DAPK3_MOUSE
ID DAPK3_MOUSE Reviewed; 448 AA.
AC O54784;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Death-associated protein kinase 3;
DE Short=DAP kinase 3;
DE EC=2.7.11.1 {ECO:0000269|PubMed:15096528, ECO:0000269|PubMed:16219639, ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:9488481};
DE AltName: Full=DAP-like kinase;
DE Short=Dlk;
DE AltName: Full=MYPT1 kinase;
DE AltName: Full=ZIP-kinase;
GN Name=Dapk3; Synonyms=Zipk;
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 {ECO:0000312|EMBL:BAA24954.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, COFACTOR, FUNCTION IN
RP APOPTOSIS, TISSUE SPECIFICITY, INTERACTION WITH ATF4, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF LYS-42; VAL-422; VAL-429 AND LEU-436.
RX PubMed=9488481; DOI=10.1128/mcb.18.3.1642;
RA Kawai T., Matsumoto M., Takeda K., Sanjo H., Akira S.;
RT "ZIP kinase, a novel serine/threonine kinase which mediates apoptosis.";
RL Mol. Cell. Biol. 18:1642-1651(1998).
RN [2] {ECO:0000305}
RP FUNCTION IN APOPTOSIS, SUBCELLULAR LOCATION, AND INTERACTION WITH DAXX AND
RP PAWR.
RX PubMed=12917339; DOI=10.1128/mcb.23.17.6174-6186.2003;
RA Kawai T., Akira S., Reed J.C.;
RT "ZIP kinase triggers apoptosis from nuclear PML oncogenic domains.";
RL Mol. Cell. Biol. 23:6174-6186(2003).
RN [3]
RP FUNCTION IN PHOSPHORYLATION OF MYL12B, CATALYTIC ACTIVITY, AND FUNCTION IN
RP CYTOSKELETON REORGANIZATION.
RX PubMed=15096528; DOI=10.1083/jcb.200309056;
RA Komatsu S., Ikebe M.;
RT "ZIP kinase is responsible for the phosphorylation of myosin II and
RT necessary for cell motility in mammalian fibroblasts.";
RL J. Cell Biol. 165:243-254(2004).
RN [4]
RP FUNCTION IN PHOSPHORYLATION OF STAT3, CATALYTIC ACTIVITY, AND INTERACTION
RP WITH STAT3.
RX PubMed=16219639; DOI=10.1093/intimm/dxh331;
RA Sato N., Kawai T., Sugiyama K., Muromoto R., Imoto S., Sekine Y.,
RA Ishida M., Akira S., Matsuda T.;
RT "Physical and functional interactions between STAT3 and ZIP kinase.";
RL Int. Immunol. 17:1543-1552(2005).
RN [5]
RP PHOSPHORYLATION AT THR-265.
RX PubMed=16325270; DOI=10.1016/j.imlet.2005.10.015;
RA Sato N., Kamada N., Muromoto R., Kawai T., Sugiyama K., Watanabe T.,
RA Imoto S., Sekine Y., Ohbayashi N., Ishida M., Akira S., Matsuda T.;
RT "Phosphorylation of threonine-265 in zipper-interacting protein kinase
RT plays an important role in its activity and is induced by IL-6 family
RT cytokines.";
RL Immunol. Lett. 103:127-134(2006).
RN [6]
RP INTERACTION WITH UBE2D1; UBE2D2 AND UBE2D3, UBIQUITINATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=18515077; DOI=10.1016/j.bbrc.2008.05.113;
RA Ohbayashi N., Okada K., Kawakami S., Togi S., Sato N., Ikeda O.,
RA Kamitani S., Muromoto R., Sekine Y., Kawai T., Akira S., Matsuda T.;
RT "Physical and functional interactions between ZIP kinase and UbcH5.";
RL Biochem. Biophys. Res. Commun. 372:708-712(2008).
RN [7]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 289-ARG-ARG-290 AND ALA-294.
RX PubMed=20854903; DOI=10.1016/j.cellsig.2010.09.016;
RA Weitzel D.H., Chambers J., Haystead T.A.;
RT "Phosphorylation-dependent control of ZIPK nuclear import is species
RT specific.";
RL Cell. Signal. 23:297-303(2011).
RN [8]
RP FUNCTION, AND INTERACTION WITH NLK AND TCF7L2.
RX PubMed=21454679; DOI=10.1074/jbc.m110.189829;
RA Togi S., Ikeda O., Kamitani S., Nakasuji M., Sekine Y., Muromoto R.,
RA Nanbo A., Oritani K., Kawai T., Akira S., Matsuda T.;
RT "Zipper-interacting protein kinase (ZIPK) modulates canonical Wnt/beta-
RT catenin signaling through interaction with Nemo-like kinase and T-cell
RT factor 4 (NLK/TCF4).";
RL J. Biol. Chem. 286:19170-19177(2011).
RN [9]
RP FUNCTION IN PHOSPHORYLATION OF RPL13A, AND CATALYTIC ACTIVITY.
RX PubMed=23071094; DOI=10.1128/mcb.01168-12;
RA Arif A., Chatterjee P., Moodt R.A., Fox P.L.;
RT "Heterotrimeric GAIT complex drives transcript-selective translation
RT inhibition in murine macrophages.";
RL Mol. Cell. Biol. 32:5046-5055(2012).
CC -!- FUNCTION: Serine/threonine kinase which is involved in the regulation
CC of apoptosis, autophagy, transcription, translation and actin
CC cytoskeleton reorganization. Regulates both type I (caspase-dependent)
CC apoptotic and type II (caspase-independent) autophagic cell deaths
CC signal, depending on the cellular setting. Involved in formation of
CC promyelocytic leukemia protein nuclear body (PML-NB). Involved in
CC apoptosis involving PAWR which mediates cytoplasmic relocation; in
CC vitro phosphorylates PAWR (By similarity). Phosphorylates MYL12B in
CC non-muscle cells leading to reorganization of actin cytoskeleton such
CC as in regulation of cell polarity and cell migration. Positively
CC regulates canonical Wnt/beta-catenin signaling through interaction with
CC NLK and TCF7L2; disrupts the NLK-TCF7L2 complex thereby influencing the
CC phosphorylation of TCF7L2 by NLK. Phosphorylates STAT3 and enhances its
CC transcriptional activity. Enhances transcription from AR-responsive
CC promoters in a hormone- and kinase-dependent manner. Phosphorylates
CC histone H3 on 'Thr-11' at centromeres during mitosis (By similarity).
CC Phosphorylates RPL13A on 'Ser-77' upon interferon-gamma activation
CC which is causing RPL13A release from the ribosome, RPL13A association
CC with the GAIT complex and its subsequent involvement in transcript-
CC selective translation inhibition. {ECO:0000250|UniProtKB:O88764,
CC ECO:0000269|PubMed:12917339, ECO:0000269|PubMed:15096528,
CC ECO:0000269|PubMed:16219639, ECO:0000269|PubMed:21454679,
CC ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:9488481}.
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=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:15096528, ECO:0000269|PubMed:16219639,
CC ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:9488481};
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=2.7.11.1; Evidence={ECO:0000269|PubMed:15096528,
CC ECO:0000269|PubMed:16219639, ECO:0000269|PubMed:23071094,
CC ECO:0000269|PubMed:9488481};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9488481};
CC -!- ACTIVITY REGULATION: A sequential activation is proposed:
CC autophosphorylation at consensus sites is leading to dimerization of
CC the catalytic domain and activation segment exchange (producing an
CC active confirmation of both kinase modules in trans) followed by
CC phosphorylation at Thr-180 in the activation segment and at other
CC regulatory sites (Probable). Phosphorylation at Thr-180, Thr-225 and
CC Thr-265 is essential for activity. Inhibited by pyridone 6 (K00225), a
CC potent, ATP-competitive inhibitor. Phosphorylation at Thr-180, Thr-225
CC and Thr-265 is essential for activity. {ECO:0000250|UniProtKB:O43293}.
CC -!- SUBUNIT: Homooligomer in its kinase-active form (homotrimers and
CC homodimers are reported); monomeric in its kinase-inactive form.
CC Homodimerization is required for activation segment autophosphorylation
CC (By similarity). Interacts with DAXX, PAWR, ATF4, NLK, TCF7L2, UBE2D1,
CC UBE2D2, UBE2D3, and CDC5L. Interacts with AR; enhanced by AATF.
CC {ECO:0000250|UniProtKB:O43293, ECO:0000269|PubMed:12917339,
CC ECO:0000269|PubMed:16219639, ECO:0000269|PubMed:18515077,
CC ECO:0000269|PubMed:21454679, ECO:0000269|PubMed:9488481}.
CC -!- INTERACTION:
CC O54784; Q06507: Atf4; NbExp=3; IntAct=EBI-77359, EBI-77383;
CC O54784; O35613: Daxx; NbExp=2; IntAct=EBI-77359, EBI-77304;
CC O54784; Q925B0: Pawr; NbExp=2; IntAct=EBI-77359, EBI-77397;
CC O54784; P42227: Stat3; NbExp=8; IntAct=EBI-77359, EBI-602878;
CC O54784; P18848: ATF4; Xeno; NbExp=2; IntAct=EBI-77359, EBI-492498;
CC O54784; P61077: UBE2D3; Xeno; NbExp=2; IntAct=EBI-77359, EBI-348268;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18515077,
CC ECO:0000269|PubMed:20854903, ECO:0000269|PubMed:9488481}. Nucleus, PML
CC body {ECO:0000269|PubMed:12917339}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:O88764}. Chromosome, centromere
CC {ECO:0000250|UniProtKB:O88764}. Cytoplasm
CC {ECO:0000250|UniProtKB:O88764}. Note=Predominantly localized to the
CC nucleus. Relocates to the cytoplasm on binding PAWR where the complex
CC appears to interact with actin filaments. Associated with the
CC centrosomes throughout the mitotic cell cycle, with the centromeres
CC from prophase to anaphase and with the contractile ring during
CC cytokinesis (By similarity). {ECO:0000250|UniProtKB:O88764}.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, brain, lung, skeletal
CC muscle, kidney and testis. Lower levels in liver and spleen.
CC {ECO:0000269|PubMed:9488481}.
CC -!- PTM: Ubiquitinated. Ubiquitination mediated by the UBE2D3 E3 ligase
CC does not lead to proteasomal degradation, but influences promyelocytic
CC leukemia protein nuclear bodies (PML-NBs) formation in the nucleus.
CC {ECO:0000269|PubMed:18515077}.
CC -!- PTM: The phosphorylation status is critical for kinase activity,
CC oligomerization and intracellular localization. Phosphorylation at Thr-
CC 180, Thr-225 and Thr-265 is essential for activity. The phosphorylated
CC form is localized in the cytoplasm and nuclear translocation or
CC retention is maximal when it is not phosphorylated. Phosphorylation
CC increases the trimeric form, and its dephosphorylation favors a kinase-
CC inactive monomeric form. {ECO:0000250|UniProtKB:O43293}.
CC -!- MISCELLANEOUS: A species-specific loss of a key phosphorylation site in
CC murine DAPK3 seems to direct it mainly to the nucleus which is proposed
CC to be compensated by the interaction with PAWR to maintain at least the
CC cytoplasmic basic membrane blebbing function in the apoptosis pathway.
CC {ECO:0000250|UniProtKB:O88764}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. DAP kinase subfamily. {ECO:0000305}.
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DR EMBL; AB007143; BAA24954.1; -; mRNA.
DR CCDS; CCDS24045.1; -.
DR RefSeq; NP_001177402.1; NM_001190473.1.
DR RefSeq; NP_031854.1; NM_007828.2.
DR RefSeq; XP_006513258.1; XM_006513195.2.
DR AlphaFoldDB; O54784; -.
DR SMR; O54784; -.
DR BioGRID; 199052; 7.
DR IntAct; O54784; 11.
DR STRING; 10090.ENSMUSP00000137333; -.
DR iPTMnet; O54784; -.
DR PhosphoSitePlus; O54784; -.
DR EPD; O54784; -.
DR PaxDb; O54784; -.
DR PeptideAtlas; O54784; -.
DR PRIDE; O54784; -.
DR ProteomicsDB; 279823; -.
DR Antibodypedia; 11137; 421 antibodies from 43 providers.
DR DNASU; 13144; -.
DR Ensembl; ENSMUST00000047665; ENSMUSP00000035962; ENSMUSG00000034974.
DR Ensembl; ENSMUST00000178422; ENSMUSP00000137333; ENSMUSG00000034974.
DR Ensembl; ENSMUST00000219850; ENSMUSP00000151577; ENSMUSG00000034974.
DR GeneID; 13144; -.
DR KEGG; mmu:13144; -.
DR UCSC; uc007ggg.2; mouse.
DR CTD; 1613; -.
DR MGI; MGI:1203520; Dapk3.
DR VEuPathDB; HostDB:ENSMUSG00000034974; -.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000161753; -.
DR HOGENOM; CLU_000288_63_55_1; -.
DR InParanoid; O54784; -.
DR OMA; PSQIMAG; -.
DR OrthoDB; 813445at2759; -.
DR PhylomeDB; O54784; -.
DR TreeFam; TF314166; -.
DR BioGRID-ORCS; 13144; 7 hits in 75 CRISPR screens.
DR ChiTaRS; Dapk3; mouse.
DR PRO; PR:O54784; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; O54784; protein.
DR Bgee; ENSMUSG00000034974; Expressed in yolk sac and 214 other tissues.
DR ExpressionAtlas; O54784; baseline and differential.
DR Genevisible; O54784; MM.
DR GO; GO:0005884; C:actin filament; ISO:MGI.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0016301; F:kinase activity; ISO:MGI.
DR GO; GO:0043522; F:leucine zipper domain binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:0097190; P:apoptotic signaling pathway; IDA:MGI.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IMP:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; ISO:MGI.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; ISO:MGI.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; ISO:MGI.
DR GO; GO:0043519; P:regulation of myosin II filament organization; IMP:UniProtKB.
DR CDD; cd14105; STKc_DAPK; 1.
DR InterPro; IPR042870; DAPK3_STKc.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Activator; Apoptosis; ATP-binding; Centromere; Chromatin regulator;
KW Chromosome; Cytoplasm; Cytoskeleton; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transcription; Transcription regulation; Transferase; Ubl conjugation.
FT CHAIN 1..448
FT /note="Death-associated protein kinase 3"
FT /id="PRO_0000085915"
FT DOMAIN 13..275
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 161..204
FT /note="Activation segment"
FT /evidence="ECO:0000250|UniProtKB:O96017"
FT REGION 390..448
FT /note="Interaction with CDC5L"
FT /evidence="ECO:0000250|UniProtKB:O88764"
FT REGION 422..436
FT /note="Leucine-zipper"
FT /evidence="ECO:0000303|PubMed:9488481"
FT ACT_SITE 139
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 19..27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43293"
FT MOD_RES 225
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43293"
FT MOD_RES 265
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:16325270"
FT MOD_RES 265
FT /note="Phosphothreonine; by ROCK1"
FT /evidence="ECO:0000250|UniProtKB:O43293"
FT MOD_RES 304
FT /note="Phosphoserine; by DAPK1"
FT /evidence="ECO:0000250|UniProtKB:O43293"
FT MOD_RES 306
FT /note="Phosphoserine; by autocatalysis and DAPK1"
FT /evidence="ECO:0000250|UniProtKB:O43293"
FT MOD_RES 307
FT /note="Phosphoserine; by DAPK1"
FT /evidence="ECO:0000250|UniProtKB:O43293"
FT MOD_RES 313
FT /note="Phosphoserine; by DAPK1"
FT /evidence="ECO:0000250|UniProtKB:O43293"
FT MOD_RES 321
FT /note="Phosphoserine; by DAPK1"
FT /evidence="ECO:0000250|UniProtKB:O43293"
FT MUTAGEN 42
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9488481"
FT MUTAGEN 289..290
FT /note="RR->AA: Nuclear localization."
FT /evidence="ECO:0000269|PubMed:20854903"
FT MUTAGEN 294
FT /note="A->D: Nuclear colocalization."
FT /evidence="ECO:0000269|PubMed:20854903"
FT MUTAGEN 422
FT /note="V->A: Decreased activity; when associated with A-429
FT and A-436."
FT /evidence="ECO:0000269|PubMed:9488481"
FT MUTAGEN 429
FT /note="V->A: Decreased activity; when associated with A-422
FT and A-436."
FT /evidence="ECO:0000269|PubMed:9488481"
FT MUTAGEN 436
FT /note="L->A: Decreased activity; when associated with A-422
FT and A-429."
FT /evidence="ECO:0000269|PubMed:9488481"
SQ SEQUENCE 448 AA; 51422 MW; DA32EF3EB1F20EFC CRC64;
MSTFRQEDVE DHYEMGEELG SGQFAIVRKC QQKGTGMEYA AKFIKKRRLP SSRRGVSREE
IEREVSILRE IRHPNIITLH DVFENKTDVV LILELVSGGE LFDFLAEKES LTEDEATQFL
KQILDGVHYL HSKRIAHFDL KPENIMLLDK HAASPRIKLI DFGIAHRIEA GSEFKNIFGT
PEFVAPEIVN YEPLGLEADM WSIGVITYIL LSGASPFLGE TKQETLTNIS AVNYDFDEEY
FSSTSELAKD FIRRLLVKDP KRRMTIAQSL EHSWIKVRRR EDGARKPERR RLRAARLREY
SLKSHSSMPR NTSYASFERF SRVLEDVAAA EQGLRELQRG RRQCRERVCA LRAAAEQREA
RCRDGSAGLG RDLRRLRTEL GRTEALRTRA QEEARAALLG AGGLKRRLCR LENRYDALAA
QVAAEVQFVR DLVRALEQER LQAECGVR
