FLNB_MOUSE
ID FLNB_MOUSE Reviewed; 2602 AA.
AC Q80X90; E9QNV9; Q8VHX4; Q8VHX7; Q99KY3;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Filamin-B;
DE Short=FLN-B;
DE AltName: Full=ABP-280-like protein;
DE AltName: Full=Actin-binding-like protein;
DE AltName: Full=Beta-filamin;
GN Name=Flnb;
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]
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1663-1752 AND 2031-2181.
RC STRAIN=C3H/HeJ;
RX PubMed=11807098; DOI=10.1083/jcb.200103037;
RA van Der Flier A., Kuikman I., Kramer D., Geerts D., Kreft M., Takafuta T.,
RA Shapiro S.S., Sonnenberg A.;
RT "Different splice variants of filamin-B affect myogenesis, subcellular
RT distribution, and determine binding to integrin (beta) subunits.";
RL J. Cell Biol. 156:361-376(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1884-2602.
RC STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary 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 [4]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=12393796; DOI=10.1093/hmg/11.23.2845;
RA Sheen V.L., Feng Y., Graham D., Takafuta T., Shapiro S.S., Walsh C.A.;
RT "Filamin A and filamin B are co-expressed within neurons during periods of
RT neuronal migration and can physically interact.";
RL Hum. Mol. Genet. 11:2845-2854(2002).
RN [5]
RP IDENTIFICATION BY 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 [6]
RP 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 [7]
RP INTERACTION WITH RFLNA AND RFLNB.
RX PubMed=21709252; DOI=10.1073/pnas.1104211108;
RA Gay O., Gilquin B., Nakamura F., Jenkins Z.A., McCartney R., Krakow D.,
RA Deshiere A., Assard N., Hartwig J.H., Robertson S.P., Baudier J.;
RT "RefilinB (FAM101B) targets filamin A to organize perinuclear actin
RT networks and regulates nuclear shape.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:11464-11469(2011).
RN [8]
RP INTERACTION WITH MICALL2.
RX PubMed=23890175; DOI=10.1111/gtc.12078;
RA Sakane A., Alamir Mahmoud Abdallah A., Nakano K., Honda K., Kitamura T.,
RA Imoto I., Matsushita N., Sasaki T.;
RT "Junctional Rab13-binding protein (JRAB) regulates cell spreading via
RT filamins.";
RL Genes Cells 18:810-822(2013).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1780, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-2518 AND LYS-2524, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [10]
RP INTERACTION WITH RFLNA AND RFLNB.
RX PubMed=24436304; DOI=10.1093/hmg/ddu007;
RA Mizuhashi K., Kanamoto T., Moriishi T., Muranishi Y., Miyazaki T.,
RA Terada K., Omori Y., Ito M., Komori T., Furukawa T.;
RT "Filamin-interacting proteins, Cfm1 and Cfm2, are essential for the
RT formation of cartilaginous skeletal elements.";
RL Hum. Mol. Genet. 23:2953-2967(2014).
RN [11]
RP INTERACTION WITH ASB2, SUBCELLULAR LOCATION, AND PROTEASOMAL DEGRADATION.
RX PubMed=26343497; DOI=10.1016/j.yjmcc.2015.08.020;
RA Thottakara T., Friedrich F.W., Reischmann S., Braumann S., Schlossarek S.,
RA Kraemer E., Juhr D., Schlueter H., van der Velden J., Muench J., Patten M.,
RA Eschenhagen T., Moog-Lutz C., Carrier L.;
RT "The E3 ubiquitin ligase Asb2beta is downregulated in a mouse model of
RT hypertrophic cardiomyopathy and targets desmin for proteasomal
RT degradation.";
RL J. Mol. Cell. Cardiol. 87:214-224(2015).
CC -!- FUNCTION: Connects cell membrane constituents to the actin
CC cytoskeleton. May promote orthogonal branching of actin filaments and
CC links actin filaments to membrane glycoproteins. Anchors various
CC transmembrane proteins to the actin cytoskeleton (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with FLNA, FLNC, INPPL1, ITGB1A, ITGB1D,
CC ITGB3, ITGB6, MYOT, MYOZ1, PSEN1 and PSEN2 (By similarity). Interacts
CC with MICALL2. Interacts with RFLNA and RFLNB
CC (PubMed:21709252,PubMed:24436304). Interacts with ASB2 isoform 1; the
CC interaction targets FLNB for proteasomal degradation (PubMed:26343497).
CC {ECO:0000250, ECO:0000269|PubMed:21709252, ECO:0000269|PubMed:24436304,
CC ECO:0000269|PubMed:26343497}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex. Cytoplasm, cytoskeleton.
CC Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:O75369}.
CC Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:26343497}.
CC -!- TISSUE SPECIFICITY: Expressed in hippocampus, cortex, cerebellar
CC Purkinje cells and granule cell layers. {ECO:0000269|PubMed:12393796}.
CC -!- DEVELOPMENTAL STAGE: Expressed within the ventricular, periventricular
CC and subventricular zones at 12.5 dpc; olfactory epithelium, radial
CC glial fibers, cortical plate and lateral ventricles at 16 dpc; in a
CC lesser degree in lung, renal cortices and alimentary tract.
CC {ECO:0000269|PubMed:12393796}.
CC -!- DOMAIN: Comprised of a NH2-terminal actin-binding domain, 24 internally
CC homologous repeats and two hinge regions. Repeat 24 and the second
CC hinge domain are important for dimer formation. The first hinge region
CC prevents binding to ITGA and ITGB subunits (By similarity).
CC {ECO:0000250}.
CC -!- PTM: ISGylation prevents ability to interact with the upstream
CC activators of the JNK cascade and inhibits IFNA-induced JNK signaling.
CC {ECO:0000250}.
CC -!- PTM: Ubiquitination by a SCF-like complex containing ASB2 isoform 1
CC leads to proteasomal degradation which promotes muscle differentiation.
CC {ECO:0000269|PubMed:26343497}.
CC -!- SIMILARITY: Belongs to the filamin family. {ECO:0000305}.
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DR EMBL; AC129222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC140322; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF353669; AAL68445.1; -; mRNA.
DR EMBL; AF353672; AAL68448.1; -; mRNA.
DR EMBL; BC003959; AAH03959.1; -; mRNA.
DR EMBL; BC048835; AAH48835.1; -; mRNA.
DR CCDS; CCDS70540.1; -.
DR RefSeq; NP_001074896.1; NM_001081427.1.
DR AlphaFoldDB; Q80X90; -.
DR SMR; Q80X90; -.
DR BioGRID; 235046; 114.
DR IntAct; Q80X90; 107.
DR STRING; 10090.ENSMUSP00000052020; -.
DR iPTMnet; Q80X90; -.
DR PhosphoSitePlus; Q80X90; -.
DR SwissPalm; Q80X90; -.
DR EPD; Q80X90; -.
DR jPOST; Q80X90; -.
DR MaxQB; Q80X90; -.
DR PaxDb; Q80X90; -.
DR PeptideAtlas; Q80X90; -.
DR PRIDE; Q80X90; -.
DR ProteomicsDB; 267597; -.
DR Antibodypedia; 1496; 291 antibodies from 32 providers.
DR DNASU; 286940; -.
DR Ensembl; ENSMUST00000052678; ENSMUSP00000052020; ENSMUSG00000025278.
DR GeneID; 286940; -.
DR KEGG; mmu:286940; -.
DR UCSC; uc007sek.1; mouse.
DR CTD; 2317; -.
DR MGI; MGI:2446089; Flnb.
DR VEuPathDB; HostDB:ENSMUSG00000025278; -.
DR eggNOG; KOG0518; Eukaryota.
DR GeneTree; ENSGT00940000156286; -.
DR HOGENOM; CLU_000783_0_0_1; -.
DR InParanoid; Q80X90; -.
DR OMA; ITYGGVH; -.
DR OrthoDB; 35998at2759; -.
DR PhylomeDB; Q80X90; -.
DR TreeFam; TF313685; -.
DR Reactome; R-MMU-1169408; ISG15 antiviral mechanism.
DR BioGRID-ORCS; 286940; 4 hits in 66 CRISPR screens.
DR ChiTaRS; Flnb; mouse.
DR PRO; PR:Q80X90; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q80X90; protein.
DR Bgee; ENSMUSG00000025278; Expressed in humerus cartilage element and 276 other tissues.
DR Genevisible; Q80X90; MM.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; IDA:MGI.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
DR GO; GO:0003382; P:epithelial cell morphogenesis; IMP:MGI.
DR GO; GO:0003334; P:keratinocyte development; IMP:MGI.
DR GO; GO:0007519; P:skeletal muscle tissue development; IDA:MGI.
DR CDD; cd00014; CH; 2.
DR Gene3D; 1.10.418.10; -; 2.
DR Gene3D; 2.60.40.10; -; 24.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR044801; Filamin.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR001298; Filamin/ABP280_rpt.
DR InterPro; IPR029874; FLNB.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR38537; PTHR38537; 3.
DR PANTHER; PTHR38537:SF7; PTHR38537:SF7; 3.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF00630; Filamin; 23.
DR SMART; SM00033; CH; 2.
DR SMART; SM00557; IG_FLMN; 24.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF81296; SSF81296; 24.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50194; FILAMIN_REPEAT; 24.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Cytoplasm; Cytoskeleton; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..2602
FT /note="Filamin-B"
FT /id="PRO_0000087299"
FT DOMAIN 16..122
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 139..242
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 249..347
FT /note="Filamin 1"
FT REPEAT 349..446
FT /note="Filamin 2"
FT REPEAT 447..543
FT /note="Filamin 3"
FT REPEAT 544..636
FT /note="Filamin 4"
FT REPEAT 640..736
FT /note="Filamin 5"
FT REPEAT 737..839
FT /note="Filamin 6"
FT REPEAT 840..938
FT /note="Filamin 7"
FT REPEAT 939..1034
FT /note="Filamin 8"
FT REPEAT 1035..1127
FT /note="Filamin 9"
FT REPEAT 1128..1222
FT /note="Filamin 10"
FT REPEAT 1223..1322
FT /note="Filamin 11"
FT REPEAT 1323..1415
FT /note="Filamin 12"
FT REPEAT 1416..1511
FT /note="Filamin 13"
FT REPEAT 1512..1608
FT /note="Filamin 14"
FT REPEAT 1609..1704
FT /note="Filamin 15"
FT REPEAT 1729..1813
FT /note="Filamin 16"
FT REPEAT 1816..1908
FT /note="Filamin 17"
FT REPEAT 1919..1994
FT /note="Filamin 18"
FT REPEAT 1997..2089
FT /note="Filamin 19"
FT REPEAT 2091..2185
FT /note="Filamin 20"
FT REPEAT 2188..2280
FT /note="Filamin 21"
FT REPEAT 2282..2375
FT /note="Filamin 22"
FT REPEAT 2379..2471
FT /note="Filamin 23"
FT REPEAT 2507..2601
FT /note="Filamin 24"
FT REGION 1..239
FT /note="Actin-binding"
FT REGION 244..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1705..1728
FT /note="Hinge 1"
FT /evidence="ECO:0000250"
FT REGION 2472..2602
FT /note="Self-association site, tail"
FT /evidence="ECO:0000250"
FT REGION 2472..2506
FT /note="Hinge 2"
FT /evidence="ECO:0000250"
FT MOD_RES 216
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75369"
FT MOD_RES 519
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75369"
FT MOD_RES 681
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75369"
FT MOD_RES 730
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75369"
FT MOD_RES 886
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75369"
FT MOD_RES 932
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75369"
FT MOD_RES 983
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75369"
FT MOD_RES 1028
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75369"
FT MOD_RES 1307
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75369"
FT MOD_RES 1316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75369"
FT MOD_RES 1433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75369"
FT MOD_RES 1505
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75369"
FT MOD_RES 1602
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75369"
FT MOD_RES 1780
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 2083
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75369"
FT MOD_RES 2113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75369"
FT MOD_RES 2369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75369"
FT MOD_RES 2465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75369"
FT MOD_RES 2478
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75369"
FT MOD_RES 2481
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75369"
FT MOD_RES 2492
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75369"
FT MOD_RES 2518
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 2524
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 2576
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75369"
FT CROSSLNK 2468
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ISG15)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 2602 AA; 277825 MW; 41BA737EC52A89DB CRC64;
MPVTEKDLAE DAPWKKIQQN TFTRWCNEHL KCVNKRIGNL QTDLSDGLRL IALLEVLSQK
RMHHKYHQRP TFRQMKLENV SVALEFLDHE SIKLVSIDSK AIVDGNLKLI LGLVWTLILH
YSISMPVWED EGDDDAKKQT PKQRLLGWIQ NKIPYLPITN FNQNWQDGKA LGALVDSCAP
GLCPDWESWD PRKPVDNARE AMQQADDWLG VPQVITPEEI IHPDVDEHSV MTYLSQFPKA
KLKPGAPLKP KLNPKKARAY GRGIEPTGNM VKQPAKFTVD TISAGQGDVM VFVEDPEGNK
EEARVTPDSD KNKTYSVEYL PKVTGLHKVI VLFAGQHISK SPFEVNVDKA QGDASKVTAK
GPGLETTGNI ANKPTYFDIY TAGAGVGDIG IEVEDPQGKN SVELLVEDRG NQVYRCVYKP
VQPGPHVVKV SFAGDAIPKS PFGVQIGEAC NPNACRASGR GLQPKGVRIR ETADFKVDTK
AAGSGELGVT VKGPKGLEEL VKQKGFLDGV YSFEYYPSTP GKYSVAVTWG GHHIPKSPFE
VQVGPEAGMQ KVRAWGPGLH GGIVGRSADF VVESIGSEVG TLGFAIEGPS QAKIEYDDQN
DGSCDVKYWP KEPGEYAVHI MCDDEDIKDS PYMAFIHPAT GDYNPDLVQA YGPGLEKSGC
TINNPAEFIV DPKDAGSAPL KILAQDGEGQ PIDIQMKSRM DGTYACSYTP LKAIKHTIAV
VWGGVNIPHS PYRVNIGQGS HPQKVKVFGP GVERSGLKAN EPTHFTVDCT EAGEGDVSVG
IKCDARVLSD DEEDVDFDII HNANDTFTVK YVPPAPGRYT IKVLFASQEI PASPFRVKVD
PSHDASKVKA EGPGLSKAGV ENGKPTHFTV HTKGAGKAPL NVQFSSPLPG EAVKDLDIID
NYDYSHTVKY TPTQQGNMQV LVTYGGDPIP KSPFTVGVAA PLDLSKIKIN GLENRVEVGK
DQEFAIDTNG AGGQGKLDVT ILSPSRKVVP CLVAPVAGRE CSTAKFIPRE EGLFAVDVTY
DGHPVPGSPY TVEASLPPDP TKVKAHGPGL EGGLVGKPAE FTIDTKGAGT GGLGLTVEGP
CEAKIECSDN GDGTCSVSYL PTKPGEYFVN ILFEEVHIPG SPFKADIEMP FDPSKVVASG
PGLEHGKVGE PGILCVDCSE AGPGTLGLEA VSDSGAKAEV SIQNNKDGTY AVTYVPLTAG
MYTLTMKYGG ELVPHFPAWV KVEPAIDTSG IKAFGPGIEG KDVFREATTD FTVDSRPLTQ
VGGDHIKAQI TNPSGASTEC FVKDNADGTY QVEYTPFEKG FHVVEVTYDD VPIPNSPFKV
AVTEGCQPSR VHAQGPGLKE AFTNKSNVFT VVTRGAGIGG LGITVEGPSE SKINCRDNKD
GSCSAEYIPF APGDYDVNIT YGGVHIPGSP FRVPSKDVVD PSKVKIAGPG LSSCVRACIP
QSFTVDSSKA GLAPLEVRVL GPRGLVEPVN VVDNGDGTHT VTYTPSQEGP YIVSVKYADE
EIPRSPFKVK VLPTYDASKV TASGPGLSAY GVPASLPVEF AIDARDAGEG LLAVQITDQE
GKPQRATVHD NKDGTYAVTY IPDKTGRYMI GVTYGGDNIP LSPYRIRATQ TGDASKCLAT
GPGIAPTVKT GEEVGFVVDA KTAGKGKVTC VILTPDGTEA EADVIENEDG TYDIFYTAAK
PGTYVIYVRF GGVDIPNSPF TVMATDGEVT AMEEAPVNAC PPGFRPWVTE EAYVPVSDMN
GLGFKPFDLV IPFAVRKGEI TGTVHMPSGK KATPEIVDNK DGTVTVRYAP TEVGLHEMHI
KYRGSHIPES PLQFYVNYPN SGSVSAYGPG LVYGVANKTA TFTIVTEDAG EGGLDLAIEG
PSKAEISCID NKDGTCTVTY LPTLPGDYSI LVKYNDKHIP GSPFTAKITD DNRRCSQVKL
GSAADFLLDI SETDLSTLTA SIKAPSGRDE PCLLKRLPNN HIGISFIPRE VGEHLVSIKK
NGNHVANSPV SIMVVQSEIG DARRAKVYGQ GLSEGRTFEM SDFIVDTRDA GYGGISLAVE
GPSKVDIQTE DLEDGTCKVS YFPTVPGVYI VSTKFADEHV PGSPFTVKIS GEGRVRESIT
RTSRAPAVAT VGSICDLNLK IPEINSSDMS AHVTSPSGHV TEAEIVPMGK NSHCVRFVPQ
EMGVHTVSVK YRGQHVTGSP FQFTVGPLGE GGAHKVRAGG PGLERGEAGI PAEFSIWTRE
AGAGGLSIAV EGPSKAEITF DDHKNGSCGV SYIAQEPGNY EVSIKFNDEH IPDSPYLVPV
IAPSDDARCL TVLSLQESGL KVNQPASFAI RLNGAKGKID AKVHSPSGAV EECHVSELEP
DKYAVRFIPH ENGIHTIDVK FNGSHVVGSP FKVRVGEPGQ AGNPALVSAY GAGLETGTTG
IQSEFFINTT QAGPGTLSVT IEGPSKVKMD CQEIPEGYKV MYTPMAPGNY LIGVKYGGPN
HISRSPFKAK VTGQRLVSPG SANETSSILV ESVTRSSTET CYSAIPKSSS DASKVTSKGA
GLSKAFVGQK SSFLVDCSKA GSNMLLIGVH GPTTPCEEVS MKHVGKQQYN VTYVVKERGD
YVLAVKWGEE HIPGSPFHVT VP
