MRCKB_MOUSE
ID MRCKB_MOUSE Reviewed; 1713 AA.
AC Q7TT50; E9QK15; Q69ZR5; Q80W33;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Serine/threonine-protein kinase MRCK beta;
DE EC=2.7.11.1;
DE AltName: Full=CDC42-binding protein kinase beta;
DE AltName: Full=DMPK-like beta;
DE AltName: Full=Myotonic dystrophy kinase-related CDC42-binding kinase beta;
DE Short=MRCK beta;
DE Short=Myotonic dystrophy protein kinase-like beta;
GN Name=Cdc42bpb {ECO:0000312|EMBL:AAP34402.1, ECO:0000312|MGI:MGI:2136459};
GN Synonyms=Kiaa1124 {ECO:0000312|EMBL:BAD32381.1};
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;
RN [1] {ECO:0000312|EMBL:AAP34402.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Huang C.Q., Wu S.L., Cheng Z.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAD32381.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 628-1713.
RC TISSUE=Fetal brain {ECO:0000312|EMBL:BAD32381.1};
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [4] {ECO:0000312|EMBL:AAP34402.1}
RP PROTEIN SEQUENCE OF 633-642, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAH49921.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1139-1713.
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH49921.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH49921.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH CPNE4.
RX PubMed=12522145; DOI=10.1074/jbc.m212632200;
RA Tomsig J.L., Snyder S.L., Creutz C.E.;
RT "Identification of targets for calcium signaling through the copine family
RT of proteins. Characterization of a coiled-coil copine-binding motif.";
RL J. Biol. Chem. 278:10048-10054(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-954, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1692 AND SER-1695, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1692, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-927; SER-1688; SER-1692 AND
RP SER-1695, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP FUNCTION, AND INTERACTION WITH FAM89B AND LIMK1.
RX PubMed=25107909; DOI=10.1074/jbc.m114.588079;
RA Lee I.C., Leung T., Tan I.;
RT "Adaptor protein LRAP25 mediates myotonic dystrophy kinase-related Cdc42-
RT binding kinase (MRCK) regulation of LIMK1 protein in lamellipodial F-actin
RT dynamics.";
RL J. Biol. Chem. 289:26989-27003(2014).
CC -!- FUNCTION: Serine/threonine-protein kinase which is an important
CC downstream effector of CDC42 and plays a role in the regulation of
CC cytoskeleton reorganization and cell migration. Regulates actin
CC cytoskeletal reorganization via phosphorylation of PPP1R12C and
CC MYL9/MLC2. In concert with MYO18A and LURAP1, is involved in modulating
CC lamellar actomyosin retrograde flow that is crucial to cell protrusion
CC and migration. Phosphorylates PPP1R12A (By similarity). In concert with
CC FAM89B/LRAP25 mediates the targeting of LIMK1 to the lamellipodium
CC resulting in its activation and subsequent phosphorylation of CFL1
CC which is important for lamellipodial F-actin regulation
CC (PubMed:25107909). {ECO:0000250|UniProtKB:Q7TT49,
CC ECO:0000269|PubMed:25107909}.
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:0000250|UniProtKB:Q5VT25};
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:0000250|UniProtKB:Q5VT25};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q5VT25};
CC -!- ACTIVITY REGULATION: Maintained in an inactive, closed conformation by
CC an interaction between the kinase domain and the negative
CC autoregulatory C-terminal coiled-coil region. Agonist binding to the
CC phorbol ester binding site disrupts this, releasing the kinase domain
CC to allow N-terminus-mediated dimerization and kinase activation by
CC transautophosphorylation. Inhibited by chelerythrine chloride (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer and homotetramer via the coiled coil regions.
CC Interacts tightly with GTP-bound but not GDP-bound CDC42. Interacts
CC with TJP1; this interaction requires the presence of catalytically
CC active CDC42. Forms a tripartite complex with MYO18A and LURAP1 with
CC the latter acting as an adapter connecting CDC42BPB and MYO18A. LURAP1
CC binding results in activation of CDC42BPB by abolition of its negative
CC autoregulation. Interacts with STRIP1, STRN3 and SIKE1 (By similarity).
CC Interacts with CPNE4 (via VWFA domain) (PubMed:12522145). Interacts
CC with LURAP1 (By similarity). Interacts (via AGC-kinase C-terminal
CC domain) with FAM89B/LRAP25 (via LRR repeat)(PubMed:25107909). Forms a
CC tripartite complex with FAM89B/LRAP25 and LIMK1 (PubMed:25107909).
CC {ECO:0000250|UniProtKB:Q7TT49, ECO:0000250|UniProtKB:Q9Y5S2,
CC ECO:0000269|PubMed:12522145, ECO:0000269|PubMed:25107909}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Cell junction {ECO:0000250}. Cell projection,
CC lamellipodium {ECO:0000250|UniProtKB:Q3UU96}. Note=Displays a dispersed
CC punctate distribution and concentrates along the cell periphery,
CC especially at the leading edge and cell-cell junction. This
CC concentration is PH-domain dependent. Detected at the leading edge of
CC migrating and wounded cells; this localization requires the presence of
CC catalytically active CDC42. Localizes in the lamellipodium in a
CC FAM89B/LRAP25-dependent manner. {ECO:0000250|UniProtKB:O54874,
CC ECO:0000250|UniProtKB:Q3UU96, ECO:0000250|UniProtKB:Q7TT49}.
CC -!- PTM: Proteolytically cleaved by caspases upon apoptosis induction.
CC {ECO:0000250|UniProtKB:Q9Y5S2}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. DMPK subfamily. {ECO:0000305}.
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DR EMBL; AY277589; AAP34402.1; -; mRNA.
DR EMBL; AC127580; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK173103; BAD32381.1; -; mRNA.
DR EMBL; BC049921; AAH49921.1; -; mRNA.
DR CCDS; CCDS26176.1; -.
DR RefSeq; NP_898837.2; NM_183016.2.
DR AlphaFoldDB; Q7TT50; -.
DR SMR; Q7TT50; -.
DR BioGRID; 229972; 5.
DR IntAct; Q7TT50; 1.
DR MINT; Q7TT50; -.
DR STRING; 10090.ENSMUSP00000042565; -.
DR iPTMnet; Q7TT50; -.
DR PhosphoSitePlus; Q7TT50; -.
DR SwissPalm; Q7TT50; -.
DR jPOST; Q7TT50; -.
DR MaxQB; Q7TT50; -.
DR PaxDb; Q7TT50; -.
DR PRIDE; Q7TT50; -.
DR ProteomicsDB; 290056; -.
DR Antibodypedia; 14692; 178 antibodies from 28 providers.
DR DNASU; 217866; -.
DR Ensembl; ENSMUST00000041965; ENSMUSP00000042565; ENSMUSG00000021279.
DR GeneID; 217866; -.
DR KEGG; mmu:217866; -.
DR UCSC; uc007pct.2; mouse.
DR CTD; 9578; -.
DR MGI; MGI:2136459; Cdc42bpb.
DR VEuPathDB; HostDB:ENSMUSG00000021279; -.
DR eggNOG; KOG0612; Eukaryota.
DR GeneTree; ENSGT01030000234517; -.
DR HOGENOM; CLU_000288_140_3_1; -.
DR InParanoid; Q7TT50; -.
DR OMA; CGRSHHV; -.
DR OrthoDB; 759391at2759; -.
DR PhylomeDB; Q7TT50; -.
DR TreeFam; TF313551; -.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR BioGRID-ORCS; 217866; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Cdc42bpb; mouse.
DR PRO; PR:Q7TT50; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q7TT50; protein.
DR Bgee; ENSMUSG00000021279; Expressed in animal zygote and 217 other tissues.
DR ExpressionAtlas; Q7TT50; baseline and differential.
DR Genevisible; Q7TT50; MM.
DR GO; GO:0042641; C:actomyosin; ISO:MGI.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; ISO:MGI.
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:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0031032; P:actomyosin structure organization; ISO:MGI.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0051179; P:localization; IEA:UniProt.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR CDD; cd00029; C1; 1.
DR CDD; cd05624; STKc_MRCK_beta; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR031597; KELK.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033232; MRCK_beta.
DR InterPro; IPR042718; MRCKB_STKc.
DR InterPro; IPR014930; Myotonic_dystrophy_kinase_coil.
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; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22988:SF34; PTHR22988:SF34; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF08826; DMPK_coil; 1.
DR Pfam; PF15796; KELK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50108; CRIB; 1.
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; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell junction; Cell membrane; Cell projection; Coiled coil;
KW Cytoplasm; Direct protein sequencing; Kinase; Magnesium; Membrane;
KW Metal-binding; Methylation; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..1713
FT /note="Serine/threonine-protein kinase MRCK beta"
FT /id="PRO_0000086395"
FT DOMAIN 76..342
FT /note="Protein kinase"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 343..413
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 1096..1215
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1241..1515
FT /note="CNH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT DOMAIN 1585..1598
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT ZN_FING 1026..1076
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 971..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1616..1713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 434..649
FT /evidence="ECO:0000255"
FT COILED 681..815
FT /evidence="ECO:0000255"
FT COILED 878..939
FT /evidence="ECO:0000255"
FT COMPBIAS 971..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1662..1676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 200
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P54265,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 82..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P54265,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 221
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 233
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 239
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 423
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5S2"
FT MOD_RES 671
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5S2"
FT MOD_RES 927
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 954
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 1682
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5S2"
FT MOD_RES 1684
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5S2"
FT MOD_RES 1688
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1692
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 1695
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 96
FT /note="K -> R (in Ref. 1; AAP34402)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1713 AA; 194753 MW; CD809A3743986A4D CRC64;
MSAKVRLKKL EQLLLDGPWR NDSALSVETL LDVLVCLYTE CSHSALRRDK YVAEFLEWAK
PFTQLVKDMQ LHREDFEIIK VIGRGAFGEV AVVKMKNTER IYAMKILNKW EMLKRAETAC
FREERDVLVN GDCQWITALH YAFQDENYLY LVMDYYVGGD LLTLLSKFED KLPEDMARFY
IGEMVLAIDS IHQLHYVHRD IKPDNVLLDV NGHIRLADFG SCLKMNDDGT VQSSVAVGTP
DYISPEILQA MEDGMGKYGP ECDWWSLGVC MYEMLYGETP FYAESLVETY GKIMNHEERF
QFPSHVTDVS EEAKDLIQRL ICSRERRLGQ NGIEDFKKHA FFEGLNWENI RNLEAPYIPD
VSSPSDTSNF DVDDDMLRNI EILPPGSHTG FSGLHLPFIG FTFTTESCFS DRGSLKSMTQ
SNTLTKDEDV QRDLENSLQI EAYERRIRRL EQEKLELSRK LQESTQTVQS LHGSTRALGN
SNRDKEIKRL NEELERMKSK MADSNRLERQ LEDTVTLRQE HEDSTHRLKG LEKQYRLARQ
EKEELHKQLV EASERLKSQT KELKDAHQQR KRALQEFSEL NERMSELRSL KQKVSRQLRD
KEEEMEVAMQ KIDSMRQDLR KSEKSRKELE ARLEDAAAEA SKERKLREHS ESFCKQMERE
LEALKVKQGG RGPGAASEHQ QEISKIRSEL EKKVLFYEEE LVRREASHVL EVKNVKKEVH
DSESHQLALQ KEVLMLKDKL EKSKRERHSE MEEAIGTVKD KYERERAMLF DENKKLTAEN
EKLCSFVDKL TAQNRQLEDE LQDLASKKES VAHWEAQIAE IIQWVSDEKD ARGYLQALAS
KMTEELETLR SSSLGSRTLD PLWKVRRSQK LDMSARLELQ SALEAEIRAK QLVQEELRKV
KDSSLAFESK LKESEAKNRE LLEEMQSLRK RMEEKFRADT GLKLPDFQDS IFEYFNTAPL
AHDLTFRTSS ASDQETQASK MDLSPSVSVA TSTEQQEDMA RPQQRPSPVP LPSTQALAMA
GPKPKAHQFS IKSFPSPTQC SHCTSLMVGL IRQGYACEVC AFSCHVSCKD SAPQVCPIPP
EQSKRPLGVD VQRGIGTAYK GYVKVPKPTG VKKGWQRAYA VVCDCKLFLY DLPEGKSTQP
GVVASQVLDL RDEEFAVSSV LASDVIHATR RDIPCIFRVT ASLLGSPSKT SSLLILTENE
NEKRKWVGIL EGLQAILHKN RLKSQVVHVA QEAYDSSLPL IKAVLAAAIV DGDRIAVGLE
EGLYVIELTR DVIVRAADCK KVYQIELAPK EKIAILLCGR NHHVHLYPWS SFDGAEASNF
DIKLPETKGC QLIATGTLRK SSSTCLFVAV KRLILCYEIQ RTKPFHRKFS ELVAPGHVQW
MAVFKDRLCV GYPSGFSLLS IQGDGPPLDL VNPTDPSLAF LSQQSFDALC AVELKSEEYL
LCFSHMGLYV DPQGRRSRMQ ELMWPAAPVA CSCSPTHVTV YSEYGVDVFD VRTMEWVQTI
GLRRIRPLNS DGSLNLLGCE PPRLIYFKNK FSGTILNVPD TSDNSKKQML RTRSKRRFVF
KVPEEERLQQ RREMLRDPEL RSKMISNPTN FNHVAHMGPG DGMQVLMDLP LSAAPTVQEE
KQGPTPAGLP RQPPSRSKPY VSWPSSGGSE PGVPVPLRSM SDPDQDFDKE PDSDSTKHST
PSNSSNPSGP PSPNSPHRSQ LPMEGLDQPS CDA
