DKF2_CAEEL
ID DKF2_CAEEL Reviewed; 1070 AA.
AC O45818; B1V8I6; G5EEQ6; H9G324; H9G325; O62166; O62167;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 4.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Serine/threonine-protein kinase dkf-2 {ECO:0000303|PubMed:17728253};
DE EC=2.7.11.13;
DE AltName: Full=D kinase family-2 {ECO:0000303|PubMed:17728253};
GN Name=dkf-2; ORFNames=T25E12.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, MUTAGENESIS OF PRO-332;
RP PRO-484; LYS-643; SER-925 AND SER-929, AND PHOSPHORYLATION AT SER-925 AND
RP SER-929.
RX PubMed=17728253; DOI=10.1074/jbc.m701532200;
RA Feng H., Ren M., Chen L., Rubin C.S.;
RT "Properties, regulation, and in vivo functions of a novel protein kinase D:
RT Caenorhabditis elegans DKF-2 links diacylglycerol second messenger to the
RT regulation of stress responses and life span.";
RL J. Biol. Chem. 282:31273-31288(2007).
RN [2] {ECO:0000312|EMBL:CAB04830.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAB04830.2};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, ACTIVITY REGULATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF SER-925 AND SER-929.
RX PubMed=19371715; DOI=10.1016/j.immuni.2009.03.007;
RA Ren M., Feng H., Fu Y., Land M., Rubin C.S.;
RT "Protein kinase D is an essential regulator of C. elegans innate
RT immunity.";
RL Immunity 30:521-532(2009).
CC -!- FUNCTION: Converts transient diacylglycerol (DAG) signals into
CC prolonged physiological effects, downstream of PKC. Acts in the
CC intestine to regulate both innate immunity by promoting activation of
CC PMK-1 and also stress response and life span by acting as an upstream,
CC negative regulator of the daf-16 transcription factor.
CC {ECO:0000269|PubMed:17728253, ECO:0000269|PubMed:19371715}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13;
CC Evidence={ECO:0000269|PubMed:17728253, ECO:0000269|PubMed:19371715};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.13; Evidence={ECO:0000269|PubMed:17728253,
CC ECO:0000269|PubMed:19371715};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17728253, ECO:0000269|PubMed:19371715};
CC -!- ACTIVITY REGULATION: Activated by DAG and phorbol esters. Phorbol-
CC ester/DAG-type domain 1 binds phorbol ester with low affinity. Phorbol-
CC ester/DAG-type domain 2 binds phorbol ester with high affinity and
CC targets the kinase to the cell periphery, enabling phosphorylation and
CC activation by colocalized tpa-1. Both domains 1 and 2 appear to bind
CC DAG with equal affinity so may contribute equally to translocation and
CC activation. {ECO:0000269|PubMed:17728253, ECO:0000269|PubMed:19371715}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17728253}. Membrane
CC {ECO:0000269|PubMed:17728253}. Note=Translocation to the cell membrane
CC is required for kinase activation. {ECO:0000269|PubMed:17728253}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=a {ECO:0000269|PubMed:9851916};
CC IsoId=O45818-1; Sequence=Displayed;
CC Name=b {ECO:0000269|PubMed:9851916};
CC IsoId=O45818-2; Sequence=VSP_053150, VSP_053153, VSP_053154,
CC VSP_053155;
CC Name=c {ECO:0000269|PubMed:9851916};
CC IsoId=O45818-3; Sequence=VSP_053151, VSP_053152;
CC Name=d;
CC IsoId=O45818-4; Sequence=VSP_053247;
CC Name=e;
CC IsoId=O45818-5; Sequence=VSP_053248;
CC Name=f;
CC IsoId=O45818-6; Sequence=VSP_053249;
CC -!- TISSUE SPECIFICITY: Expressed in the late embryo, all larval stages,
CC and adult in the intestine and in cells positioned near the posterior
CC bulb of the pharynx. {ECO:0000269|PubMed:17728253,
CC ECO:0000269|PubMed:19371715}.
CC -!- PTM: Phosphorylation on Ser-925 by tpa-1 is the dominant regulator of
CC catalysis, phosphorylation on Ser-929 by tpa-1 has a lesser effect.
CC Prolonged phosphorylation results in ubiquitination and degradation.
CC {ECO:0000269|PubMed:17728253}.
CC -!- DISRUPTION PHENOTYPE: Increase in adult life span. Increased levels of
CC daf-16 translocate into the nucleus in response to heat stress.
CC Hypersensitive to killing by bacteria. {ECO:0000269|PubMed:17728253,
CC ECO:0000269|PubMed:19371715}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. PKD subfamily. {ECO:0000255}.
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DR EMBL; Z82052; CAB04830.2; -; Genomic_DNA.
DR EMBL; AL021507; CAB04830.2; JOINED; Genomic_DNA.
DR EMBL; AL021572; CAB04830.2; JOINED; Genomic_DNA.
DR EMBL; Z92967; CAB04830.2; JOINED; Genomic_DNA.
DR EMBL; Z92967; CAB07477.1; -; Genomic_DNA.
DR EMBL; Z92967; CAQ35035.1; -; Genomic_DNA.
DR EMBL; AL021507; CAQ35035.1; JOINED; Genomic_DNA.
DR EMBL; AL021572; CAQ35035.1; JOINED; Genomic_DNA.
DR EMBL; Z92967; CCD31057.1; -; Genomic_DNA.
DR EMBL; AL021507; CCD31057.1; JOINED; Genomic_DNA.
DR EMBL; AL021572; CCD31057.1; JOINED; Genomic_DNA.
DR EMBL; Z82052; CCG28246.1; -; Genomic_DNA.
DR EMBL; AL021507; CCG28246.1; JOINED; Genomic_DNA.
DR EMBL; AL021572; CCG28246.1; JOINED; Genomic_DNA.
DR EMBL; Z92967; CCG28246.1; JOINED; Genomic_DNA.
DR EMBL; Z82052; CCG28247.1; -; Genomic_DNA.
DR EMBL; AL021507; CCG28247.1; JOINED; Genomic_DNA.
DR EMBL; AL021572; CCG28247.1; JOINED; Genomic_DNA.
DR EMBL; Z92967; CCG28247.1; JOINED; Genomic_DNA.
DR RefSeq; NP_001123022.1; NM_001129550.1. [O45818-3]
DR RefSeq; NP_001256724.1; NM_001269795.1. [O45818-5]
DR RefSeq; NP_001256725.1; NM_001269796.1. [O45818-6]
DR RefSeq; NP_001256726.1; NM_001269797.1. [O45818-4]
DR RefSeq; NP_507239.2; NM_074838.5. [O45818-1]
DR RefSeq; NP_507240.1; NM_074839.3.
DR AlphaFoldDB; O45818; -.
DR SMR; O45818; -.
DR BioGRID; 45108; 1.
DR STRING; 6239.T25E12.4f; -.
DR iPTMnet; O45818; -.
DR EPD; O45818; -.
DR PaxDb; O45818; -.
DR PeptideAtlas; O45818; -.
DR PRIDE; O45818; -.
DR EnsemblMetazoa; T25E12.4a.1; T25E12.4a.1; WBGene00012019. [O45818-1]
DR EnsemblMetazoa; T25E12.4b.1; T25E12.4b.1; WBGene00012019.
DR EnsemblMetazoa; T25E12.4c.1; T25E12.4c.1; WBGene00012019. [O45818-3]
DR EnsemblMetazoa; T25E12.4d.1; T25E12.4d.1; WBGene00012019. [O45818-4]
DR EnsemblMetazoa; T25E12.4e.1; T25E12.4e.1; WBGene00012019. [O45818-5]
DR EnsemblMetazoa; T25E12.4f.1; T25E12.4f.1; WBGene00012019. [O45818-6]
DR GeneID; 180121; -.
DR KEGG; cel:CELE_T25E12.4; -.
DR UCSC; T25E12.4a; c. elegans.
DR CTD; 180121; -.
DR WormBase; T25E12.4a; CE42484; WBGene00012019; dkf-2. [O45818-1]
DR WormBase; T25E12.4b; CE52401; WBGene00012019; dkf-2. [O45818-2]
DR WormBase; T25E12.4c; CE42507; WBGene00012019; dkf-2. [O45818-3]
DR WormBase; T25E12.4d; CE46242; WBGene00012019; dkf-2. [O45818-4]
DR WormBase; T25E12.4e; CE47100; WBGene00012019; dkf-2. [O45818-5]
DR WormBase; T25E12.4f; CE47405; WBGene00012019; dkf-2. [O45818-6]
DR eggNOG; KOG4236; Eukaryota.
DR GeneTree; ENSGT00950000183024; -.
DR InParanoid; O45818; -.
DR OMA; SIMAPKQ; -.
DR OrthoDB; 367841at2759; -.
DR PhylomeDB; O45818; -.
DR Reactome; R-CEL-1660661; Sphingolipid de novo biosynthesis.
DR PRO; PR:O45818; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00012019; Expressed in larva and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:WormBase.
DR GO; GO:0005829; C:cytosol; IDA:WormBase.
DR GO; GO:0016020; C:membrane; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:1902554; C:serine/threonine protein kinase complex; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004698; F:calcium-dependent protein kinase C activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:WormBase.
DR GO; GO:0004672; F:protein kinase activity; IDA:WormBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:WormBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:WormBase.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR GO; GO:0045087; P:innate immune response; IMP:WormBase.
DR GO; GO:0035556; P:intracellular signal transduction; IMP:WormBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:WormBase.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IGI:WormBase.
DR GO; GO:0006606; P:protein import into nucleus; IMP:WormBase.
DR GO; GO:0089700; P:protein kinase D signaling; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:WormBase.
DR CDD; cd00029; C1; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR015727; Protein_Kinase_C_mu-related.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22968; PTHR22968; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Immunity; Innate immunity;
KW Kinase; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1070
FT /note="Serine/threonine-protein kinase dkf-2"
FT /id="PRO_0000385354"
FT DOMAIN 624..726
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 770..1026
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ZN_FING 321..371
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 473..523
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 42..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 893
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 776..784
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 799
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9XUJ7,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 925
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17728253"
FT MOD_RES 929
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17728253"
FT VAR_SEQ 1..533
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_053150"
FT VAR_SEQ 1..222
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_053247"
FT VAR_SEQ 1..197
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_053151"
FT VAR_SEQ 198..310
FT /note="DHSDDEVWTPYRPPPNREYSSSSEPMMGDLTFRLQSGIHKKSIAVEGTEIAL
FT RDLRNEALQFIKEIYPEKGCSSLEDYILLYKHDLRSINILQLITTSSDVTDGTLVEVVI
FT GS -> MTDRHPESKTSTSSNSPSISSSTSSSLKMMKKQQRAKSCATPNSGRKSPRLEV
FT KAMTISSSPTAQRFVFQQQASFQVLEDFENLKVYEEKEKQRKKEKAPDVGRRTYIVIGA
FT (in isoform c)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_053152"
FT VAR_SEQ 470..471
FT /note="Missing (in isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_053248"
FT VAR_SEQ 534..701
FT /note="LGSQADDGASEDRDDDLSLRSGSGAHKKAQNTPSAPLQGSEGSGSPGPVVSF
FT AANALSNMPDDDVISSESANIPLMRVVMSKKQTKRKNNKLLKEGWIVHYTDQQNMRKKH
FT YWRLDTKGITMYQDENTTRYYKEIPLNEILNVSMSPPDKTADYLFEIRTGVCVYFIS
FT -> MILNILRLPHADEPTTSQSVQDYPLVHFSPRRHQKFRTIISVGDSDVIKDSSLTDE
FT ELYNIIHASPIARKSSTVSSTDSGYLGSSGASSSCVRSREGSTVSSTITVERTRRGGST
FT ASSEPDSVADSEGAGSYSSFSSIASTASRMLGRAADCLVLMTKRNGWSGDA (in
FT isoform b)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_053153"
FT VAR_SEQ 541
FT /note="G -> GTSLTGSMDNLRMCSVPFGSDQSTSG (in isoform f)"
FT /evidence="ECO:0000305"
FT /id="VSP_053249"
FT VAR_SEQ 750..755
FT /note="ETGHLG -> KTRPPY (in isoform b)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_053154"
FT VAR_SEQ 756..1070
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_053155"
FT MUTAGEN 332
FT /note="P->G: Loss of sensitivity to phorbol ester or DAG
FT stimulation of kinase activity; when associated with G-484.
FT No effect on sensitivity to phorbol ester, loss of DAG
FT stimulation of kinase activity."
FT /evidence="ECO:0000269|PubMed:17728253"
FT MUTAGEN 484
FT /note="P->G: Loss of sensitivity to phorbol ester or DAG
FT stimulation of kinase activity. Loss of sensitivity to
FT phorbol ester or DAG stimulation of kinase activity; when
FT associated with G-332."
FT /evidence="ECO:0000269|PubMed:17728253"
FT MUTAGEN 643
FT /note="K->A: Small increase in basal kinase activity, no
FT effect on sensitivity to phorbol ester stimulation of
FT kinase activity."
FT /evidence="ECO:0000269|PubMed:17728253"
FT MUTAGEN 925
FT /note="S->A: Loss of sensitivity to phorbol ester
FT stimulation of kinase activity."
FT /evidence="ECO:0000269|PubMed:17728253,
FT ECO:0000269|PubMed:19371715"
FT MUTAGEN 925
FT /note="S->D: High basal kinase activity, loss of phorbol
FT ester-stimulated kinase activity and ability to
FT phosphorylate pmk-1; when associated with D-929."
FT /evidence="ECO:0000269|PubMed:17728253,
FT ECO:0000269|PubMed:19371715"
FT MUTAGEN 929
FT /note="S->A: Moderate loss of sensitivity to phorbol ester
FT stimulation of kinase activity."
FT /evidence="ECO:0000269|PubMed:17728253,
FT ECO:0000269|PubMed:19371715"
FT MUTAGEN 929
FT /note="S->D: High basal kinase activity, loss of phorbol
FT ester-stimulated kinase activity and ability to
FT phosphorylate pmk-1; when associated with D-925."
FT /evidence="ECO:0000269|PubMed:17728253,
FT ECO:0000269|PubMed:19371715"
SQ SEQUENCE 1070 AA; 120583 MW; 6A4891629C021973 CRC64;
MDANDYPRLY YTSMPSSSTS MVTTTRFSTS FSPSIPCHRQ ENFRRHSTSA LAKRNGSESE
KSAEIRENPD EIEVSRVSGR DSSLAFYTTA HETSSMLSRD SRDETLTPNE HIHQASSRRV
SANDSVFEDG YVDFVDEPRE HGSRRKSFEK FTDRNGEEKE GRVFELSTPQ PTREAAPGAH
QFQLPTLLVT STPTTVFDHS DDEVWTPYRP PPNREYSSSS EPMMGDLTFR LQSGIHKKSI
AVEGTEIALR DLRNEALQFI KEIYPEKGCS SLEDYILLYK HDLRSINILQ LITTSSDVTD
GTLVEVVIGS CPQNERIVVH PHTLFVHSYK VPTFCDFCGE LLFGLVKQGL KCFGCGLNYH
KRCASKIPNN CNGSKQRRPS AIPLSPSNSN ILNLNERRHS RRESCLEALD AARPSSTLGG
AATPNIFITS DDCGDAVGGN YLQMPRKDRS CSWSGRPLWM EIAEATRVKL QVPHTFQVHS
YKLPTVCQHC KKLLKGLIRQ GMQCRDCKYN CHKKCSEHVA KDCSGNTKAS QFFLGSQADD
GASEDRDDDL SLRSGSGAHK KAQNTPSAPL QGSEGSGSPG PVVSFAANAL SNMPDDDVIS
SESANIPLMR VVMSKKQTKR KNNKLLKEGW IVHYTDQQNM RKKHYWRLDT KGITMYQDEN
TTRYYKEIPL NEILNVSMSP PDKTADYLFE IRTGVCVYFI SGSPSDEKGS SLDAQSWTTA
IQSALMPVTP QSSVVGGKRI DKLKVPTEGE TGHLGAKIQT EHEFSQLYQI FAEEVLGSGQ
FGTVYGGIHR RNGQHVAVKL IDKLKFPPNK EDLLRAEVQI LEKVDHPGVV HFMQMLETTD
RIFVVMEKLK GDMLEMILSS EKGRLSERTT QFLVAQILEA LRYLHHLNIV HCDLKPENIL
LNSNSDFPQV KLCDFGFARI IGEKSFRRSV VGTPAYLAPE VLRNKGFNRS LDMWSVGVIV
YVSLSGTFPF NEDEDINDQI QNAEFMYPPT PWKEISENAI EFINGLLQVK MSKRYTVTKA
QSQIWMQNYT LWSDLRVLEK AVGQRFVTHE SDDVRWQAYE KEHNVTPVYV
