SVIL_MOUSE
ID SVIL_MOUSE Reviewed; 2170 AA.
AC Q8K4L3; E9Q983;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Supervillin;
DE AltName: Full=Archvillin;
DE AltName: Full=p205/p250;
GN Name=Svil;
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 [MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=12711699; DOI=10.1242/jcs.00422;
RA Oh S.W., Pope R.K., Smith K.P., Crowley J.L., Nebl T., Lawrence J.B.,
RA Luna E.J.;
RT "Archvillin, a muscle-specific isoform of supervillin, is an early
RT expressed component of the costameric membrane skeleton.";
RL J. Cell Sci. 116:2261-2275(2003).
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]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-857 AND SER-960, 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-960, 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220; SER-227; SER-241;
RP SER-299; SER-300; SER-632; SER-761; TYR-809; THR-811; SER-857; SER-960;
RP SER-1011; SER-1031; SER-1181; SER-1184; THR-1186; SER-1190 AND SER-1361,
RP 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 [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1159, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
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).
RN [8]
RP INTERACTION WITH TASOR, AND TISSUE SPECIFICITY.
RX PubMed=31112734; DOI=10.1016/j.yexcr.2019.05.018;
RA Gresakova V., Novosadova V., Prochazkova M., Bhargava S., Jenickova I.,
RA Prochazka J., Sedlacek R.;
RT "Fam208a orchestrates interaction protein network essential for early
RT embryonic development and cell division.";
RL Exp. Cell Res. 382:111437-111437(2019).
CC -!- FUNCTION: [Isoform 1]: Forms a high-affinity link between the actin
CC cytoskeleton and the membrane. Is among the first costameric proteins
CC to assemble during myogenesis and it contributes to myogenic membrane
CC structure and differentiation. Appears to be involved in myosin II
CC assembly. May modulate myosin II regulation through MLCK during cell
CC spreading, an initial step in cell migration. May play a role in
CC invadopodial function. {ECO:0000250|UniProtKB:O95425}.
CC -!- FUNCTION: [Isoform 2]: May be involved in modulation of focal
CC adhesions. Supervillin-mediated down-regulation of focal adhesions
CC involves binding to TRIP6. Plays a role in cytokinesis through KIF14
CC interaction (By similarity). {ECO:0000250|UniProtKB:O46385}.
CC -!- SUBUNIT: Associates with F-actin (By similarity). Interacts with NEB
CC (By similarity). Interacts with MYH9 (By similarity). Interacts with
CC MYLK (By similarity). Interacts with TASOR (PubMed:31112734).
CC {ECO:0000250|UniProtKB:O46385, ECO:0000269|PubMed:31112734}.
CC -!- SUBUNIT: [Isoform 2]: Interacts with TRIP6 (By similarity). Interacts
CC with DYNLT1 (By similarity). Interacts with KIF14; at midbody during
CC cytokinesis (By similarity). {ECO:0000250|UniProtKB:O46385}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O95425};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:O95425}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:O95425}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O95425}. Cell projection, invadopodium
CC {ECO:0000250|UniProtKB:O95425}. Cell projection, podosome
CC {ECO:0000250|UniProtKB:O95425}. Midbody {ECO:0000250|UniProtKB:O46385}.
CC Cleavage furrow {ECO:0000250|UniProtKB:O46385}. Note=Tightly associated
CC with both actin filaments and plasma membranes.
CC {ECO:0000250|UniProtKB:O95425}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Archvillin {ECO:0000250|UniProtKB:O95425};
CC IsoId=Q8K4L3-1; Sequence=Displayed;
CC Name=2; Synonyms=Supervillin {ECO:0000250|UniProtKB:O95425};
CC IsoId=Q8K4L3-3; Sequence=VSP_058333, VSP_058334;
CC -!- TISSUE SPECIFICITY: Expressed in the heart, tongue and granular cells
CC within the cerebellum. {ECO:0000269|PubMed:31112734}.
CC -!- DOMAIN: As opposed to other villin-type headpiece domains, supervillin
CC HP (SVHP) doesn't bind F-actin due to the absence of a conformationally
CC flexible region (V-loop). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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DR EMBL; AF317422; AAM89518.1; -; mRNA.
DR EMBL; AC115928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124770; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS37720.1; -. [Q8K4L3-1]
DR CCDS; CCDS84352.1; -. [Q8K4L3-3]
DR RefSeq; NP_001334378.1; NM_001347449.1. [Q8K4L3-3]
DR RefSeq; NP_694793.1; NM_153153.3. [Q8K4L3-1]
DR RefSeq; XP_011245180.1; XM_011246878.2. [Q8K4L3-1]
DR AlphaFoldDB; Q8K4L3; -.
DR SMR; Q8K4L3; -.
DR BioGRID; 230358; 10.
DR IntAct; Q8K4L3; 3.
DR MINT; Q8K4L3; -.
DR STRING; 10090.ENSMUSP00000115078; -.
DR iPTMnet; Q8K4L3; -.
DR PhosphoSitePlus; Q8K4L3; -.
DR EPD; Q8K4L3; -.
DR jPOST; Q8K4L3; -.
DR MaxQB; Q8K4L3; -.
DR PaxDb; Q8K4L3; -.
DR PeptideAtlas; Q8K4L3; -.
DR PRIDE; Q8K4L3; -.
DR ProteomicsDB; 254785; -. [Q8K4L3-1]
DR ProteomicsDB; 254786; -. [Q8K4L3-3]
DR Antibodypedia; 4390; 121 antibodies from 21 providers.
DR DNASU; 225115; -.
DR Ensembl; ENSMUST00000025079; ENSMUSP00000025079; ENSMUSG00000024236. [Q8K4L3-1]
DR Ensembl; ENSMUST00000126977; ENSMUSP00000115078; ENSMUSG00000024236. [Q8K4L3-1]
DR Ensembl; ENSMUST00000140448; ENSMUSP00000119803; ENSMUSG00000024236. [Q8K4L3-1]
DR Ensembl; ENSMUST00000143254; ENSMUSP00000119287; ENSMUSG00000024236. [Q8K4L3-3]
DR GeneID; 225115; -.
DR KEGG; mmu:225115; -.
DR UCSC; uc008dyr.2; mouse. [Q8K4L3-1]
DR UCSC; uc012aza.1; mouse.
DR CTD; 6840; -.
DR MGI; MGI:2147319; Svil.
DR VEuPathDB; HostDB:ENSMUSG00000024236; -.
DR eggNOG; KOG0445; Eukaryota.
DR GeneTree; ENSGT00940000154653; -.
DR InParanoid; Q8K4L3; -.
DR OMA; KGGMVIH; -.
DR PhylomeDB; Q8K4L3; -.
DR TreeFam; TF316081; -.
DR BioGRID-ORCS; 225115; 2 hits in 68 CRISPR screens.
DR ChiTaRS; Svil; mouse.
DR PRO; PR:Q8K4L3; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8K4L3; protein.
DR Bgee; ENSMUSG00000024236; Expressed in soleus muscle and 278 other tissues.
DR ExpressionAtlas; Q8K4L3; baseline and differential.
DR Genevisible; Q8K4L3; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR GO; GO:0043034; C:costamere; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0036449; C:microtubule minus-end; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0051014; P:actin filament severing; IBA:GO_Central.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IBA:GO_Central.
DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0007519; P:skeletal muscle tissue development; ISO:MGI.
DR Gene3D; 1.10.950.10; -; 1.
DR Gene3D; 3.40.20.10; -; 5.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR015628; SV/p205.
DR InterPro; IPR007122; Villin/Gelsolin.
DR InterPro; IPR003128; Villin_headpiece.
DR InterPro; IPR036886; Villin_headpiece_dom_sf.
DR PANTHER; PTHR11977; PTHR11977; 1.
DR PANTHER; PTHR11977:SF86; PTHR11977:SF86; 1.
DR Pfam; PF00626; Gelsolin; 1.
DR Pfam; PF02209; VHP; 1.
DR PRINTS; PR00597; GELSOLIN.
DR SMART; SM00262; GEL; 5.
DR SMART; SM00153; VHP; 1.
DR SUPFAM; SSF47050; SSF47050; 1.
DR PROSITE; PS51089; HP; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Calcium; Cell junction; Cell membrane;
KW Cell projection; Cytoplasm; Cytoskeleton; Membrane; Methylation;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..2170
FT /note="Supervillin"
FT /id="PRO_0000218741"
FT REPEAT 1397..1496
FT /note="Gelsolin-like 1"
FT REPEAT 1516..1638
FT /note="Gelsolin-like 2"
FT REPEAT 1708..1818
FT /note="Gelsolin-like 3"
FT REPEAT 1837..1938
FT /note="Gelsolin-like 4"
FT REPEAT 1971..2078
FT /note="Gelsolin-like 5"
FT DOMAIN 2107..2170
FT /note="HP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00595"
FT REGION 1..167
FT /note="Interaction with MYLK"
FT /evidence="ECO:0000250"
FT REGION 37..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1375..1643
FT /note="Interaction with NEB"
FT /evidence="ECO:0000250"
FT COMPBIAS 51..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95425"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95425"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95425"
FT MOD_RES 761
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 809
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 811
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 857
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 877
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95425"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95425"
FT MOD_RES 960
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 1011
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1031
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1077
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95425"
FT MOD_RES 1159
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1186
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95425"
FT MOD_RES 1361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 257..628
FT /note="Missing (in isoform 2)"
FT /id="VSP_058333"
FT VAR_SEQ 709..740
FT /note="Missing (in isoform 2)"
FT /id="VSP_058334"
SQ SEQUENCE 2170 AA; 243162 MW; AEAB710184FB71C6 CRC64;
MKRKERIARR LEGIENDSQP ILLQSCTGLV THRLLEEDTP RYMRATDPAS PHIGRSKEEE
DTPGSSLEKQ TPSKYCIETS GIHSSGSMDT HSLESKAERI ARYKAERRRQ LAEKYGLTLD
PEADSEYLSR YAKSRKDPDV TERRGKSDKQ EEQSKDANSR HSRTESGPRT SLVASQDCTP
LGSNMSDQEQ LLNVENQRRV QDPPLGEDGS SAFFSERSIS FPEVPRSPKQ IPSSPLQQPA
SPNHPGDSPL PTEARASTGK PTHEWFLQRD SEGDTPSLIN WPSRVKVREK LVKEESARSS
PELTSESLTQ RRQQPAPAHF LPIQSESSTF DRVTSKAVSS LQPSQSGVLP TDPVHAIKLV
TMDTPESTSE FSWVGSATPK VIKSTTLKIL EGGSRDAPVL HICESKAEDW LSPEPLERSP
KSLLTSEDDR LVRGHKDPSG NKDLDKAIIC SIDVESERER QVQHLPTQRT GRSEMLLYVQ
SGPVSQDATL TSHTKEASPK KRKVLARSLS DYTGPPQLQV PRHKDEAPSQ ELELQSSRAE
GPGAEASVLD TRVSVAQLRN IFMESTRASK KPELQSRVER SAEGIGLPME RERGSRKPRR
YLSPGESRKT SERFRTQPIT SAERKESDRY PSGSEIPVVE DEEKVDERAK LSVAAKRLLF
REMEKSFDEH TVPKRHSRNA AVEQRLRRLQ DRSHTQPITT EEVVIAATEP IPASCSGVTH
PVTARLPSPT VARSSVQPAR LQASAHQKAL ARDQANEGRE SAEPGEPDSS TLSLAEKLAL
FNKLSQPVSK AISTRNRIDV RQRRMNARYQ TQPVTLGEVE QVQSGKLISF SPTVNTSVSI
MASAVAPTYA GDLRKLSVDN NTSATDYKSP PAENSDSPVR SILKPQAWRP LVEHSGSKGM
PGESGKTESK NALTVAAEDS GVQTRGAFEE EEEPSYPILG RVREGDGQKE PKHVVLRRGS
LELGNPSAAH LGDELKEVST AKSSLQENLD LKDKQASEEN TDVETVMRKF SLKEFGETTS
EQTEVAARKA SVQMATPGAW KQQESSEQLA EKLFKNPCAM FASGEVKVPV GDSFLDSPSK
TMSIKERLAL LKKSGEEDWK NRLIRKQEYG KATGGLHTQE VEQSLKKKRV TESRESQMTI
EERKHLITVR EEAWKTKGRG AANDSTQFTV AGRMVKKGLA SPTSITPISS PLCSKSRGTT
PVSKPLEDIE ARPDMQLESD LKLDRLETFL RRLNNKVAGI QETVLTVTGK SVKEVMKLDD
DETFAKFYRS VDHSIPRSPV ELEEDFDVIF DPYAPKLTSS VAEHKRQVRP KRRVQASKNP
LKLLAARDDL LQEYTEQRLN VAFMESKRMK VEKMSSNSNF SEVTLAGLAS RENFSNINLR
SVNLMEQNSN NSAMPYKKLM LLQIKGRRHV QTRLVEPRAS SLNSGDCFLL LSPQYCFLWV
GEFSNVIEKA KASELATLIQ TKRELGCRAT YIQTIEEGIN THTHAAKDFW KLLGGQTSYQ
SAGDPKEDEL YETAIIETNC VYRLTDDKLV PDDDYWGKIP KCSLLQSKEV LVFDFGSEVY
VWHGKEVTLA QRKIAFQLAK HLWNGTFDYE NCDINPLDPG ECNPLIPRKG QGRPDWAIFG
RVTEHNETIL FKEKFLDWTE LKRPTEKNSG EVVQQKDDPR ADVKPYDVTR MVATPQITAG
TILDGVNVGR GYGLVEGDDR RQFEIATVSV DVWHILEFDY SRLPRQSIGQ FHEGDAYVVK
WKYMASTAVG SRQKGEHLVR VAGKEKCVYF FWQGRHSTVS EKGTSALMTV ELDEERGAQV
QVLQGKEPPC FLQCFQGGMV VHSGRREEEE ENVQSEWRLY CVRGEVPMEG NLLEVACHCS
SLRSRTSMVV LNINKALIYL WHGCKAQGHT KEVGRTAANK IKEECPLEAG LHSSSNVTIH
ECDEGSEPLG FWDALGRRDR KAYDCMLQDP GSFNFAPRLF ILSSSSGDFS ATEFVYPAQA
PSAVSSMPFL QEDLYSAPQP ALFLVDNHHE VYLWQGWWPT ENKITGSARI RWASDRKSAM
ETVLQYCRGK NLKRPPPKSY LIHAGLEPLT FTNMFPSWEH REDIAEITEM DTEVSNQITL
VEDVLAKLCK TIYPLADLLA RPLPEGVDPL KLEIYLTDED FEFALDMSRD EFNALPTWKQ
VNLKKSKGLF
