQQE VELPSIEGLI FINIPSWGSG ADLWGSDSDS RFEKPRIDDG
LLEVVGVTGV VHMGQVQGGL RSGIRIAQGS YFRVTLLKAT PVQVDGEPWI QAPGHMIISA
TAPKVHMLRK AKQKPRKAGA IRDTRVDTLP APEGNPL
