ID SVIL_BOVIN Reviewed; 2194 AA.
AC O46385;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 24-JAN-2024, entry version 123.
DE RecName: Full=Supervillin {ECO:0000303|PubMed:9382871};
DE AltName: Full=Archvillin {ECO:0000250|UniProtKB:O95425};
DE AltName: Full=p205/p250 {ECO:0000303|PubMed:9382871};
GN Name=SVIL {ECO:0000303|PubMed:9382871};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND
RP INTERACTION WITH ACTIN.
RX PubMed=9382871; DOI=10.1083/jcb.139.5.1255;
RA Pestonjamasp K.N., Pope R.K., Wulfkuhle J.D., Luna E.J.;
RT "Supervillin (p205): A novel membrane-associated, F-actin-binding protein
RT in the villin/gelsolin superfamily.";
RL J. Cell Biol. 139:1255-1269(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 448-712 (ISOFORM 1).
RA Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA Holt R., Jones S.J., Marra M.A.;
RT "Bovine genome sequencing program: full-length cDNA sequencing.";
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12202484; DOI=10.1074/jbc.m205386200;
RA Nebl T., Pestonjamasp K.N., Leszyk J.D., Crowley J.L., Oh S.W., Luna E.J.;
RT "Proteomic analysis of a detergent-resistant membrane skeleton from
RT neutrophil plasma membranes.";
RL J. Biol. Chem. 277:43399-43409(2002).
RN [5]
RP INTERACTION WITH MYH9.
RX PubMed=12917436; DOI=10.1074/jbc.m305311200;
RA Chen Y., Takizawa N., Crowley J.L., Oh S.W., Gatto C.L., Kambara T.,
RA Sato O., Li X.-D., Ikebe M., Luna E.J.;
RT "F-actin and myosin II binding domains in supervillin.";
RL J. Biol. Chem. 278:46094-46106(2003).
RN [6]
RP FUNCTION (ISOFORM 2), INTERACTION WITH TRIP6 AND DYNLT1 (ISOFORM 2), AND
RP MUTAGENESIS OF 828-ARG-TYR-829.
RX PubMed=16880273; DOI=10.1083/jcb.200512051;
RA Takizawa N., Smith T.C., Nebl T., Crowley J.L., Palmieri S.J.,
RA Lifshitz L.M., Ehrhardt A.G., Hoffman L.M., Beckerle M.C., Luna E.J.;
RT "Supervillin modulation of focal adhesions involving TRIP6/ZRP-1.";
RL J. Cell Biol. 174:447-458(2006).
RN [7]
RP FUNCTION (ISOFORM 2), AND INTERACTION WITH MLCK AND MYH9.
RX PubMed=17925381; DOI=10.1242/jcs.008219;
RA Takizawa N., Ikebe R., Ikebe M., Luna E.J.;
RT "Supervillin slows cell spreading by facilitating myosin II activation at
RT the cell periphery.";
RL J. Cell Sci. 120:3792-3803(2007).
RN [8]
RP FUNCTION (ISOFORM 2), INTERACTION WITH KIF14, AND SUBCELLULAR LOCATION.
RX PubMed=20309963; DOI=10.1002/cm.20449;
RA Smith T.C., Fang Z., Luna E.J.;
RT "Novel interactors and a role for supervillin in early cytokinesis.";
RL Cytoskeleton 67:346-364(2010).
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 (By similarity). {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 (PubMed:16880273, PubMed:17925381). Plays a
CC role in cytokinesis through KIF14 interaction (PubMed:20309963).
CC {ECO:0000269|PubMed:16880273, ECO:0000269|PubMed:17925381,
CC ECO:0000269|PubMed:20309963}.
CC -!- SUBUNIT: Associates with F-actin. Interacts with NEB (By similarity).
CC Interacts with MYH9. Interacts with MYLK. Interacts with TASOR (By
CC similarity). {ECO:0000250|UniProtKB:Q8K4L3,
CC ECO:0000269|PubMed:12917436, ECO:0000269|PubMed:17925381,
CC ECO:0000269|PubMed:9382871}.
CC -!- SUBUNIT: [Isoform 2]: Interacts with TRIP6 and DYNLT1
CC (PubMed:16880273). Interacts with KIF14; at midbody during cytokinesis
CC (PubMed:20309963). {ECO:0000269|PubMed:16880273,
CC ECO:0000269|PubMed:20309963}.
CC -!- INTERACTION:
CC O46385; P51807: Dynlt1; Xeno; NbExp=4; IntAct=EBI-6995105, EBI-642797;
CC O46385; Q15058: KIF14; Xeno; NbExp=3; IntAct=EBI-6995105, EBI-1045252;
CC O46385; Q9UHB6: LIMA1; Xeno; NbExp=3; IntAct=EBI-6995105, EBI-351479;
CC O46385; P35579: MYH9; Xeno; NbExp=2; IntAct=EBI-6995105, EBI-350338;
CC O46385; Q15654: TRIP6; Xeno; NbExp=5; IntAct=EBI-6995105, EBI-742327;
CC O46385; Q7LZ83; Xeno; NbExp=2; IntAct=EBI-6995105, EBI-6995234;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Cytoplasm, cytoskeleton. Cell projection,
CC invadopodium {ECO:0000250|UniProtKB:O95425}. Cell projection, podosome
CC {ECO:0000250|UniProtKB:O95425}. Midbody {ECO:0000269|PubMed:20309963}.
CC Cleavage furrow {ECO:0000269|PubMed:20309963}. Note=Tightly associated
CC with both actin filaments and plasma membranes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Archvillin {ECO:0000250|UniProtKB:O95425}, p250
CC {ECO:0000250|UniProtKB:O95425};
CC IsoId=O46385-1; Sequence=Displayed;
CC Name=2; Synonyms=Supervillin {ECO:0000303|PubMed:9382871}, p205
CC {ECO:0000303|PubMed:9382871};
CC IsoId=O46385-2; Sequence=VSP_037598, VSP_037599;
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; AF025996; AAC48783.1; -; mRNA.
DR EMBL; AAFC03127701; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03076280; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03076281; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03076282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DV816343; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T08878; T08878.
DR RefSeq; NP_776615.1; NM_174190.2. [O46385-2]
DR AlphaFoldDB; O46385; -.
DR BMRB; O46385; -.
DR SMR; O46385; -.
DR IntAct; O46385; 50.
DR MINT; O46385; -.
DR STRING; 9913.ENSBTAP00000049248; -.
DR PaxDb; 9913-ENSBTAP00000049248; -.
DR Ensembl; ENSBTAT00000027592.6; ENSBTAP00000027592.6; ENSBTAG00000027444.5. [O46385-2]
DR GeneID; 281509; -.
DR KEGG; bta:281509; -.
DR CTD; 6840; -.
DR VEuPathDB; HostDB:ENSBTAG00000027444; -.
DR eggNOG; KOG0445; Eukaryota.
DR GeneTree; ENSGT00940000154653; -.
DR InParanoid; O46385; -.
DR OrthoDB; 2999535at2759; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000027444; Expressed in supraspinatus muscle and 107 other cell types or tissues.
DR ExpressionAtlas; O46385; baseline and differential.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
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; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0036449; C:microtubule minus-end; IDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; IDA:DisProt.
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; IMP:UniProtKB.
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 DisProt; DP02337; -.
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.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Calcium; Cell junction; Cell membrane;
KW Cell projection; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..2194
FT /note="Supervillin"
FT /id="PRO_0000378515"
FT REPEAT 1421..1520
FT /note="Gelsolin-like 1"
FT REPEAT 1540..1662
FT /note="Gelsolin-like 2"
FT REPEAT 1732..1842
FT /note="Gelsolin-like 3"
FT REPEAT 1861..1962
FT /note="Gelsolin-like 4"
FT REPEAT 1995..2102
FT /note="Gelsolin-like 5"
FT DOMAIN 2131..2194
FT /note="HP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00595"
FT REGION 1..174
FT /note="Interaction with MYLK"
FT REGION 35..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1036..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1399..1667
FT /note="Interaction with NEB"
FT /evidence="ECO:0000250"
FT COMPBIAS 53..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1075
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95425"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95425"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4L3"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4L3"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4L3"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4L3"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95425"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95425"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4L3"
FT MOD_RES 829
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4L3"
FT MOD_RES 831
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95425"
FT MOD_RES 893
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95425"
FT MOD_RES 899
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95425"
FT MOD_RES 903
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95425"
FT MOD_RES 947
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95425"
FT MOD_RES 979
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4L3"
FT MOD_RES 1031
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4L3"
FT MOD_RES 1099
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95425"
FT MOD_RES 1205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95425"
FT MOD_RES 1210
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95425"
FT MOD_RES 1214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4L3"
FT MOD_RES 1302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95425"
FT MOD_RES 1385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4L3"
FT VAR_SEQ 279..648
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9382871"
FT /id="VSP_037598"
FT VAR_SEQ 728..759
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9382871"
FT /id="VSP_037599"
FT MUTAGEN 828..829
FT /note="RY->AA: Diminishes interaction with TRIP6 and
FT DYNLT1."
FT /evidence="ECO:0000269|PubMed:16880273"
SQ SEQUENCE 2194 AA; 244892 MW; 345C450DC2D8516C CRC64;
MKRKERIARR LEGIETDTQP ILLQSCTGLV THRLLEEDTP RYMRATDPAS PHIGRSNEEE
ETSDSSLEKQ TRSKQCTETS GIHADSPYSS GIMDTQSLES KAERIARYKA ERRRQLAEKY
GLTLDPEADS ETPSRYSRSR KDPEAAEKRG VRSERSAESS RDAGSSYSRT ELSGLRTCVA
ESKDYGLHRS DGVSDTEVLL NAENQRRGQE PSATGLARDL PLAGEVSSSF SFSGRDSALG
EVPRSPKAVH SLPSPSPGQP ASPSHSTSDL PLPAEARASI GKPKHEWFLQ KDSEGDTPSL
INWPSRVKVR EKLVREESAR SSPELTSESL TQRRHQTAPG HYLAFQSENS AFDRVSGKVA
SSARQPIRGY VQPAEPVHTI TLVTSDTPES ISEGSWVGPA PQTVTKPPPS KVLEGERRDT
PVLHICESKA EDVLFSDALE KTRKTLAVLE DRGSGRSQEA PSGTEDLSQP AVGIVTAEPQ
KESESLAHPP MAQQQPTERM GRSEMVMYVQ SEAVSQGHRK EVPTRKHRVL TRSLSDYTGP
PQLQALKAKA PAPKRDAESQ TSKAELELGL LDTKVSVAQL RNAFLESARA SRKPELHSRV
EGSSEGPGVE RERGSRKPRR YFSPGENRKT SERFRTQPIT SAERKESDRS TSNSEMPAAE
DEEKVDERAR LSVAAKRLLF REMEKSFDEK SVPKRRSRNA AVEQRLRRLQ DRSHTQPVTT
EEVVIAAEPT PASCSVATHP VMTRHPSPTV AKSPVQPART LQASAHQKAL ARDQTNESKD
SAEQGEPDSS TLSLAEKLAL FNKLSQPVSK AISTRNRLDM RQRRMNARYQ TQPVTLGEVE
QVQSGKLMAF SPTINTSVST VASTVPPMYA GNLRTKPLPD DSFGATEQKF ASSLENSDSP
VRSILKSQGW QPSVEGAGSK AMLREFEETE RKGGLTGGDG GVTKYGSFEE AELSYPVLSR
VREGDNHKEA IYALPRKGSL ELAHPPIAQL GDDLKEFSTP KSTMQASPDW KERQLFEEKV
DLENVTKRKF SLKAAEFGEP TSEQTGAAAG KPAAPTATPV SWKPQDPSEQ PQEKRYQSPC
AMFAAGEIKA PAVEGSLDSP SKTMSIKERL ALLKKSGEED WRNRLNRKQE YGKASITSSL
HIQETEQSLK KKRVTESRES QMTIEERKHL ITVREDAWKT RGKGAANDST QFTVAGRMVK
RGLASPTAIT PVASPVSSKA RGTTPVSRPL EDIEARPDMQ LESDLKLDRL ETFLRRLNNK
VGGMQETVLT VTGKSVKEVM KPDDDETFAK FYRSVDSSLP RSPVELDEDF DVIFDPYAPR
LTSSVAEHKR AVRPKRRVQA SKNPLKMLAA REDLLQEYTE QRLNVAFVES KRMKVEKLSA
NSSFSEVTLA GLASKENFSN VSLRSVNLTE QNSNNSAVPY KKLMLLQVKG RRHVQTRLVE
PRAPSLNSGD CFLLLSPHHC FLWVGEFANV IEKAKASELA SLIQTKRELG CRATYIQTVE
EGINTHTHAA KDFWKLLGGQ ASYQSAGDPK EDELYETAII ETNCIYRLMD DKLVPDDDYW
GKIPKCSLLQ SKEVLVFDFG SEVYVWHGKE VTLAQRKIAF QLAKHLWNGT FDYENCDINP
LDPGECNPLI PRKGQGRPDW AIFGRLTEHN ETILFKEKFL DWTELKRPNE KNASELAQHK
DDARAEVKPY DVTRMVPVPQ TTAGTVLDGV NVGRGYGLVE GDDRRQFEIA SISVDVWHIL
EFDYSRLPKQ SIGQFHEGDA YVVKWKFIVS TAVGSRQKGE HSVRVAGKEK CVYFFWQGRQ
STVSEKGTSA LMTVELDEER GAQVQVLQGK EPPCFLQCFQ GGMVVHSGRR EEEEENTQSE
WRLYCVRGEV PVEGNLLEVA CHCSSLRSRT SMVVLNVHKA LIYLWHGCKA QAHTKEVGRT
AANKIKDQCP LEAGLHSSSK VTIHECDEGS EPLGFWDALG RRDRKAYDCM LQDPGNFNFT
PRLFILSSSS GDFSATEFMY PARDPSVVNS MPFLQEDLYS APQPALFLVD NHHEVYLWQG
WWPIENKITG SARIRWASDR KSAMETVLQY CRGKNLKKPP PKSYLIHAGL EPLTFTNMFP
SWEHREDIAE ITEMDTEVSN QITLVEDVLA KLCKTIYPLA DLLARPLPEG VDPLKLEIYL
TDEDFEFALD MTRDEYNALP AWKQVNLKKA KGLF
//
