MINK1_MOUSE
ID MINK1_MOUSE Reviewed; 1308 AA.
AC Q9JM52; Q5SXG2; Q921M6; Q9JM92;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Misshapen-like kinase 1;
DE EC=2.7.11.1;
DE AltName: Full=GCK family kinase MiNK;
DE AltName: Full=MAPK/ERK kinase kinase kinase 6;
DE Short=MEK kinase kinase 6;
DE Short=MEKKK 6;
DE AltName: Full=Misshapen/NIK-related kinase;
DE AltName: Full=Mitogen-activated protein kinase kinase kinase kinase 6;
GN Name=Mink1 {ECO:0000250|UniProtKB:Q8N4C8};
GN Synonyms=Map4k6 {ECO:0000312|MGI:MGI:1355329},
GN Mink {ECO:0000312|EMBL:BAA94837.1};
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 {ECO:0000312|EMBL:BAA94837.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=10708748; DOI=10.1016/s0014-5793(00)01247-3;
RA Dan I., Watanabe N.M., Kobayashi T., Yamashita-Suzuki K., Fukagaya Y.,
RA Kajikawa E., Kimura W.K., Nakashima T.M., Matsumoto K., Ninomiya-Tsuji J.,
RA Kusumi A.;
RT "Molecular cloning of MINK, a novel member of mammalian GCK family kinases,
RT which is up-regulated during postnatal mouse cerebral development.";
RL FEBS Lett. 469:19-23(2000).
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}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 148-1308 (ISOFORM 3).
RC TISSUE=Mammary gland;
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 [5] {ECO:0000305}
RP PROTEIN SEQUENCE OF 735-742 AND 908-920, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP FUNCTION, AND INTERACTION WITH NCK1.
RX PubMed=15608642; DOI=10.1038/ni1145;
RA McCarty N., Paust S., Ikizawa K., Dan I., Li X., Cantor H.;
RT "Signaling by the kinase MINK is essential in the negative selection of
RT autoreactive thymocytes.";
RL Nat. Immunol. 6:65-72(2005).
RN [7]
RP ERRATUM OF PUBMED:15608642.
RX DOI=10.1038/ni0205-219a;
RA McCarty N., Paust S., Ikizawa K., Dan I., Li X., Cantor H.;
RL Nat. Immunol. 6:219-219(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729, 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-324; SER-326; SER-729;
RP SER-746; SER-750 AND THR-867, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP SER-702 (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, 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 METHYLATION [LARGE SCALE ANALYSIS] AT ARG-503 AND ARG-511, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Serine/threonine kinase which acts as a negative regulator of
CC Ras-related Rap2-mediated signal transduction to control neuronal
CC structure and AMPA receptor trafficking. Required for normal synaptic
CC density, dendrite complexity, as well as surface AMPA receptor
CC expression in hippocampal neurons. Can activate the JNK and MAPK14/p38
CC pathways and mediates stimulation of the stress-activated protein
CC kinase MAPK14/p38 MAPK downstream of the Raf/ERK pathway.
CC Phosphorylates: TANC1 upon stimulation by RAP2A, MBP and SMAD1. Has an
CC essential function in negative selection of thymocytes, perhaps by
CC coupling NCK1 to activation of JNK1. {ECO:0000269|PubMed:10708748,
CC ECO:0000269|PubMed:15608642}.
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:10708748};
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:10708748};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10708748};
CC -!- SUBUNIT: Interacts with RAP2A and TANC1 (By similarity). Interacts with
CC NCK1. {ECO:0000250, ECO:0000269|PubMed:15608642}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Postsynaptic density
CC {ECO:0000250}. Cell projection, axon {ECO:0000250}. Cell projection,
CC dendrite {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=2 {ECO:0000269|PubMed:10708748}; Synonyms=MiNK-2;
CC IsoId=Q9JM52-1; Sequence=Displayed;
CC Name=1 {ECO:0000269|PubMed:10708748}; Synonyms=MiNK-1;
CC IsoId=Q9JM52-2; Sequence=VSP_007062;
CC Name=3 {ECO:0000269|PubMed:10708748};
CC IsoId=Q9JM52-3; Sequence=VSP_007061;
CC -!- TISSUE SPECIFICITY: Appears to be ubiquitous, expressed in all tissue
CC types examined. Highly expressed in the brain, moderately expressed in
CC kidney and spleen, low levels present in heart and skeletal muscle.
CC Isoform 2 is more abundant in the brain than isoform 1.
CC {ECO:0000269|PubMed:10708748}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during postnatal brain development.
CC {ECO:0000269|PubMed:10708748}.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
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; AB041925; BAA94837.1; -; mRNA.
DR EMBL; AB035697; BAA90752.1; -; mRNA.
DR EMBL; AL592547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR933736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466596; EDL12579.1; -; Genomic_DNA.
DR EMBL; BC011346; AAH11346.1; -; mRNA.
DR CCDS; CCDS24954.1; -. [Q9JM52-2]
DR CCDS; CCDS24955.1; -. [Q9JM52-1]
DR RefSeq; NP_057922.2; NM_016713.2. [Q9JM52-2]
DR RefSeq; NP_795712.2; NM_176893.2. [Q9JM52-1]
DR RefSeq; XP_006533744.1; XM_006533681.3. [Q9JM52-3]
DR AlphaFoldDB; Q9JM52; -.
DR SMR; Q9JM52; -.
DR BioGRID; 206164; 12.
DR CORUM; Q9JM52; -.
DR IntAct; Q9JM52; 6.
DR STRING; 10090.ENSMUSP00000072649; -.
DR iPTMnet; Q9JM52; -.
DR PhosphoSitePlus; Q9JM52; -.
DR EPD; Q9JM52; -.
DR jPOST; Q9JM52; -.
DR MaxQB; Q9JM52; -.
DR PaxDb; Q9JM52; -.
DR PeptideAtlas; Q9JM52; -.
DR PRIDE; Q9JM52; -.
DR ProteomicsDB; 295942; -. [Q9JM52-1]
DR ProteomicsDB; 295943; -. [Q9JM52-2]
DR ProteomicsDB; 295944; -. [Q9JM52-3]
DR Antibodypedia; 5678; 240 antibodies from 32 providers.
DR DNASU; 50932; -.
DR Ensembl; ENSMUST00000102558; ENSMUSP00000099618; ENSMUSG00000020827. [Q9JM52-2]
DR Ensembl; ENSMUST00000102559; ENSMUSP00000099619; ENSMUSG00000020827. [Q9JM52-1]
DR GeneID; 50932; -.
DR KEGG; mmu:50932; -.
DR UCSC; uc007jvj.1; mouse. [Q9JM52-1]
DR UCSC; uc007jvl.1; mouse. [Q9JM52-2]
DR CTD; 50488; -.
DR MGI; MGI:1355329; Mink1.
DR VEuPathDB; HostDB:ENSMUSG00000020827; -.
DR eggNOG; KOG0587; Eukaryota.
DR GeneTree; ENSGT00950000183196; -.
DR HOGENOM; CLU_001831_2_0_1; -.
DR InParanoid; Q9JM52; -.
DR OrthoDB; 533537at2759; -.
DR Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
DR BioGRID-ORCS; 50932; 3 hits in 78 CRISPR screens.
DR ChiTaRS; Mink1; mouse.
DR PRO; PR:Q9JM52; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9JM52; protein.
DR Bgee; ENSMUSG00000020827; Expressed in visual cortex and 241 other tissues.
DR ExpressionAtlas; Q9JM52; baseline and differential.
DR Genevisible; Q9JM52; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IDA: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:0031532; P:actin cytoskeleton reorganization; ISO:MGI.
DR GO; GO:0007420; P:brain development; IEP:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; ISS:UniProtKB.
DR GO; GO:0048813; P:dendrite morphogenesis; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0045060; P:negative thymic T cell selection; IMP:MGI.
DR GO; GO:0070050; P:neuron cellular homeostasis; ISO:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:UniProtKB.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; IDA:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; ISS:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; ISO:MGI.
DR GO; GO:0022407; P:regulation of cell-cell adhesion; ISO:MGI.
DR GO; GO:0001952; P:regulation of cell-matrix adhesion; ISO:MGI.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR InterPro; IPR001180; CNH_dom.
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; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50219; CNH; 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 Alternative splicing; ATP-binding; Cell projection; Cytoplasm;
KW Direct protein sequencing; Kinase; Methylation; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Synapse; Transferase.
FT CHAIN 1..1308
FT /note="Misshapen-like kinase 1"
FT /id="PRO_0000086330"
FT DOMAIN 25..289
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 995..1282
FT /note="CNH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT REGION 299..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..1308
FT /note="Mediates interaction with RAP2A"
FT /evidence="ECO:0000250"
FT REGION 881..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..335
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..575
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..665
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..801
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..820
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 153
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 31..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 503
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 511
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 644
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N4C8"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N4C8"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 745
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N4C8"
FT MOD_RES 746
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 750
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 867
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 698
FT /note="A -> ARPRSNSAWQIYLQRRAERGTPKPPGPPAQPPGPPNAS (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007061"
FT VAR_SEQ 769..776
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:10708748"
FT /id="VSP_007062"
FT CONFLICT 221
FT /note="I -> V (in Ref. 4; AAH11346)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="F -> L (in Ref. 4; AAH11346)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="E -> R (in Ref. 4; AAH11346)"
FT /evidence="ECO:0000305"
FT CONFLICT 542..546
FT /note="AKPSS -> RSQAG (in Ref. 1; BAA90752/BAA94837)"
FT /evidence="ECO:0000305"
FT CONFLICT 832
FT /note="Missing (in Ref. 4; AAH11346)"
FT /evidence="ECO:0000305"
FT CONFLICT 840
FT /note="S -> T (in Ref. 1; BAA94837/BAA90752)"
FT /evidence="ECO:0000305"
FT MOD_RES Q9JM52-3:702
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1308 AA; 147295 MW; 455E546EC5459B47 CRC64;
MGDPAPARSL DDIDLSALRD PAGIFELVEV VGNGTYGQVY KGRHVKTGQL AAIKVMDVTE
DEEEEIKQEI NMLKKYSHHR NIATYYGAFI KKSPPGNDDQ LWLVMEFCGA GSVTDLVKNT
KGNALKEDCI AYICREILRG LAHLHAHKVI HRDIKGQNVL LTENAEVKLV DFGVSAQLDR
TVGRRNTFIG TPYWMAPEVI ACDENPDATY DYRSDIWSLG ITAIEMAEGA PPLCDMHPMR
ALFLIPRNPP PRLKSKKWSK KFTDFIDTCL IKTYLSRPPT EQLLKFPFIR DQPTERQVRI
QLKDHIDRSR KKRGEKEETE YEYSGSEEED DSHGEEGEPS SIMNVPGEST LRREFLRLQQ
ENKSNSEALK QQQQLQQQQQ RDPEAHIKHL LHQRQRRIEE QKEERRRVEE QQRREREQRK
LQEKEQQRRL EDMQALRREE ERRQAEREQE YKRKQLEEQR QSERLQRQLQ QEHAYLKSLQ
QQQQQQQLQK QQQQQQQILP GDRKPLYHYG RGINPADKPA WAREVEERAR MNKQQNSPLA
KAKPSSAGPE PPISQASPSP PGPLSQTPPM QRPVEPQEGP HKSLVAHRVP LKPYAAPVPR
SQSLQDQPTR NLAAFPASHD PDPAAVPTPT ATPSARGAVI RQNSDPTSEG PGPSPNPPSW
VRPDNEAPPK VPQRTSSIAT ALNTSGAGGS RPAQAVRASN PDLRRSDPGW ERSDSVLPAS
HGHLPQAGSL ERNRNRVGAS TKLDSSPVLS PGNKAKPEDH RSRPGRPASY KRAIGEDFVL
LKERTLDEAP KPPKKAMDYS SSSEEVESSE EEEEEGDGEP SEGSRDTPGG RSDGDTDSVS
TMVVHDVEEI SGTQPSYGGG TMVVQRTPEE ERSLLLADSN GYTNLPDVVQ PSHSPTENSK
GQSPPTKDGG SDYQSRGLVK APGKSSFTMF VDLGIYQPGG SGDTIPITAL VGGEGGRLDQ
LQFDVRKGSV VNVNPTNTRA HSETPEIRKY KKRFNSEILC AALWGVNLLV GTENGLMLLD
RSGQGKVYGL IGRRRFQQMD VLEGLNLLIT ISGKRNKLRV YYLSWLRNKI LHNDPEVEKK
QGWTTVGDME GCGHYRVVKY ERIKFLVIAL KNSVEVYAWA PKPYHKFMAF KSFADLPHRP
LLVDLTVEEG QRLKVIYGSS AGFHAVDVDS GNSYDIYIPV HIQSQITPHA IIFLPNTDGM
EMLLCYEDEG VYVNTYGRII KDVVLQWGEM PTSVAYICSN QIMGWGEKAI EIRSVETGHL
DGVFMHKRAQ RLKFLCERND KVFFASVRSG GSSQVYFMTL NRNCIMNW
