SPIKE_CVMA5
ID SPIKE_CVMA5 Reviewed; 1324 AA.
AC P11224; O39227;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Spike glycoprotein {ECO:0000255|HAMAP-Rule:MF_04099};
DE Short=S glycoprotein {ECO:0000255|HAMAP-Rule:MF_04099};
DE AltName: Full=E2 {ECO:0000255|HAMAP-Rule:MF_04099};
DE AltName: Full=Peplomer protein {ECO:0000255|HAMAP-Rule:MF_04099};
DE Contains:
DE RecName: Full=Spike protein S1 {ECO:0000255|HAMAP-Rule:MF_04099};
DE Contains:
DE RecName: Full=Spike protein S2 {ECO:0000255|HAMAP-Rule:MF_04099};
DE Contains:
DE RecName: Full=Spike protein S2' {ECO:0000255|HAMAP-Rule:MF_04099};
DE Flags: Precursor;
GN Name=S {ECO:0000255|HAMAP-Rule:MF_04099}; ORFNames=3;
OS Murine coronavirus (strain A59) (MHV-A59) (Murine hepatitis virus).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus.
OX NCBI_TaxID=11142;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2825419; DOI=10.1016/0042-6822(87)90142-5;
RA Luytjes W., Sturman L.S., Bredenbeek P.J., Charite J.,
RA van der Zeijst B.A.M., Horzinek M.C., Spaan W.J.M.;
RT "Primary structure of the glycoprotein E2 of coronavirus MHV-A59 and
RT identification of the trypsin cleavage site.";
RL Virology 161:479-487(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate C12 mutant;
RX PubMed=9426441; DOI=10.1006/viro.1997.8877;
RA Leparc-Goffart I., Hingley S.T., Chua M.M., Jiang X., Lavi E., Weiss S.R.;
RT "Altered pathogenesis of a mutant of the murine coronavirus MHV-A59 is
RT associated with a Q159L amino acid substitution in the spike protein.";
RL Virology 239:1-10(1997).
RN [3]
RP INTERACTION WITH M PROTEIN.
RX PubMed=10627571; DOI=10.1128/jvi.74.3.1566-1571.2000;
RA Godeke G.J., de Haan C.A., Rossen J.W., Vennema H., Rottier P.J.;
RT "Assembly of spikes into coronavirus particles is mediated by the carboxy-
RT terminal domain of the spike protein.";
RL J. Virol. 74:1566-1571(2000).
RN [4]
RP INTERACTION WITH MURINE CEACAM1.
RX PubMed=1719235; DOI=10.1128/jvi.65.12.6881-6891.1991;
RA Dveksler G.S., Pensiero M.N., Cardellichio C.B., Williams R.K.,
RA Jiang G.-S., Holmes K.V., Dieffenbach C.W.;
RT "Cloning of the mouse hepatitis virus (MHV) receptor: expression in human
RT and hamster cell lines confers susceptibility to MHV.";
RL J. Virol. 65:6881-6891(1991).
RN [5]
RP INTERACTION WITH MURINE CEACAM1.
RX PubMed=8380065; DOI=10.1128/jvi.67.1.1-8.1993;
RA Dveksler G.S., Dieffenback C.B., Cardellichio C.B., McCuaig K.,
RA Pensiero M.N., Jiang G.-S., Beauchemin N., Holmes K.V.;
RT "Several members of the mouse carcinoembryonic antigen-related glycoprotein
RT family are functional receptors for the coronavirus mouse hepatitis virus-
RT A59.";
RL J. Virol. 67:1-8(1993).
RN [6]
RP INTERACTION WITH MURINE CEACAM2.
RX PubMed=8207827; DOI=10.1128/jvi.68.7.4525-4537.1994;
RA Nedellec P., Dveksler G.S., Daniels E., Turbide C., Chow B., Basile A.A.,
RA Holmes K.V., Beauchemin N.;
RT "Bgp2, a new member of the carcinoembryonic antigen-related gene family,
RT encodes an alternative receptor for mouse hepatitis viruses.";
RL J. Virol. 68:4525-4537(1994).
RN [7]
RP CLEAVAGE BY HOST FURIN OR FURIN-LIKE ENZYME.
RX PubMed=15141003; DOI=10.1128/jvi.78.11.6048-6054.2004;
RA de Haan C.A.M., Stadler K., Godeke G.-J., Bosch B.J., Rottier P.J.;
RT "Cleavage inhibition of the murine coronavirus spike protein by a furin-
RT like enzyme affects cell-cell but not virus-cell fusion.";
RL J. Virol. 78:6048-6054(2004).
RN [8]
RP MUTAGENESIS OF SER-33; THR-62; LEU-65; 79-LEU--THR-82; TYR-162 AND LYS-183.
RX PubMed=15749126; DOI=10.1016/j.virol.2005.01.016;
RA Thackray L.B., Turner B.C., Holmes K.V.;
RT "Substitutions of conserved amino acids in the receptor-binding domain of
RT the spike glycoprotein affect utilization of murine CEACAM1a by the murine
RT coronavirus MHV-A59.";
RL Virology 334:98-110(2005).
RN [9]
RP FUNCTION.
RX PubMed=16014947; DOI=10.1128/jvi.79.15.9862-9871.2005;
RA Choi K.S., Aizaki H., Lai M.M.;
RT "Murine coronavirus requires lipid rafts for virus entry and cell-cell
RT fusion but not for virus release.";
RL J. Virol. 79:9862-9871(2005).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 969-1024.
RX PubMed=15123674; DOI=10.1074/jbc.m403760200;
RA Xu Y., Liu Y., Lou Z., Qin L., Li X., Bai Z., Pang H., Tien P., Gao G.F.,
RA Rao Z.;
RT "Structural basis for coronavirus-mediated membrane fusion. Crystal
RT structure of mouse hepatitis virus spike protein fusion core.";
RL J. Biol. Chem. 279:30514-30522(2004).
CC -!- FUNCTION: [Spike protein S1]: Attaches the virion to the cell membrane
CC by interacting with host receptor, initiating the infection. Interacts
CC with murine CEACAM1 to mediate viral entry. {ECO:0000255|HAMAP-
CC Rule:MF_04099, ECO:0000269|PubMed:16014947}.
CC -!- FUNCTION: [Spike protein S2]: Mediates fusion of the virion and
CC cellular membranes by acting as a class I viral fusion protein. Under
CC the current model, the protein has at least three conformational
CC states: pre-fusion native state, pre-hairpin intermediate state, and
CC post-fusion hairpin state. During viral and target cell membrane
CC fusion, the coiled coil regions (heptad repeats) assume a trimer-of-
CC hairpins structure, positioning the fusion peptide in close proximity
CC to the C-terminal region of the ectodomain. The formation of this
CC structure appears to drive apposition and subsequent fusion of viral
CC and target cell membranes. {ECO:0000255|HAMAP-Rule:MF_04099,
CC ECO:0000269|PubMed:16014947}.
CC -!- FUNCTION: [Spike protein S2']: Acts as a viral fusion peptide which is
CC unmasked following S2 cleavage occurring upon virus endocytosis.
CC {ECO:0000255|HAMAP-Rule:MF_04099}.
CC -!- SUBUNIT: Homotrimer; each monomer consists of a S1 and a S2 subunit.
CC The resulting peplomers protrude from the virus surface as spikes (By
CC similarity). Cytoplasmic tail interacts with M protein. S1 interacts
CC with murine CEACAM1, and weakly with murine CEACAM2 in tissue culture.
CC {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:10627571,
CC ECO:0000269|PubMed:1719235, ECO:0000269|PubMed:8207827,
CC ECO:0000269|PubMed:8380065}.
CC -!- INTERACTION:
CC P11224; P11224: S; NbExp=3; IntAct=EBI-16196052, EBI-16196052;
CC P11224; Q3LFS9: Ceacam1; Xeno; NbExp=2; IntAct=EBI-16196052, EBI-25747689;
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04099}. Host endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass
CC type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Host cell
CC membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_04099}. Note=Accumulates in the
CC endoplasmic reticulum-Golgi intermediate compartment, where it
CC participates in virus particle assembly. Some S oligomers are
CC transported to the host plasma membrane, where they may mediate cell-
CC cell fusion. {ECO:0000255|HAMAP-Rule:MF_04099}.
CC -!- DOMAIN: Fusion peptide 1 (FP1) and fusion peptide 2 (FP2) function
CC cooperatively and have a membrane-ordering effect on lipid headgroups
CC and shallow hydrophobic regions of target bilayers. They are considered
CC as two domains of an extended, bipartite FP. The membrane-ordering
CC activity is calcium-dependent and also dependent on correct folding,
CC which is maintained by an internal disulfide bond in FP2.
CC {ECO:0000255|HAMAP-Rule:MF_04099}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. The
CC precursor is processed into S1 and S2 by host cell furin or another
CC cellular protease to yield the mature S1 and S2 proteins. Additionally,
CC a second cleavage leads to the release of a fusion peptide after viral
CC attachment to host cell receptor. {ECO:0000255|HAMAP-Rule:MF_04099}.
CC -!- PTM: The cytoplasmic Cys-rich domain is palmitoylated. Spike
CC glycoprotein is digested within host endosomes. {ECO:0000255|HAMAP-
CC Rule:MF_04099}.
CC -!- SIMILARITY: Belongs to the betacoronaviruses spike protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04099}.
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DR EMBL; M18379; AAA46455.1; -; Genomic_RNA.
DR EMBL; AF029248; AAB86819.1; -; Genomic_RNA.
DR PIR; A27402; VGIH59.
DR RefSeq; NP_045300.1; NC_001846.1.
DR PDB; 1WDF; X-ray; 2.50 A; A/B=969-1024, A/B=1216-1254.
DR PDB; 1WDG; X-ray; 2.06 A; A/B=969-1017, A/B=1224-1254.
DR PDB; 3JCL; EM; 4.00 A; A/B/C=15-1231.
DR PDB; 6B3O; EM; 4.10 A; A/B/C=714-1252.
DR PDB; 6VSJ; EM; 3.94 A; A/B/C=15-1228.
DR PDBsum; 1WDF; -.
DR PDBsum; 1WDG; -.
DR PDBsum; 3JCL; -.
DR PDBsum; 6B3O; -.
DR PDBsum; 6VSJ; -.
DR SMR; P11224; -.
DR DIP; DIP-61967N; -.
DR IntAct; P11224; 2.
DR SwissPalm; P11224; -.
DR ABCD; P11224; 1 sequenced antibody.
DR GeneID; 1489752; -.
DR KEGG; vg:1489752; -.
DR EvolutionaryTrace; P11224; -.
DR Proteomes; UP000007192; Genome.
DR GO; GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044177; C:host cell Golgi apparatus; IDA:CACAO.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-UniRule.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IEA:UniProtKB-UniRule.
DR CDD; cd21625; MHV-like_Spike_S1_NTD; 1.
DR Gene3D; 2.60.120.960; -; 1.
DR HAMAP; MF_04099; BETA_CORONA_SPIKE; 1.
DR InterPro; IPR032500; bCoV_S1_N.
DR InterPro; IPR042578; BETA_CORONA_SPIKE.
DR InterPro; IPR043607; CoV_S1_C.
DR InterPro; IPR043473; S2_sf_CoV.
DR InterPro; IPR043002; Spike_N_sf.
DR InterPro; IPR044339; Spike_S1_NTD_MHV-like.
DR InterPro; IPR018548; Spike_S1_RBD_bCoV.
DR InterPro; IPR036326; Spike_S1_RBD_sf_bCoV.
DR InterPro; IPR002552; Spike_S2_CoV.
DR InterPro; IPR043614; Spike_S2_CoV_C.
DR InterPro; IPR044873; Spike_S2_CoV_HR1.
DR InterPro; IPR044874; Spike_S2_CoV_HR2.
DR Pfam; PF16451; bCoV_S1_N; 1.
DR Pfam; PF09408; bCoV_S1_RBD; 1.
DR Pfam; PF19209; CoV_S1_C; 1.
DR Pfam; PF01601; CoV_S2; 1.
DR Pfam; PF19214; CoV_S2_C; 1.
DR SUPFAM; SSF111474; SSF111474; 2.
DR SUPFAM; SSF143587; SSF143587; 1.
DR PROSITE; PS51921; BCOV_S1_CTD; 1.
DR PROSITE; PS51922; BCOV_S1_NTD; 1.
DR PROSITE; PS51923; COV_S2_HR1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Disulfide bond;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host cell membrane; Host membrane; Host-virus interaction; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virulence;
KW Virus entry into host cell.
FT SIGNAL 1..13
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CHAIN 15..1324
FT /note="Spike glycoprotein"
FT /id="PRO_0000037214"
FT CHAIN 15..717
FT /note="Spike protein S1"
FT /id="PRO_0000037215"
FT CHAIN 718..1324
FT /note="Spike protein S2"
FT /id="PRO_0000037216"
FT CHAIN 870..1324
FT /note="Spike protein S2'"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT /id="PRO_0000444084"
FT TOPO_DOM 14..1265
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT TRANSMEM 1266..1286
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT TOPO_DOM 1287..1324
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT DOMAIN 15..296
FT /note="BetaCoV S1-NTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DOMAIN 327..566
FT /note="BetaCoV S1-CTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT REGION 17..330
FT /note="Receptor binding site"
FT REGION 870..891
FT /note="Fusion peptide 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 889..909
FT /note="Fusion peptide 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 970..1020
FT /note="Heptad repeat 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 1214..1254
FT /note="Heptad repeat 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT COILED 999..1043
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT COILED 1227..1255
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT MOTIF 1320..1324
FT /note="KxHxx"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT SITE 717..718
FT /note="Cleavage; by host"
FT SITE 869..870
FT /note="Cleavage"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 625
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 657
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 665
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 688
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 737
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 754
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 893
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1180
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1190
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1209
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1225
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1246
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT DISULFID 21..158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DISULFID 153..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DISULFID 165..246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DISULFID 284..294
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DISULFID 329..354
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT DISULFID 372..425
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT DISULFID 384..564
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT DISULFID 894..905
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT VARIANT 82
FT /note="R -> T (in strain: Isolate C12 mutant)"
FT VARIANT 98
FT /note="N -> S (in strain: Isolate C12 mutant)"
FT VARIANT 159
FT /note="Q -> L (in strain: Isolate C12 mutant; associated
FT with altered pathogenesis)"
FT VARIANT 716
FT /note="H -> D (in strain: Isolate C12 mutant)"
FT MUTAGEN 33
FT /note="S->G: Complete loss of infectivity on murine cells."
FT /evidence="ECO:0000269|PubMed:15749126"
FT MUTAGEN 33
FT /note="S->R: No effect for infectivity on murine cells."
FT /evidence="ECO:0000269|PubMed:15749126"
FT MUTAGEN 62
FT /note="T->A,S: No effect for infectivity on murine cells."
FT /evidence="ECO:0000269|PubMed:15749126"
FT MUTAGEN 65
FT /note="L->A,H: No effect for infectivity on murine cells."
FT /evidence="ECO:0000269|PubMed:15749126"
FT MUTAGEN 79..82
FT /note="LALR->AALA: No effect for infectivity on murine
FT cells."
FT /evidence="ECO:0000269|PubMed:15749126"
FT MUTAGEN 79..82
FT /note="LALR->MALM: Complete loss of infectivity on murine
FT cells."
FT /evidence="ECO:0000269|PubMed:15749126"
FT MUTAGEN 162
FT /note="Y->A,H,Q: Complete loss of infectivity on murine
FT cells."
FT /evidence="ECO:0000269|PubMed:15749126"
FT MUTAGEN 162
FT /note="Y->F: No effect for infectivity on murine cells."
FT /evidence="ECO:0000269|PubMed:15749126"
FT MUTAGEN 183
FT /note="K->G: Complete loss of infectivity on murine cells."
FT /evidence="ECO:0000269|PubMed:15749126"
FT MUTAGEN 183
FT /note="K->R: No effect for infectivity on murine cells."
FT /evidence="ECO:0000269|PubMed:15749126"
FT HELIX 970..1015
FT /evidence="ECO:0007829|PDB:1WDG"
FT HELIX 1040..1045
FT /evidence="ECO:0007829|PDB:1WDG"
FT HELIX 1047..1056
FT /evidence="ECO:0007829|PDB:1WDG"
SQ SEQUENCE 1324 AA; 146019 MW; E198EF8F0BCDBF0E CRC64;
MLFVFILFLP SCLGYIGDFR CIQLVNSNGA NVSAPSISTE TVEVSQGLGT YYVLDRVYLN
ATLLLTGYYP VDGSKFRNLA LRGTNSVSLS WFQPPYLNQF NDGIFAKVQN LKTSTPSGAT
AYFPTIVIGS LFGYTSYTVV IEPYNGVIMA SVCQYTICQL PYTDCKPNTN GNKLIGFWHT
DVKPPICVLK RNFTLNVNAD AFYFHFYQHG GTFYAYYADK PSATTFLFSV YIGDILTQYY
VLPFICNPTA GSTFAPRYWV TPLVKRQYLF NFNQKGVITS AVDCASSYTS EIKCKTQSML
PSTGVYELSG YTVQPVGVVY RRVANLPACN IEEWLTARSV PSPLNWERKT FQNCNFNLSS
LLRYVQAESL FCNNIDASKV YGRCFGSISV DKFAVPRSRQ VDLQLGNSGF LQTANYKIDT
AATSCQLHYT LPKNNVTINN HNPSSWNRRY GFNDAGVFGK NQHDVVYAQQ CFTVRSSYCP
CAQPDIVSPC TTQTKPKSAF VNVGDHCEGL GVLEDNCGNA DPHKGCICAN NSFIGWSHDT
CLVNDRCQIF ANILLNGINS GTTCSTDLQL PNTEVVTGIC VKYDLYGITG QGVFKEVKAD
YYNSWQTLLY DVNGNLNGFR DLTTNKTYTI RSCYSGRVSA AFHKDAPEPA LLYRNINCSY
VFSNNISREE NPLNYFDSYL GCVVNADNRT DEALPNCDLR MGAGLCVDYS KSRRAHRSVS
TGYRLTTFEP YTPMLVNDSV QSVDGLYEMQ IPTNFTIGHH EEFIQTRSPK VTIDCAAFVC
GDNTACRQQL VEYGSFCVNV NAILNEVNNL LDNMQLQVAS ALMQGVTISS RLPDGISGPI
DDINFSPLLG CIGSTCAEDG NGPSAIRGRS AIEDLLFDKV KLSDVGFVEA YNNCTGGQEV
RDLLCVQSFN GIKVLPPVLS ESQISGYTTG ATAAAMFPPW SAAAGVPFSL SVQYRINGLG
VTMNVLSENQ KMIASAFNNA LGAIQDGFDA TNSALGKIQS VVNANAEALN NLLNQLSNRF
GAISASLQEI LTRLEAVEAK AQIDRLINGR LTALNAYISK QLSDSTLIKV SAAQAIEKVN
ECVKSQTTRI NFCGNGNHIL SLVQNAPYGL YFIHFSYVPI SFTTANVSPG LCISGDRGLA
PKAGYFVQDD GEWKFTGSSY YYPEPITDKN SVIMSSCAVN YTKAPEVFLN TSIPNPPDFK
EELDKWFKNQ TSIAPDLSLD FEKLNVTLLD LTYEMNRIQD AIKKLNESYI NLKEVGTYEM
YVKWPWYVWL LIGLAGVAVC VLLFFICCCT GCGSCCFKKC GNCCDEYGGH QDSIVIHNIS
SHED
