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   27-MAR-2024, entry version 161.
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,
RC   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   [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   GlyGen; Q8K4L3; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8K4L3; -.
DR   PhosphoSitePlus; Q8K4L3; -.
DR   EPD; Q8K4L3; -.
DR   jPOST; Q8K4L3; -.
DR   MaxQB; Q8K4L3; -.
DR   PaxDb; 10090-ENSMUSP00000115078; -.
DR   PeptideAtlas; Q8K4L3; -.
DR   ProteomicsDB; 254785; -. [Q8K4L3-1]
DR   ProteomicsDB; 254786; -. [Q8K4L3-3]
DR   Pumba; Q8K4L3; -.
DR   Antibodypedia; 4390; 121 antibodies from 21 providers.
DR   DNASU; 225115; -.
DR   Ensembl; ENSMUST00000025079.16; ENSMUSP00000025079.10; ENSMUSG00000024236.19. [Q8K4L3-1]
DR   Ensembl; ENSMUST00000126977.8; ENSMUSP00000115078.2; ENSMUSG00000024236.19. [Q8K4L3-1]
DR   Ensembl; ENSMUST00000140448.8; ENSMUSP00000119803.2; ENSMUSG00000024236.19. [Q8K4L3-1]
DR   Ensembl; ENSMUST00000143254.8; ENSMUSP00000119287.2; ENSMUSG00000024236.19. [Q8K4L3-3]
DR   GeneID; 225115; -.
DR   KEGG; mmu:225115; -.
DR   UCSC; uc008dyr.2; mouse. [Q8K4L3-1]
DR   UCSC; uc012aza.1; mouse.
DR   AGR; MGI:2147319; -.
DR   CTD; 6840; -.
DR   MGI; MGI:2147319; Svil.
DR   VEuPathDB; HostDB:ENSMUSG00000024236; -.
DR   eggNOG; KOG0445; Eukaryota.
DR   GeneTree; ENSGT00940000154653; -.
DR   InParanoid; Q8K4L3; -.
DR   OMA; MEQHKRA; -.
DR   PhylomeDB; Q8K4L3; -.
DR   TreeFam; TF316081; -.
DR   BioGRID-ORCS; 225115; 2 hits in 73 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 282 other cell types or tissues.
DR   ExpressionAtlas; Q8K4L3; baseline and differential.
DR   GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR   GO; GO:0071944; C:cell periphery; IDA:MGI.
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; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005925; C:focal adhesion; IDA:MGI.
DR   GO; GO:0036449; C:microtubule minus-end; ISS:UniProtKB.
DR   GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:MGI.
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:0042383; C:sarcolemma; IDA:MGI.
DR   GO; GO:0051015; F:actin filament binding; IDA: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:0042692; P:muscle cell differentiation; IDA:MGI.
DR   GO; GO:0032467; P:positive regulation of cytokinesis; ISS:UniProtKB.
DR   GO; GO:0007519; P:skeletal muscle tissue development; ISO:MGI.
DR   CDD; cd11280; gelsolin_like; 1.
DR   CDD; cd11289; gelsolin_S2_like; 1.
DR   CDD; cd11293; gelsolin_S4_like; 1.
DR   CDD; cd11288; gelsolin_S5_like; 1.
DR   Gene3D; 3.40.20.10; Severin; 5.
DR   Gene3D; 1.10.950.10; Villin headpiece domain; 1.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   InterPro; IPR007123; Gelsolin-like_dom.
DR   InterPro; IPR007122; Villin/Gelsolin.
DR   InterPro; IPR003128; Villin_headpiece.
DR   InterPro; IPR036886; Villin_headpiece_dom_sf.
DR   PANTHER; PTHR11977:SF45; SUPERVILLIN; 1.
DR   PANTHER; PTHR11977; VILLIN; 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; SSF55753; Actin depolymerizing proteins; 5.
DR   SUPFAM; SSF47050; VHP, Villin headpiece domain; 1.
DR   PROSITE; PS51089; HP; 1.
DR   Genevisible; Q8K4L3; MM.
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
//