FLNC_MOUSE
ID FLNC_MOUSE Reviewed; 2726 AA.
AC Q8VHX6; B2RY80; B9EKT2; Q6PAI6; Q9JJ38;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Filamin-C;
DE Short=FLN-C;
DE AltName: Full=ABP-280-like protein;
DE AltName: Full=ABP-L;
DE AltName: Full=Actin-binding-like protein;
DE AltName: Full=Filamin-2;
DE AltName: Full=Gamma-filamin;
GN Name=Flnc; Synonyms=Abpl, Fln2;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1687-1800 (ISOFORMS 1 AND 2), AND
RP DEVELOPMENTAL STAGE.
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2535-2726.
RC STRAIN=C3H/HeJ; TISSUE=Myotube;
RX PubMed=10679933;
RX DOI=10.1002/(sici)1097-0177(200001)217:1<99::aid-dvdy9>3.0.co;2-5;
RA Chiang W., Greaser M.L., Lyons G.E.;
RT "Filamin isogene expression during mouse myogenesis.";
RL Dev. Dyn. 217:99-108(2000).
RN [5]
RP INTERACTION WITH KY.
RX PubMed=15385448; DOI=10.1093/hmg/ddh308;
RA Beatham J., Romero R., Townsend S.K.M., Hacker T., van der Ven P.F.M.,
RA Blanco G.;
RT "Filamin C interacts with the muscular dystrophy KY protein and is
RT abnormally distributed in mouse KY deficient muscle fibres.";
RL Hum. Mol. Genet. 13:2863-2874(2004).
RN [6]
RP FUNCTION.
RX PubMed=16914736; DOI=10.1128/mcb.00243-06;
RA Dalkilic I., Schienda J., Thompson T.G., Kunkel L.M.;
RT "Loss of FilaminC (FLNc) results in severe defects in myogenesis and
RT myotube structure.";
RL Mol. Cell. Biol. 26:6522-6534(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2234, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC 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 [9]
RP INTERACTION WITH IGFN1.
RX PubMed=20206623; DOI=10.1016/j.yexcr.2010.02.027;
RA Baker J., Riley G., Romero M.R., Haynes A.R., Hilton H., Simon M.,
RA Hancock J., Tateossian H., Ripoll V.M., Blanco G.;
RT "Identification of a Z-band associated protein complex involving KY, FLNC
RT and IGFN1.";
RL Exp. Cell Res. 316:1856-1870(2010).
RN [10]
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 [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1003, AND IDENTIFICATION BY MASS
RP 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: Muscle-specific filamin, which plays a central role in
CC sarcomere assembly and organization (By similarity). Critical for
CC normal myogenesis, it probably functions as a large actin-cross-linking
CC protein with structural functions at the Z lines in muscle cells. May
CC be involved in reorganizing the actin cytoskeleton in response to
CC signaling events (PubMed:16914736). {ECO:0000250|UniProtKB:Q14315,
CC ECO:0000269|PubMed:16914736}.
CC -!- SUBUNIT: Homodimer; the filamin repeat 24 and the second hinge domain
CC are important for dimer formation (By similarity). Interacts with FLNB,
CC INPPL1, ITGB1A, KCND2, MYOT, MYOZ1 and MYOZ3. Interacts with
CC sarcoglycans SGCD and SGCG. Interacts (via filament repeats 17-18, 20-
CC 21 and 24) with USP25 (isoform USP25m only). Interacts with FBLIM1 (By
CC similarity). Interacts with XIRP1; this interaction is mediated by
CC filamin 20 repeat (By similarity). Interacts with KY. Interacts with
CC IGFN1. Interacts with MICALL2. Interacts with ANK3. Interacts with
CC MICALL2 (By similarity). Interacts with ANK3. Interacts with SYNPO2 (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q14315}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250}.
CC Note=A small amount localizes at membranes. In striated muscle cells,
CC it predominantly localizes in myofibrillar Z lines, while a minor
CC fraction localizes with subsarcolemme (By similarity). Targeting to
CC developing and mature Z lines is mediated by the intradomain insert (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=H1;
CC IsoId=Q8VHX6-1; Sequence=Displayed;
CC Name=2; Synonyms=Delta-H1;
CC IsoId=Q8VHX6-2; Sequence=VSP_007580;
CC -!- DEVELOPMENTAL STAGE: During myogenesis, isoform 1 is expressed the
CC first day, then is replaced by isoform 2.
CC {ECO:0000269|PubMed:11807098}.
CC -!- PTM: Ubiquitinated by FBXL22, leading to proteasomal degradation.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the filamin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC044807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC052186; AAH52186.1; -; mRNA.
DR EMBL; BC060276; AAH60276.1; -; mRNA.
DR EMBL; BC151097; AAI51098.1; -; mRNA.
DR EMBL; BC158128; AAI58129.1; -; mRNA.
DR EMBL; AF353670; AAL68446.1; -; mRNA.
DR EMBL; AF119148; AAF97411.1; -; mRNA.
DR CCDS; CCDS39452.1; -. [Q8VHX6-1]
DR CCDS; CCDS80503.1; -. [Q8VHX6-2]
DR RefSeq; NP_001074654.1; NM_001081185.1. [Q8VHX6-1]
DR RefSeq; NP_001298003.1; NM_001311074.1. [Q8VHX6-2]
DR SMR; Q8VHX6; -.
DR BioGRID; 213053; 16.
DR CORUM; Q8VHX6; -.
DR IntAct; Q8VHX6; 10.
DR MINT; Q8VHX6; -.
DR STRING; 10090.ENSMUSP00000064163; -.
DR iPTMnet; Q8VHX6; -.
DR PhosphoSitePlus; Q8VHX6; -.
DR EPD; Q8VHX6; -.
DR jPOST; Q8VHX6; -.
DR MaxQB; Q8VHX6; -.
DR PaxDb; Q8VHX6; -.
DR PeptideAtlas; Q8VHX6; -.
DR PRIDE; Q8VHX6; -.
DR ProteomicsDB; 267483; -. [Q8VHX6-1]
DR ProteomicsDB; 267484; -. [Q8VHX6-2]
DR Antibodypedia; 1492; 150 antibodies from 20 providers.
DR Ensembl; ENSMUST00000065090; ENSMUSP00000064163; ENSMUSG00000068699. [Q8VHX6-1]
DR Ensembl; ENSMUST00000101617; ENSMUSP00000099139; ENSMUSG00000068699. [Q8VHX6-2]
DR GeneID; 68794; -.
DR KEGG; mmu:68794; -.
DR UCSC; uc009bdn.1; mouse. [Q8VHX6-1]
DR UCSC; uc009bdo.2; mouse. [Q8VHX6-2]
DR CTD; 2318; -.
DR MGI; MGI:95557; Flnc.
DR VEuPathDB; HostDB:ENSMUSG00000068699; -.
DR eggNOG; KOG0518; Eukaryota.
DR GeneTree; ENSGT00940000153588; -.
DR InParanoid; Q8VHX6; -.
DR OMA; YPVMAGK; -.
DR OrthoDB; 657777at2759; -.
DR PhylomeDB; Q8VHX6; -.
DR Reactome; R-MMU-446353; Cell-extracellular matrix interactions.
DR BioGRID-ORCS; 68794; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Flnc; mouse.
DR PRO; PR:Q8VHX6; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8VHX6; protein.
DR Bgee; ENSMUSG00000068699; Expressed in hindlimb stylopod muscle and 161 other tissues.
DR Genevisible; Q8VHX6; MM.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR GO; GO:0016528; C:sarcoplasm; ISO:MGI.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; TAS:MGI.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0030506; F:ankyrin binding; ISO:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0030029; P:actin filament-based process; TAS:MGI.
DR GO; GO:0055001; P:muscle cell development; IDA:UniProtKB.
DR GO; GO:0045214; P:sarcomere organization; ISS:UniProtKB.
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; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR38537; PTHR38537; 2.
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 Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton; Membrane;
KW Methylation; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..2726
FT /note="Filamin-C"
FT /id="PRO_0000087302"
FT DOMAIN 37..143
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 160..263
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 271..369
FT /note="Filamin 1"
FT REPEAT 371..469
FT /note="Filamin 2"
FT REPEAT 470..566
FT /note="Filamin 3"
FT REPEAT 567..659
FT /note="Filamin 4"
FT REPEAT 663..759
FT /note="Filamin 5"
FT REPEAT 760..862
FT /note="Filamin 6"
FT REPEAT 863..961
FT /note="Filamin 7"
FT REPEAT 962..1057
FT /note="Filamin 8"
FT REPEAT 1058..1150
FT /note="Filamin 9"
FT REPEAT 1151..1245
FT /note="Filamin 10"
FT REPEAT 1246..1345
FT /note="Filamin 11"
FT REPEAT 1346..1438
FT /note="Filamin 12"
FT REPEAT 1439..1534
FT /note="Filamin 13"
FT REPEAT 1535..1631
FT /note="Filamin 14"
FT REPEAT 1636..1735
FT /note="Filamin 15"
FT REPEAT 1760..1855
FT /note="Filamin 16"
FT REPEAT 1856..1947
FT /note="Filamin 17"
FT REPEAT 1948..2034
FT /note="Filamin 18"
FT REPEAT 2037..2129
FT /note="Filamin 19"
FT REPEAT 2212..2307
FT /note="Filamin 20; mediates interaction with XIRP1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00087"
FT REPEAT 2310..2402
FT /note="Filamin 21"
FT REPEAT 2404..2497
FT /note="Filamin 22"
FT REPEAT 2501..2593
FT /note="Filamin 23"
FT REPEAT 2631..2725
FT /note="Filamin 24"
FT REGION 1..260
FT /note="Actin-binding"
FT REGION 1736..1759
FT /note="Hinge 1"
FT REGION 2163..2244
FT /note="Intradomain insert; mediate targeting to Z lines"
FT /evidence="ECO:0000250"
FT REGION 2193..2214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2241..2261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2404..2725
FT /note="Interaction with INPPL1"
FT /evidence="ECO:0000250"
FT REGION 2594..2726
FT /note="Self-association site, tail"
FT /evidence="ECO:0000250"
FT REGION 2594..2630
FT /note="Hinge 2"
FT COMPBIAS 2193..2211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14315"
FT MOD_RES 1003
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14315"
FT MOD_RES 1339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14315"
FT MOD_RES 2043
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14315"
FT MOD_RES 2234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 2237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14315"
FT MOD_RES 2239
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14315"
FT MOD_RES 2587
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14315"
FT MOD_RES 2618
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14315"
FT MOD_RES 2621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14315"
FT MOD_RES 2633
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14315"
FT MOD_RES 2715
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14315"
FT MOD_RES 2719
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14315"
FT VAR_SEQ 1735..1767
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11807098,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007580"
FT CONFLICT 1406
FT /note="C -> R (in Ref. 2; AAI51098)"
FT /evidence="ECO:0000305"
FT CONFLICT 2606
FT /note="E -> Q (in Ref. 4; AAF97411)"
FT /evidence="ECO:0000305"
FT CONFLICT 2609
FT /note="T -> S (in Ref. 4; AAF97411)"
FT /evidence="ECO:0000305"
FT CONFLICT 2617
FT /note="K -> H (in Ref. 4; AAF97411)"
FT /evidence="ECO:0000305"
FT CONFLICT 2631
FT /note="K -> N (in Ref. 4; AAF97411)"
FT /evidence="ECO:0000305"
FT CONFLICT 2663..2665
FT /note="KAG -> QAR (in Ref. 4; AAF97411)"
FT /evidence="ECO:0000305"
FT CONFLICT 2669
FT /note="M -> I (in Ref. 4; AAF97411)"
FT /evidence="ECO:0000305"
FT CONFLICT 2695
FT /note="V -> F (in Ref. 4; AAF97411)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2726 AA; 291119 MW; BFBE03CBFFEE3863 CRC64;
MMNNSNYSDA SGLGLVDEAD EMPSTEKDLA EDAPWKKIQQ NTFTRWCNEH LKCVGKRLTD
LQRDLSDGLR LIALLEVLSQ KRMYRKFHPR PNFRQMKLEN VSVALEFLER EHIKLVSIDS
KAIVDGNLKL ILGLIWTLIL HYSISMPMWE DEDDEDARKQ TPKQRLLGWI QNKVPQLPIT
NFNRDWQDGK ALGALVDNCA PGLCPDWEAW DPNQPVQNAR EAMQQADDWL GVPQVIAPEE
IVDPNVDEHS VMTYLSQFPK AKLKPGAPVR SKQLNPKKAI AYGPGIEPQG NTVLQPAHFT
VQTVDAGVGE VLVYIEDPEG HTEEAKVVPN NDKDRTYAVS YVPKVAGLHK VTVLFAGQNI
ERSPFEVNVG MALGDANKVS ARGPGLEPVG NVANKPTYFD IYTAGAGTGD VAVVIVDPQG
RRDTVEVALE DKGDNTFRCT YRPVMEGPHT VHVAFAGAPI TRSPFPVHVA EACNPNACRA
SGRGLQPKGV RVKEVADFKV FTKGAGSGEL KVTVKGPKGT EEPVKVREAG DGVFECEYYP
VVPGKYVVTI TWGGYAIPRS PFEVQVSPEA GAQKVRAWGP GLETGQVGKS ADFVVEAIGT
EVGTLGFSIE GPSQAKIECD DKGDGSCDVR YWPTEPGEYA VHVICDDEDI RDSPFIAHIQ
PAPPDCFPDK VKAFGPGLEP TGCIVDRPAE FTIDARAAGK GDLKLYAQDA DGCPIDIKVI
PNGDGTFRCS YVPTKPIKHT IIVSWGGVNV PKSPFRVNVG EGSHPERVKV YGPGVEKTGL
KANEPTYFTV DCSEAGQGDV SIGIKCAPGV VGPVEADIDF DIIKNDNDTF TVKYTPPGAG
HYTIMVLFAN QEIPASPFHI KVDPSHDASK VKAEGPGLSR TGVEVGKPTH FTVLTKGAGK
AKLDVHFAGA AKGEAVRDFE IIDNHDYSYT VKYTAVQQGN MAVTVTYGGD PVPKSPFVVN
VAPPLDLSKV KVQGLNSKVA VGQEQAFSVN TRGAGGQGQL DVRMTSPSRR PIPCKLEPGG
GAEAQAVRYM PPEEGPYKVD ITYDGHPVPG SPFAVEGVLP PDPSKVCAYG PGLKGGLVGT
PAPFSIDTKG AGTGGLGLTV EGPCEAKIEC QDNGDGSCAV SYLPTEPGEY TINILFAEAH
IPGSPFKATI QPVFDPSKVR ASGPGLERGK AGEAATFTVD CSEAGEAELT IEILSDAGVK
AEVLIQNNAD GTYHITYSPA FPGTYTITIK YGGHPIPKFP TRVHVQPAVD TSGIKVSGPG
VEPHGVLREV TTEFTVDARS LTATGGNHVT ARVLNPSGAK TDTYVTDNGD GTYRVQYTAY
EEGVHLVEVL YDEVAVPKSP FRVGVTEGCD PTRVRAFGPG LEGGLVNKAN RFTVETRGAG
TGGLGLAIEG PSEAKMSCKD NKDGSCTVEY IPFTPGDYDV NITFGGQPIP GSPFRVPVKD
VVDPGKVKCS GPGLGTGVRA RVPQTFTVDC SQAGRAPLQV AVLGPTGVAE PVEVRDNGDG
THTVHYTPAT DGPYTVAVKY ADQEVPRSPF KIKVLPSHDA SKVRASGPGL NASGIPASLP
VEFTIDARDA GQGLLTVQIL DPEGKPKKAN IRDNGDGTYT VSYLPDMSGR YTITIKYGGD
EIPYSPFRIH ALPTGDASKC LVTVSIGGHG LGACLGPRIQ IGEETVITVD AKAAGKGKVT
CTVSTPDGAE LDVDVVENHD GTFDIYYTAP EPGKYVITIR FGGEHIPNSP FHVLACDPLP
HVEEPAEMLQ MRQPYAPLRP GTCPTHWATE EPVVPVEPLE SMLRPFNLVI PFTVQKGELT
GEVRMPSGKT ARPNITDNKD GTITVRYAPT EKGLHQMGIK YDGNHIPGSP LQFYVDAINS
RHVSAYGPGL SHGMVNKPAT FTIVTKDAGE GGLSLAVEGP SKAEITCKDN KDGTCTVSYL
PTAPGDYSII VRFDDKHIPG SPFTAKITGD DSMRTSQLNV GTSTDVSLKI TEGDLSQLTA
SIRAPSGNEE PCLLKRLPNR HIGISFTPKE VGEHVVSVRK SGKHVTNSPF KILVGPSEIG
DASKVRVWGK GLSEGQTFQV AEFIVDTRNA GYGGLGLSIE GPSKVDINCE DMEDGTCKVT
YCPTEPGTYI INIKFADKHV PGSPFTVKVT GEGRMKESIT RRRQAPSIAT IGSTCDLNLK
IPGNWFQMVS AQERLTRTFT RSSHTYTRTE RTEISKTRGG ETKREVRVEE STQVGGDPFP
AVFGDFLGRE RLGSFGSITR QQEGEASSQD MTAQVTSPSG KTEAAEIVEG EDSAYSVRFV
PQEMGPHTVT VKYRGQHVPG SPFQFTVGPL GEGGAHKVRA GGTGLERGVA GVPAEFSIWT
REAGAGGLSI AVEGPSKAEI AFEDRKDGSC GVSYVVQEPG DYEVSIKFND EHIPDSPFVV
PVASLSDDAR RLTVTSLQET GLKVNQPASF AVQLNGARGV IDARVHTPSG AVEECYVSEL
DSDKHTIRFI PHENGVHSID VKFNGAHIPG SPFKIRVGEQ SQAGDPGLVS AYGPGLEGGT
TGVSSEFIVN TQNAGSGALS VTIDGPSKVQ LDCRECPEGH VVTYTPMAPG NYLIAIKYGG
PQHIVGSPFK AKVTGPRLSG GHSLHETSTV LVETVTKSSS SRGASYSSIP KFSSDASKVV
TRGPGLSQAF VGQKNSFTVD CSKAGTNMMM VGVHGPKTPC EEVYVKHMGN RVYNVTYTVK
EKGDYILIVK WGDESVPGSP FKVNVP
