VP7_ROTRH
ID VP7_ROTRH Reviewed; 326 AA.
AC P12476; C3RX25; E7EDR5; P11855;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2018, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Outer capsid glycoprotein VP7 {ECO:0000255|HAMAP-Rule:MF_04131};
DE Flags: Precursor;
OS Rotavirus A (strain RVA/Monkey/United States/RRV/1975/G3P5B[3]) (RV-A).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=444185;
OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate MMU-18006;
RX PubMed=2823458; DOI=10.1016/0042-6822(87)90181-4;
RA Green K.Y., Midthun K., Gorziglia M., Hoshino Y., Kapikian A.Z.,
RA Chanock R.M., Flores J.;
RT "Comparison of the amino acid sequences of the major neutralization protein
RT of four human rotavirus serotypes.";
RL Virology 161:153-159(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2457279; DOI=10.1016/0042-6822(88)90595-8;
RA Mackow E.R., Shaw R.D., Matsui S.M., Vo P.T., Benfield D.A.,
RA Greenberg H.B.;
RT "Characterization of homotypic and heterotypic VP7 neutralization sites of
RT rhesus rotavirus.";
RL Virology 165:511-517(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT.
RX PubMed=11080489; DOI=10.1006/viro.2000.0625;
RA Dormitzer P.R., Greenberg H.B., Harrison S.C.;
RT "Purified recombinant rotavirus VP7 forms soluble, calcium-dependent
RT trimers.";
RL Virology 277:420-428(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372078; DOI=10.1038/sj.emboj.7600408;
RA Kearney K., Chen D., Taraporewala Z.F., Vende P., Hoshino Y.,
RA Tortorici M.A., Barro M., Patton J.T.;
RT "Cell-line-induced mutation of the rotavirus genome alters expression of an
RT IRF3-interacting protein.";
RL EMBO J. 23:4072-4081(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18216098; DOI=10.1128/jvi.02257-07;
RA Matthijnssens J., Ciarlet M., Heiman E.M., Arijs I., Delbeke T.,
RA McDonald S.M., Palombo E.A., Iturriza-Gomara M., Maes P., Patton J.T.,
RA Rahman M., Van Ranst M.;
RT "Full genome-based classification of rotaviruses reveals a common origin
RT between human Wa-Like and porcine rotavirus strains and human DS-1-like and
RT bovine rotavirus strains.";
RL J. Virol. 82:3204-3219(2008).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rotashield RRV;
RA Zhao B.P., Ren Z.A., Li C.D.;
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rotashield RRV;
RA Buonagurio D.A., Georgiu A.F., Lerch R.A., Mason B.B., Murthy S.C.,
RA Rappaport R.S., Sidhu M.S., Udem S.A., Zamb T.J.;
RT "Sequence Analysis of the Tetravalent Rotavirus Vaccine (United States
RT Patent US 7,485,415 B2 (Feb. 3, 2009); International Publication number WO
RT 03/072716 A2 (Sept. 4, 2003)).";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=21367894; DOI=10.1128/jvi.02691-10;
RA Criglar J., Greenberg H.B., Estes M.K., Ramig R.F.;
RT "Reconciliation of rotavirus temperature-sensitive mutant collections and
RT assignment of reassortment groups D, J, and K to genome segments.";
RL J. Virol. 85:5048-5060(2011).
RN [9]
RP GLYCOSYLATION, AND SUBUNIT.
RX PubMed=8035518; DOI=10.1128/jvi.68.8.5204-5215.1994;
RA Svensson L., Dormitzer P.R., von Bonsdorff C.-H., Maunula L.,
RA Greenberg H.B.;
RT "Intracellular manipulation of disulfide bond formation in rotavirus
RT proteins during assembly.";
RL J. Virol. 68:5204-5215(1994).
RN [10]
RP SUBUNIT.
RX PubMed=10933714; DOI=10.1128/jvi.74.17.8048-8052.2000;
RA Mirazimi A., Svensson L.;
RT "ATP is required for correct folding and disulfide bond formation of
RT rotavirus VP7.";
RL J. Virol. 74:8048-8052(2000).
RN [11]
RP INTERACTION WITH INTEGRIN HETERODIMER ITGAV/ITGB3.
RX PubMed=15452204; DOI=10.1128/jvi.78.20.10839-10847.2004;
RA Zarate S., Romero P., Espinosa R., Arias C.F., Lopez S.;
RT "VP7 mediates the interaction of rotaviruses with integrin alphavbeta3
RT through a novel integrin-binding site.";
RL J. Virol. 78:10839-10847(2004).
RN [12]
RP REVIEW.
RX PubMed=15165605; DOI=10.1016/j.tim.2004.04.003;
RA Lopez S., Arias C.F.;
RT "Multistep entry of rotavirus into cells: a Versaillesque dance.";
RL Trends Microbiol. 12:271-278(2004).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=15596814; DOI=10.1128/jvi.79.1.184-192.2005;
RA Lopez T., Camacho M., Zayas M., Najera R., Sanchez R., Arias C.F.,
RA Lopez S.;
RT "Silencing the morphogenesis of rotavirus.";
RL J. Virol. 79:184-192(2005).
RN [14]
RP FUNCTION.
RX PubMed=21849465; DOI=10.1128/jvi.00234-11;
RA Aoki S.T., Trask S.D., Coulson B.S., Greenberg H.B., Dormitzer P.R.,
RA Harrison S.C.;
RT "Cross-linking of rotavirus outer capsid protein VP7 by antibodies or
RT disulfides inhibits viral entry.";
RL J. Virol. 85:10509-10517(2011).
RN [15]
RP FUNCTION.
RX PubMed=25211455; DOI=10.1371/journal.ppat.1004355;
RA Abdelhakim A.H., Salgado E.N., Fu X., Pasham M., Nicastro D.,
RA Kirchhausen T., Harrison S.C.;
RT "Structural correlates of rotavirus cell entry.";
RL PLoS Pathog. 10:E1004355-E1004355(2014).
RN [16]
RP STRUCTURE BY ELECTRON MICROSCOPY OF THE VIRAL PARTICLE (40 ANGSTROMS), AND
RP SUBCELLULAR LOCATION.
RX PubMed=2832610; DOI=10.1016/0022-2836(88)90313-0;
RA Prasad B.V., Wang G.J., Clerx J.P., Chiu W.;
RT "Three-dimensional structure of rotavirus.";
RL J. Mol. Biol. 199:269-275(1988).
RN [17]
RP STRUCTURE BY ELECTRON MICROSCOPY OF THE VIRAL PARTICLE (3.80 ANGSTROMS) OF
RP 58-312 IN COMPLEX WITH CALCIUM AND N-ACETYL-D-GLUCOSAMINE, GLYCOSYLATION AT
RP ASN-69, DISULFIDE BONDS, AND SUBCELLULAR LOCATION.
RX PubMed=19487668; DOI=10.1073/pnas.0904024106;
RA Chen J.Z., Settembre E.C., Aoki S.T., Zhang X., Bellamy A.R.,
RA Dormitzer P.R., Harrison S.C., Grigorieff N.;
RT "Molecular interactions in rotavirus assembly and uncoating seen by high-
RT resolution cryo-EM.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:10644-10648(2009).
RN [18] {ECO:0007744|PDB:3FMG}
RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 51-326 IN COMPLEX WITH CALCIUM,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=19520960; DOI=10.1126/science.1170481;
RA Aoki S.T., Settembre E.C., Trask S.D., Greenberg H.B., Harrison S.C.,
RA Dormitzer P.R.;
RT "Structure of rotavirus outer-layer protein VP7 bound with a neutralizing
RT Fab.";
RL Science 324:1444-1447(2009).
RN [19]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF 51-326, GLYCOSYLATION
RP AT ASN-69, INTERACTION WITH THE INTERMEDIATE PROTEIN VP6, INTERACTION WITH
RP THE OUTER CAPSID PROTEIN VP5*, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21157433; DOI=10.1038/emboj.2010.322;
RA Settembre E.C., Chen J.Z., Dormitzer P.R., Grigorieff N., Harrison S.C.;
RT "Atomic model of an infectious rotavirus particle.";
RL EMBO J. 30:408-416(2011).
CC -!- FUNCTION: Calcium-binding protein that interacts with rotavirus cell
CC receptors once the initial attachment by VP4 has been achieved.
CC Rotavirus attachment and entry into the host cell probably involves
CC multiple sequential contacts between the outer capsid proteins VP4 and
CC VP7, and the cell receptors. Following entry into the host cell, low
CC intracellular or intravesicular Ca(2+) concentration probably causes
CC the calcium-stabilized VP7 trimers to dissociate from the virion
CC (PubMed:25211455, PubMed:21849465). This step is probably necessary for
CC the membrane-disrupting entry step and the release of VP4, which is
CC locked onto the virion by VP7 (PubMed:25211455, PubMed:21849465,
CC PubMed:21157433). {ECO:0000255|HAMAP-Rule:MF_04131,
CC ECO:0000269|PubMed:21157433, ECO:0000269|PubMed:21849465,
CC ECO:0000269|PubMed:25211455, ECO:0000303|PubMed:15165605}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked (PubMed:11080489,
CC PubMed:19520960, PubMed:8035518, PubMed:10933714). 2 Ca(2+) ions bound
CC at each subunit interface in the trimer hold the trimer together
CC (PubMed:19520960). Interacts with the intermediate capsid protein VP6
CC (PubMed:21157433). Interacts with the outer capsid protein VP5*
CC (PubMed:21157433). Interacts with host integrin heterodimer ITGAV/ITGB3
CC (PubMed:15452204). {ECO:0000255|HAMAP-Rule:MF_04131,
CC ECO:0000269|PubMed:10933714, ECO:0000269|PubMed:11080489,
CC ECO:0000269|PubMed:15452204, ECO:0000269|PubMed:19520960,
CC ECO:0000269|PubMed:21157433, ECO:0000269|PubMed:8035518}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04131,
CC ECO:0000269|PubMed:19487668, ECO:0000269|PubMed:19520960,
CC ECO:0000269|PubMed:21157433, ECO:0000269|PubMed:2832610}. Host
CC endoplasmic reticulum lumen {ECO:0000255|HAMAP-Rule:MF_04131}. Note=The
CC outer layer contains 780 copies of VP7, grouped as 260 trimers.
CC Immature double-layered particles assembled in the cytoplasm bud across
CC the membrane of the endoplasmic reticulum, acquiring during this
CC process a transient lipid membrane that is modified with the ER
CC resident viral glycoproteins NSP4 and VP7; these enveloped particles
CC also contain VP4. As the particles move towards the interior of the ER
CC cisternae, the transient lipid membrane and the non-structural protein
CC NSP4 are lost, while the virus surface proteins VP4 and VP7 rearrange
CC to form the outermost virus protein layer, yielding mature infectious
CC triple-layered particles. {ECO:0000255|HAMAP-Rule:MF_04131,
CC ECO:0000269|PubMed:15596814, ECO:0000269|PubMed:21157433,
CC ECO:0000269|PubMed:2832610}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=P12476-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P12476-2; Sequence=VSP_038635;
CC -!- PTM: N-glycosylated. {ECO:0000255|HAMAP-Rule:MF_04131,
CC ECO:0000269|PubMed:19487668, ECO:0000269|PubMed:21157433,
CC ECO:0000269|PubMed:8035518}.
CC -!- PTM: The N-terminus is blocked possibly by pyroglutamic acid.
CC {ECO:0000255|HAMAP-Rule:MF_04131}.
CC -!- MISCELLANEOUS: Some rotavirus strains are neuraminidase-sensitive and
CC require sialic acid to attach to the cell surface. Some rotavirus
CC strains are integrin-dependent. Some rotavirus strains depend on
CC ganglioside for their entry into the host cell. Hsp70 also seems to be
CC involved in the entry of some strains. {ECO:0000255|HAMAP-
CC Rule:MF_04131, ECO:0000269|PubMed:15165605}.
CC -!- MISCELLANEOUS: In group A rotaviruses, VP7 defines the G serotype.
CC {ECO:0000255|HAMAP-Rule:MF_04131}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative initiation at Met-
CC 30 of isoform 1. {ECO:0000250|UniProtKB:P03533}.
CC -!- SIMILARITY: Belongs to the rotavirus VP7 family. {ECO:0000255|HAMAP-
CC Rule:MF_04131}.
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DR EMBL; M21650; AAA47346.1; -; Genomic_RNA.
DR EMBL; AF295303; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; EU636932; ACC94320.1; -; Genomic_RNA.
DR EMBL; HQ846851; AEK32834.1; -; Genomic_RNA.
DR EMBL; HQ665466; ADU24500.1; -; Genomic_RNA.
DR PIR; A29247; VGXRRH.
DR PDB; 3FMG; X-ray; 3.40 A; A=51-326.
DR PDB; 3GZT; EM; 3.80 A; B/F/G/H/I/J/K/L/M/N/O/P/Q=58-312.
DR PDB; 4V7Q; EM; 3.80 A; BA/BF/BG/BH/BI/BJ/BK/BL/BM/BN/BO/BP/BQ=51-326.
DR PDB; 6WXE; EM; 3.40 A; a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r=1-326.
DR PDB; 6WXF; EM; 4.30 A; a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r=1-326.
DR PDB; 6WXG; EM; 3.30 A; a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r=1-326.
DR PDBsum; 3FMG; -.
DR PDBsum; 3GZT; -.
DR PDBsum; 4V7Q; -.
DR PDBsum; 6WXE; -.
DR PDBsum; 6WXF; -.
DR PDBsum; 6WXG; -.
DR SMR; P12476; -.
DR iPTMnet; P12476; -.
DR ABCD; P12476; 1 sequenced antibody.
DR EvolutionaryTrace; P12476; -.
DR Proteomes; UP000123891; Genome.
DR Proteomes; UP000174556; Genome.
DR GO; GO:0044166; C:host cell endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0039621; C:T=13 icosahedral viral capsid; IDA:UniProtKB.
DR GO; GO:0039624; C:viral outer capsid; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IDA:UniProtKB.
DR Gene3D; 2.60.120.800; -; 1.
DR Gene3D; 3.40.50.11130; -; 1.
DR HAMAP; MF_04130; Rota_VP7; 1.
DR HAMAP; MF_04131; Rota_VP7_A; 1.
DR InterPro; IPR001963; VP7.
DR InterPro; IPR042207; VP7_1.
DR InterPro; IPR042210; VP7_2.
DR Pfam; PF00434; VP7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Calcium; Capsid protein;
KW Disulfide bond; Glycoprotein; Host endoplasmic reticulum;
KW Host-virus interaction; Metal-binding; Outer capsid protein; Signal;
KW T=13 icosahedral capsid protein; Virion.
FT SIGNAL 1..50
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131"
FT CHAIN 51..326
FT /note="Outer capsid glycoprotein VP7"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131"
FT /id="PRO_0000149620"
FT REGION 165..167
FT /note="CNP motif; interaction with ITGAV/ITGB3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131,
FT ECO:0000269|PubMed:15452204"
FT REGION 237..239
FT /note="LVD motif; interaction with ITGA4/ITGB1 heterodimer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131"
FT REGION 253..255
FT /note="GPR motif; interaction with ITGAX/ITGB2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131,
FT ECO:0000269|PubMed:19520960"
FT BINDING 177
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131,
FT ECO:0000269|PubMed:19520960"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131,
FT ECO:0000269|PubMed:19520960"
FT BINDING 214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131,
FT ECO:0000269|PubMed:19487668, ECO:0000269|PubMed:19520960"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131,
FT ECO:0000269|PubMed:19487668, ECO:0000269|PubMed:19520960"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131,
FT ECO:0000269|PubMed:19520960"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131,
FT ECO:0000269|PubMed:19520960"
FT BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131,
FT ECO:0000269|PubMed:19487668, ECO:0000269|PubMed:19520960"
FT BINDING 301
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131,
FT ECO:0000269|PubMed:19520960"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:19487668,
FT ECO:0000269|PubMed:21157433"
FT DISULFID 82..135
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131,
FT ECO:0000269|PubMed:19487668"
FT DISULFID 165..249
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131,
FT ECO:0000269|PubMed:19487668"
FT DISULFID 191..244
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131,
FT ECO:0000269|PubMed:19487668"
FT DISULFID 196..207
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131,
FT ECO:0000269|PubMed:19487668"
FT VAR_SEQ 1..29
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038635"
FT VARIANT 32
FT /note="F -> C"
FT /evidence="ECO:0000305"
FT VARIANT 171
FT /note="T -> A"
FT /evidence="ECO:0000305"
FT VARIANT 324
FT /note="Y -> N"
FT /evidence="ECO:0000305"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:3FMG"
FT HELIX 87..93
FT /evidence="ECO:0007829|PDB:3FMG"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:3FMG"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:3FMG"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:3FMG"
FT STRAND 135..143
FT /evidence="ECO:0007829|PDB:3FMG"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:3FMG"
FT HELIX 152..159
FT /evidence="ECO:0007829|PDB:3FMG"
FT STRAND 160..167
FT /evidence="ECO:0007829|PDB:3FMG"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:3FMG"
FT STRAND 182..198
FT /evidence="ECO:0007829|PDB:3FMG"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:3FMG"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:3FMG"
FT STRAND 215..227
FT /evidence="ECO:0007829|PDB:3FMG"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:3FMG"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:3FMG"
FT STRAND 244..254
FT /evidence="ECO:0007829|PDB:3FMG"
FT STRAND 258..264
FT /evidence="ECO:0007829|PDB:3FMG"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:3FMG"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:3FMG"
FT HELIX 292..301
FT /evidence="ECO:0007829|PDB:3FMG"
FT HELIX 303..308
FT /evidence="ECO:0007829|PDB:3FMG"
SQ SEQUENCE 326 AA; 37112 MW; F84A49C30945AAAF CRC64;
MYGIEYTTVL TFLISLILLN YILKSLTRMM DFIIYRFLFI VVILSPLLKA QNYGINLPIT
GSMDTAYANS TQEETFLTST LCLYYPTEAA TEINDNSWKD TLSQLFLTKG WPTGSVYFKE
YTDIASFSVD PQLYCDYNVV LMKYDATLQL DMSELADLIL NEWLCNPMDI TLYYYQQTDE
ANKWISMGSS CTIKVCPLNT QTLGIGCLTT DTATFEEVAT AEKLVITDVV DGVNHKLDVT
TATCTIRNCK KLGPRENVAV IQVGGSDVLD ITADPTTAPQ TERMMRINWK KWWQVFYTVV
DYVNQIIQAM SKRSRSLNSA AFYYRI
