TAOK2_RAT
ID TAOK2_RAT Reviewed; 1235 AA.
AC Q9JLS3; A6BM05;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Serine/threonine-protein kinase TAO2;
DE EC=2.7.11.1;
DE AltName: Full=Thousand and one amino acid protein 2;
GN Name=Taok2; Synonyms=Tao2;
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 [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
RP MAP2K3 AND MAP2K6.
RC TISSUE=Brain;
RX PubMed=10497253; DOI=10.1074/jbc.274.40.28803;
RA Chen Z., Hutchison M., Cobb M.H.;
RT "Isolation of the protein kinase TAO2 and identification of its mitogen-
RT activated protein kinase/extracellular signal-regulated kinase kinase
RT binding domain.";
RL J. Biol. Chem. 274:28803-28807(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH PCDH8,
RP SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-57, AND PHOSPHORYLATION AT
RP SER-1038 (ISOFORM 2).
RX PubMed=17988630; DOI=10.1016/j.neuron.2007.08.020;
RA Yasuda S., Tanaka H., Sugiura H., Okamura K., Sakaguchi T., Tran U.,
RA Takemiya T., Mizoguchi A., Yagita Y., Sakurai T., De Robertis E.M.,
RA Yamagata K.;
RT "Activity-induced protocadherin arcadlin regulates dendritic spine number
RT by triggering N-cadherin endocytosis via TAO2beta and p38 MAP kinases.";
RL Neuron 56:456-471(2007).
RN [3] {ECO:0007744|PDB:1U5Q, ECO:0007744|PDB:1U5R}
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-320, AND PHOSPHORYLATION AT
RP SER-181.
RX PubMed=15458637; DOI=10.1016/j.str.2004.07.021;
RA Zhou T., Raman M., Gao Y., Earnest S., Chen Z., Machius M., Cobb M.H.,
RA Goldsmith E.J.;
RT "Crystal structure of the TAO2 kinase domain: activation and specificity of
RT a Ste20p MAP3K.";
RL Structure 12:1891-1900(2004).
RN [4] {ECO:0007744|PDB:2GCD}
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-320 IN COMPLEX WITH
RP STAUROSPORINE, AND ACTIVITY REGULATION.
RX PubMed=16761096; DOI=10.1111/j.1745-7270.2006.00173.x;
RA Zhou T.J., Sun L.G., Gao Y., Goldsmith E.J.;
RT "Crystal structure of the MAP3K TAO2 kinase domain bound by an inhibitor
RT staurosporine.";
RL Acta Biochim. Biophys. Sin. 38:385-392(2006).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in different
CC processes such as membrane blebbing and apoptotic bodies formation DNA
CC damage response and MAPK14/p38 MAPK stress-activated MAPK cascade.
CC Phosphorylates itself, MBP, activated MAPK8, MAP2K3, MAP2K6 and
CC tubulins. Activates the MAPK14/p38 MAPK signaling pathway through the
CC specific activation and phosphorylation of the upstream MAP2K3 and
CC MAP2K6 kinases. In response to DNA damage, involved in the G2/M
CC transition DNA damage checkpoint by activating the p38/MAPK14 stress-
CC activated MAPK cascade, probably by mediating phosphorylation of
CC upstream MAP2K3 and MAP2K6 kinases. May affect microtubule organization
CC and stability. May play a role in the osmotic stress-MAPK8 pathway.
CC Prevents MAP3K7-mediated activation of CHUK, and thus NF-kappa-B
CC activation. Isoform 2, but not isoform 1, is required for PCDH8
CC endocytosis. Following homophilic interactions between PCDH8
CC extracellular domains, isoform 2 phosphorylates and activates
CC MAPK14/p38 MAPK which in turn phosphorylates isoform 2. This process
CC leads to PCDH8 endocytosis and CDH2 cointernalization. Both isoforms
CC are involved in MAPK14/p38 MAPK activation.
CC {ECO:0000269|PubMed:10497253, ECO:0000269|PubMed:17988630}.
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 -!- 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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Moderately inhibited by staurosporine, a broad-
CC range protein kinase inhibitor. {ECO:0000269|PubMed:16761096}.
CC -!- SUBUNIT: Self-associates. Interacts with MAP2K3 and MAP2K6. Interacts
CC with tubulins. Interacts with MAP3K7 and interfers with MAP3K7-binding
CC to CHUK and thus prevents NF-kappa-B activation (By similarity).
CC Isoform 2 interacts with PCDH8; this complex may also include CDH2.
CC {ECO:0000250, ECO:0000269|PubMed:10497253, ECO:0000269|PubMed:16761096,
CC ECO:0000269|PubMed:17988630}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Note=Found to be perinuclear and localized to vesicular
CC compartment. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell projection, dendrite. Note=In
CC dendrites, colocalizes with PCDH8.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=TAO2-alpha;
CC IsoId=Q9JLS3-1; Sequence=Displayed;
CC Name=2; Synonyms=TAO2-beta;
CC IsoId=Q9JLS3-2; Sequence=VSP_040545, VSP_040546, VSP_040547;
CC -!- PTM: Autophosphorylated. Phosphorylated by ATM (By similarity).
CC {ECO:0000250}.
CC -!- PTM: [Isoform 2]: Phosphorylated on Ser-1038 by MAPK14. This
CC phosphorylation is required PCDH8 for endocytosis.
CC {ECO:0000269|PubMed:15458637}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; AF140556; AAD39480.2; -; mRNA.
DR EMBL; AB290408; BAF64457.1; -; mRNA.
DR RefSeq; NP_073193.1; NM_022702.1. [Q9JLS3-1]
DR PDB; 1U5Q; X-ray; 2.10 A; A/B=1-320.
DR PDB; 1U5R; X-ray; 2.10 A; A/B=1-320.
DR PDB; 2GCD; X-ray; 2.55 A; A/B=12-320.
DR PDBsum; 1U5Q; -.
DR PDBsum; 1U5R; -.
DR PDBsum; 2GCD; -.
DR AlphaFoldDB; Q9JLS3; -.
DR SMR; Q9JLS3; -.
DR IntAct; Q9JLS3; 1.
DR STRING; 10116.ENSRNOP00000061854; -.
DR BindingDB; Q9JLS3; -.
DR ChEMBL; CHEMBL4523465; -.
DR iPTMnet; Q9JLS3; -.
DR PhosphoSitePlus; Q9JLS3; -.
DR PaxDb; Q9JLS3; -.
DR GeneID; 64666; -.
DR KEGG; rno:64666; -.
DR UCSC; RGD:621590; rat. [Q9JLS3-1]
DR CTD; 9344; -.
DR RGD; 621590; Taok2.
DR eggNOG; KOG0577; Eukaryota.
DR InParanoid; Q9JLS3; -.
DR OrthoDB; 617606at2759; -.
DR PhylomeDB; Q9JLS3; -.
DR EvolutionaryTrace; Q9JLS3; -.
DR PRO; PR:Q9JLS3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0044295; C:axonal growth cone; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0044294; C:dendritic growth cone; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IDA:RGD.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IDA:RGD.
DR GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; ISO:RGD.
DR GO; GO:0038191; F:neuropilin binding; ISO:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0007409; P:axonogenesis; ISO:RGD.
DR GO; GO:0150020; P:basal dendrite arborization; IGI:ARUK-UCL.
DR GO; GO:0150019; P:basal dendrite morphogenesis; IMP:ARUK-UCL.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0048041; P:focal adhesion assembly; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000165; P:MAPK cascade; IDA:RGD.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0008360; P:regulation of cell shape; ISO:RGD.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0099179; P:regulation of synaptic membrane adhesion; IDA:SynGO.
DR GO; GO:0051403; P:stress-activated MAPK cascade; ISS:UniProtKB.
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 3D-structure; Alternative splicing; ATP-binding; Cell projection;
KW Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Kinase;
KW Magnesium; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1235
FT /note="Serine/threonine-protein kinase TAO2"
FT /id="PRO_0000086735"
FT TRANSMEM 967..987
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 989..1009
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1014..1034
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1040..1060
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1170..1190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 28..281
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 318..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1210..1235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 488..523
FT /evidence="ECO:0000255"
FT COILED 576..603
FT /evidence="ECO:0000255"
FT COILED 683..715
FT /evidence="ECO:0000255"
FT COMPBIAS 344..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..397
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..939
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 34..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 106..108
FT /ligand="staurosporine"
FT /ligand_id="ChEBI:CHEBI:57491"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:16761096,
FT ECO:0007744|PDB:2GCD"
FT BINDING 155
FT /ligand="staurosporine"
FT /ligand_id="ChEBI:CHEBI:57491"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:16761096,
FT ECO:0007744|PDB:2GCD"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UL54"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15458637"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UL54"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZQ29"
FT MOD_RES 777
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UL54"
FT MOD_RES 825
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UL54"
FT MOD_RES 827
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UL54"
FT VAR_SEQ 333
FT /note="E -> ELTPCSQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17988630"
FT /id="VSP_040545"
FT VAR_SEQ 747..1050
FT /note="VRAGQLPMGLPATGALGPLSTGTLSEEQPCSSGQEAILGQRMLGEEEEAVPE
FT RMILGKEGTTLEPEEQRILGEEMGTFSSSPQKHRSLVNEEDWDISKEMKESRVPSLASQ
FT ERNIIGQEEAGAWNLWEKEHGNLVDMEFKLGWVQGPVLTPVPEEEEEEEEEGGAPIGTP
FT RDPGDGCPSPDIPPEPPPSHLRQYPASQLPGFLSHGLLTGLSFAVGSSSGLLPLLLLLL
FT LPLLAAQGGGGLQAALLALEVGLVGLGASYLFLCTALHLPPSLFLLLAQGTALGAVLSL
FT SWRRGLMGVPLGLGAA -> SKELQIKKQFQETCKIQTRQYKALRAHLLETTPKAQHKS
FT LVKRLKEEQTRKLAILAEQYDQSISEMLSSQALRLDETQEAEFQALRQRSNRNWSSLML
FT TRARSKIRTESQHERELRELEQRVALRRALLEQRVEEELLALQTGRSERIRSLLERQAR
FT EIEAFDAESMRLGFSSMALGGIPAEAAAQGYPAPPPAPAWPSRPVPRSGAHWSHGPPPP
FT GMPPPAWRXPALLAPPGPPNWLGPPTQSGTPSGGALLLLRNSPQPLKRAASGGSSGENV
FT GPPAAVPGPLSRSTSVASHILNGSSHFYS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17988630"
FT /id="VSP_040546"
FT VAR_SEQ 1051..1235
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17988630"
FT /id="VSP_040547"
FT MUTAGEN 57
FT /note="K->A: Loss of activity. Loss of MAPK14
FT phosphorylation and of PCDH8 internalization."
FT /evidence="ECO:0000269|PubMed:17988630"
FT CONFLICT 434
FT /note="P -> L (in Ref. 2; BAF64457)"
FT /evidence="ECO:0000305"
FT HELIX 13..18
FT /evidence="ECO:0007829|PDB:1U5Q"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:1U5Q"
FT STRAND 28..36
FT /evidence="ECO:0007829|PDB:1U5Q"
FT STRAND 38..47
FT /evidence="ECO:0007829|PDB:1U5Q"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:1U5Q"
FT STRAND 52..61
FT /evidence="ECO:0007829|PDB:1U5Q"
FT HELIX 66..82
FT /evidence="ECO:0007829|PDB:1U5Q"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:1U5Q"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:1U5Q"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1U5Q"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:1U5Q"
FT HELIX 125..144
FT /evidence="ECO:0007829|PDB:1U5Q"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1U5Q"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:1U5Q"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:1U5Q"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:1U5Q"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:1U5Q"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:1U5Q"
FT HELIX 191..195
FT /evidence="ECO:0007829|PDB:1U5Q"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:2GCD"
FT HELIX 205..220
FT /evidence="ECO:0007829|PDB:1U5Q"
FT TURN 224..227
FT /evidence="ECO:0007829|PDB:1U5Q"
FT HELIX 230..239
FT /evidence="ECO:0007829|PDB:1U5Q"
FT HELIX 252..261
FT /evidence="ECO:0007829|PDB:1U5Q"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:1U5Q"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:1U5Q"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:1U5Q"
FT HELIX 289..303
FT /evidence="ECO:0007829|PDB:1U5Q"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:2GCD"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:1U5Q"
FT HELIX 311..319
FT /evidence="ECO:0007829|PDB:1U5Q"
FT MOD_RES Q9JLS3-2:1038
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17988630"
SQ SEQUENCE 1235 AA; 138751 MW; 426960D0812518AD CRC64;
MPAGGRAGSL KDPDVAELFF KDDPEKLFSD LREIGHGSFG AVYFARDVRN SEVVAIKKMS
YSGKQSNEKW QDIIKEVRFL QKLRHPNTIQ YRGCYLREHT AWLVMEYCLG SASDLLEVHK
KPLQEVEIAA VTHGALQGLA YLHSHNMIHR DVKAGNILLS EPGLVKLGDF GSASIMAPAN
SFVGTPYWMA PEVILAMDEG QYDGKVDVWS LGITCIELAE RKPPLFNMNA MSALYHIAQN
ESPALQSGHW SEYFRNFVDS CLQKIPQDRP TSEVLLKHRF VLRERPPTVI MDLIQRTKDA
VRELDNLQYR KMKKILFQEA PNGPGAEAPE EEEEAEPYMH RAGTLTSLES SHSVPSMSIS
ASSQSSSVNS LADASDNEEE EEEEEEEEEE EEEEGPESRE MAMMQEGEHT VTSHSSIIHR
LPGSDNLYDD PYQPEMTPGP LQPPAAPPTS TSSSSARRRA YCRNRDHFAT IRTASLVSRQ
IQEHEQDSAL REQLSGYKRM RRQHQKQLLA LESRLRGERE EHSGRLQREL EAQRAGFGTE
AEKLARRHQA IGEKEARAAQ AEERKFQQHI LGQQKKELAA LLEAQKRTYK LRKEQLKEEL
QENPSTPKRE KAEWLLRQKE QLQQCQAEEE AGLLRRQRQY FELQCRQYKR KMLLARHSLD
QDLLREDLNK KQTQKDLECA LLLRQHEATR ELELRQLQAV QRTRAELTRL QHQTELGNQL
EYNKRREQEL RQKHAAQVRQ QPKSLKVRAG QLPMGLPATG ALGPLSTGTL SEEQPCSSGQ
EAILGQRMLG EEEEAVPERM ILGKEGTTLE PEEQRILGEE MGTFSSSPQK HRSLVNEEDW
DISKEMKESR VPSLASQERN IIGQEEAGAW NLWEKEHGNL VDMEFKLGWV QGPVLTPVPE
EEEEEEEEGG APIGTPRDPG DGCPSPDIPP EPPPSHLRQY PASQLPGFLS HGLLTGLSFA
VGSSSGLLPL LLLLLLPLLA AQGGGGLQAA LLALEVGLVG LGASYLFLCT ALHLPPSLFL
LLAQGTALGA VLSLSWRRGL MGVPLGLGAA WLLAWPSLAL PLAAMAAGGK WVRQQGPQMR
RGISRLWLRV LLRLSPMVFR ALQGCAAVGD RGLFALYPKT NKNGFRSRLP VPWPRQGNPR
TTQHPLALLA RVWALCKGWN WRLARASHRL ASCLPPWAVH ILASWGLLKG ERPSRIPRLL
PRSQRRLGLS ASRQLPPGTV AGRRSQTRRA LPPWR
