DGKA_PIG
ID DGKA_PIG Reviewed; 734 AA.
AC P20192;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Diacylglycerol kinase alpha;
DE Short=DAG kinase alpha;
DE EC=2.7.1.107 {ECO:0000269|PubMed:23949095, ECO:0000269|PubMed:8034597, ECO:0000269|PubMed:8809050};
DE AltName: Full=80 kDa diacylglycerol kinase;
DE AltName: Full=Diglyceride kinase alpha;
DE Short=DGK-alpha;
GN Name=DGKA; Synonyms=DAGK, DAGK1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Lymphocyte;
RX PubMed=2156169; DOI=10.1038/344345a0;
RA Sakane F., Yamada K., Kanoh H., Yokoyama C., Tanabe T.;
RT "Porcine diacylglycerol kinase sequence has zinc finger and E-F hand
RT motifs.";
RL Nature 344:345-348(1990).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=8034597; DOI=10.1016/s0021-9258(17)32336-0;
RA Kai M., Sakane F., Imai S., Wada I., Kanoh H.;
RT "Molecular cloning of a diacylglycerol kinase isozyme predominantly
RT expressed in human retina with a truncated and inactive enzyme expression
RT in most other human cells.";
RL J. Biol. Chem. 269:18492-18498(1994).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, REGION, AND MUTAGENESIS.
RX PubMed=8809050; DOI=10.1042/bj3180583;
RA Sakane F., Kai M., Wada I., Imai S., Kanoh H.;
RT "The C-terminal part of diacylglycerol kinase alpha lacking zinc fingers
RT serves as a catalytic domain.";
RL Biochem. J. 318:583-590(1996).
RN [4]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
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:8034597). 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:8034597). Also plays an important
CC role in the biosynthesis of complex lipids. Can also phosphorylate 1-
CC alkyl-2-acylglycerol in vitro as efficiently as diacylglycerol provided
CC it contains an arachidonoyl group. Also involved in the production of
CC alkyl-lysophosphatidic acid, another bioactive lipid, through the
CC phosphorylation of 1-alkyl-2-acetyl glycerol (By similarity).
CC {ECO:0000250|UniProtKB:P23743, ECO:0000269|PubMed:8034597}.
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:8034597, ECO:0000269|PubMed:8809050};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC Evidence={ECO:0000305|PubMed:8034597};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycerol + ATP = 1,2-dihexadecanoyl-sn-
CC glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:63324,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:72859,
CC ChEBI:CHEBI:82929, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P23743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63325;
CC Evidence={ECO:0000250|UniProtKB:P23743};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-
CC hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:43416, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:64839, ChEBI:CHEBI:75466, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P23743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43417;
CC Evidence={ECO:0000250|UniProtKB:P23743};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z-octadecenoyl)-glycerol + ATP = 2-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:63328,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:73990,
CC ChEBI:CHEBI:77593, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P23743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63329;
CC Evidence={ECO:0000250|UniProtKB:P23743};
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:8034597};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC Evidence={ECO:0000305|PubMed:8034597};
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:8034597};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324;
CC Evidence={ECO:0000305|PubMed:8034597};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-didecanoyl-sn-glycerol + ATP = 1,2-didecanoyl-sn-glycero-
CC 3-phosphate + ADP + H(+); Xref=Rhea:RHEA:43428, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18155, ChEBI:CHEBI:30616, ChEBI:CHEBI:78227,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:8034597};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43429;
CC Evidence={ECO:0000305|PubMed:8034597};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-alkyl-2-acyl-sn-glycerol + ATP = 1-O-alkyl-2-acyl-sn-
CC glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:44072,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:52595,
CC ChEBI:CHEBI:73332, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P23743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44073;
CC Evidence={ECO:0000250|UniProtKB:P23743};
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:P51556};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41677;
CC Evidence={ECO:0000250|UniProtKB:P51556};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol +
CC ATP = 1-O-hexadecyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-
CC phosphate + ADP + H(+); Xref=Rhea:RHEA:40403, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:77184, ChEBI:CHEBI:77186,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P23743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40404;
CC Evidence={ECO:0000250|UniProtKB:P23743};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-O-
CC hexadecyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:40407, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:77185, ChEBI:CHEBI:77187, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P23743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40408;
CC Evidence={ECO:0000250|UniProtKB:P23743};
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:P51556};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41673;
CC Evidence={ECO:0000250|UniProtKB:P51556};
CC -!- ACTIVITY REGULATION: Stimulated by calcium and phosphatidylserine.
CC {ECO:0000269|PubMed:23949095}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.13 mM for ATP (at pH 7.4) {ECO:0000269|PubMed:8809050};
CC KM=0.1 mM for ATP (at pH 7.4 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:23949095};
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC {ECO:0000305|PubMed:8034597}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P23743}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:8809050}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000305}.
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DR EMBL; X53256; CAA37347.1; -; mRNA.
DR PIR; S09156; S09156.
DR RefSeq; NP_999197.1; NM_214032.2.
DR RefSeq; XP_005663934.1; XM_005663877.2.
DR AlphaFoldDB; P20192; -.
DR SMR; P20192; -.
DR STRING; 9823.ENSSSCP00000000387; -.
DR BindingDB; P20192; -.
DR ChEMBL; CHEMBL4523195; -.
DR SwissLipids; SLP:000000924; -.
DR iPTMnet; P20192; -.
DR PaxDb; P20192; -.
DR PeptideAtlas; P20192; -.
DR PRIDE; P20192; -.
DR Ensembl; ENSSSCT00005020961; ENSSSCP00005012568; ENSSSCG00005012782.
DR Ensembl; ENSSSCT00015071712; ENSSSCP00015028738; ENSSSCG00015053448.
DR Ensembl; ENSSSCT00015071920; ENSSSCP00015028848; ENSSSCG00015053448.
DR Ensembl; ENSSSCT00040003422; ENSSSCP00040001033; ENSSSCG00040002738.
DR Ensembl; ENSSSCT00040003461; ENSSSCP00040001053; ENSSSCG00040002738.
DR Ensembl; ENSSSCT00045059915; ENSSSCP00045042055; ENSSSCG00045034839.
DR Ensembl; ENSSSCT00045060222; ENSSSCP00045042289; ENSSSCG00045034839.
DR Ensembl; ENSSSCT00055021361; ENSSSCP00055016919; ENSSSCG00055010666.
DR Ensembl; ENSSSCT00055021423; ENSSSCP00055016971; ENSSSCG00055010666.
DR Ensembl; ENSSSCT00060098048; ENSSSCP00060042504; ENSSSCG00060071679.
DR Ensembl; ENSSSCT00060098153; ENSSSCP00060042553; ENSSSCG00060071679.
DR Ensembl; ENSSSCT00065064046; ENSSSCP00065027748; ENSSSCG00065046800.
DR Ensembl; ENSSSCT00065064056; ENSSSCP00065027755; ENSSSCG00065046800.
DR GeneID; 397097; -.
DR KEGG; ssc:397097; -.
DR CTD; 1606; -.
DR eggNOG; KOG1169; Eukaryota.
DR HOGENOM; CLU_003770_1_1_1; -.
DR InParanoid; P20192; -.
DR OrthoDB; 633642at2759; -.
DR TreeFam; TF313104; -.
DR BRENDA; 2.7.1.107; 6170.
DR Reactome; R-SSC-114508; Effects of PIP2 hydrolysis.
DR SABIO-RK; P20192; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P20192; SS.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004143; F:diacylglycerol kinase activity; IDA:UniProtKB.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0046339; P:diacylglycerol metabolic process; IDA:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0046834; P:lipid phosphorylation; IDA:UniProtKB.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR CDD; cd00029; C1; 1.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 1.10.238.110; -; 1.
DR Gene3D; 3.40.50.10330; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR029477; DAG_kinase_typeI_N.
DR InterPro; IPR037607; DGK.
DR InterPro; IPR038199; DGK_typeI_N_sf.
DR InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR PANTHER; PTHR11255; PTHR11255; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF14513; DAG_kinase_N; 1.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF111331; SSF111331; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR SUPFAM; SSF57889; SSF57889; 2.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Calcium; Cytoplasm; Direct protein sequencing;
KW Kinase; Lipid metabolism; Metal-binding; Nucleotide-binding;
KW Reference proteome; Repeat; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..734
FT /note="Diacylglycerol kinase alpha"
FT /id="PRO_0000218455"
FT DOMAIN 109..144
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 154..189
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 371..505
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT ZN_FING 204..252
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 268..318
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 358..505
FT /note="Necessary and sufficient for the diacylglycerol
FT kinase activity"
FT /evidence="ECO:0000269|PubMed:8809050"
FT BINDING 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 124
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 126
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 133
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 169
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 483
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P23743"
FT MUTAGEN 248
FT /note="K->R: No significant effect on diacylglycerol kinase
FT activity."
FT /evidence="ECO:0000269|PubMed:8809050"
FT MUTAGEN 383
FT /note="K->N: No significant effect on diacylglycerol kinase
FT activity."
FT /evidence="ECO:0000269|PubMed:8809050"
FT MUTAGEN 395
FT /note="K->N: No significant effect on diacylglycerol kinase
FT activity."
FT /evidence="ECO:0000269|PubMed:8809050"
FT MUTAGEN 483
FT /note="K->N: No significant effect on diacylglycerol kinase
FT activity."
FT /evidence="ECO:0000269|PubMed:8809050"
FT MUTAGEN 492
FT /note="K->R: No significant effect on diacylglycerol kinase
FT activity."
FT /evidence="ECO:0000269|PubMed:8809050"
FT MUTAGEN 554
FT /note="K->N: No significant effect on diacylglycerol kinase
FT activity."
FT /evidence="ECO:0000269|PubMed:8809050"
SQ SEQUENCE 734 AA; 82606 MW; 711C2E66FB4B4E80 CRC64;
MSKERGLISP SDFAQLQKYM EYSTKKVSDV LKLFEDGEMA EYLQGDAIGY EGFQQFLKIY
LEVDSVPSHL SLALFQSFQT SYCSEETVKR DVVCLSDVSC YFSLLEGGRP EDKLEFTFKL
YDTDRNGILD SSEVDRIIIQ MMRMAEYLDW DVSELRPILQ EMMKEIDYDG SGSVSLAEWL
RAGATTVPLL VLLGLEMTLK DNGQHMWRPK RFPRPVYCNL CESSIGLGKQ GLSCNLCKYT
VHDQCAMKAL PCEVSTYAKS RKDIGVQTHV WVRGGCESGR CDRCQKKIRI YHSLVGLHCV
WCHLEIHDDC LPAMGHECDC GLLRDHILPP SSIYPSVLAS GQERKVSKTS QKTTDDLNLS
TSEALRIDPV SNTHPLLVFV NPKSGGKQGE RVLWKFQYLL NPRQVFNLLK DGPEPGLRFF
REVPDYRILV CGGDGTVGWI LETIDKANLP FVPPVAVLPL GTGNDLARCL RWGGGYEGQN
LGKILKDLEA SKVVHMDRWS VEVIPQQTEE KSDPVPFQII NNYFSIGVDA SIAHRFHIMR
EKYPEKFNSR MKNKLWYFEF ATSESIFSTC KKLEESLTVE ICGKPLDLSN LSLEGIAVLN
IPSTHGGSNL WGDTKRPHGD IHGINQALGA MAKVITDPDI LKTCVPDLSD KRLEVVGLEG
AIEMGQIYTK LKNAGHRLAK CSEITFHTTK TLPMQIDGEP WMQTPCTIKI THRNQMPMLV
GPPPRSSNFF GFLC
