SPIKE_IBVB
ID SPIKE_IBVB Reviewed; 1162 AA.
AC P11223; P05134; Q4ZJS1;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 23-FEB-2022, entry version 122.
DE RecName: Full=Spike glycoprotein {ECO:0000255|HAMAP-Rule:MF_04098};
DE Short=S glycoprotein {ECO:0000255|HAMAP-Rule:MF_04098};
DE AltName: Full=E2 {ECO:0000255|HAMAP-Rule:MF_04098};
DE AltName: Full=Peplomer protein {ECO:0000255|HAMAP-Rule:MF_04098};
DE Contains:
DE RecName: Full=Spike protein S1 {ECO:0000255|HAMAP-Rule:MF_04098};
DE Contains:
DE RecName: Full=Spike protein S2 {ECO:0000255|HAMAP-Rule:MF_04098};
DE Contains:
DE RecName: Full=Spike protein S2' {ECO:0000255|HAMAP-Rule:MF_04098};
DE Flags: Precursor;
GN Name=S {ECO:0000255|HAMAP-Rule:MF_04098}; ORFNames=2;
OS Avian infectious bronchitis virus (strain Beaudette) (IBV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Gammacoronavirus; Igacovirus.
OX NCBI_TaxID=11122;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2984314; DOI=10.1099/0022-1317-66-4-719;
RA Binns M.M., Boursnell M.E.G., Cavanagh D., Pappin D.J.C., Brown T.D.K.;
RT "Cloning and sequencing of the gene encoding the spike protein of the
RT coronavirus IBV.";
RL J. Gen. Virol. 66:719-726(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3025348; DOI=10.1099/0022-1317-67-12-2825;
RA Binns M.M., Boursnell M.E.G., Tomley F.M., Brown T.D.K.;
RT "Comparison of the spike precursor sequences of coronavirus IBV strains M41
RT and 6/82 with that of IBV Beaudette.";
RL J. Gen. Virol. 67:2825-2831(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA / MRNA].
RC STRAIN=Isolate Vero cell-adapted p36, and Isolate Vero cell-adapted p65;
RX PubMed=16137658; DOI=10.1016/j.bbrc.2005.08.105;
RA Fang S.G., Shen S., Tay F.P., Liu D.X.;
RT "Selection of and recombination between minor variants lead to the
RT adaptation of an avian coronavirus to primate cells.";
RL Biochem. Biophys. Res. Commun. 336:417-423(2005).
RN [4]
RP SUBCELLULAR LOCATION, DI-LYSINE MOTIF, AND MUTAGENESIS OF LYS-1159 AND
RP LYS-1160.
RC STRAIN=Isolate Vero cell-adapted p65;
RX PubMed=15140989; DOI=10.1128/jvi.78.11.5913-5922.2004;
RA Lontok E., Corse E., Machamer C.E.;
RT "Intracellular targeting signals contribute to localization of coronavirus
RT spike proteins near the virus assembly site.";
RL J. Virol. 78:5913-5922(2004).
RN [5]
RP FUNCTION OF SPIKE PROTEIN S2.
RX PubMed=16537586; DOI=10.1128/jvi.80.7.3180-3188.2006;
RA Chu V.C., McElroy L.J., Chu V., Bauman B.E., Whittaker G.R.;
RT "The avian coronavirus infectious bronchitis virus undergoes direct low-pH-
RT dependent fusion activation during entry into host cells.";
RL J. Virol. 80:3180-3188(2006).
RN [6]
RP CLEAVAGE.
RX PubMed=19553314; DOI=10.1128/jvi.00613-09;
RA Yamada Y., Liu D.X.;
RT "Proteolytic activation of the spike protein at a novel RRRR/S motif is
RT implicated in furin-dependent entry, syncytium formation, and infectivity
RT of coronavirus infectious bronchitis virus in cultured cells.";
RL J. Virol. 83:8744-8758(2009).
RN [7]
RP FUNCTION.
RC STRAIN=M41;
RX PubMed=24314633; DOI=10.1016/j.virol.2013.09.018;
RA Promkuntod N., van Eijndhoven R.E., de Vrieze G., Groene A., Verheije M.H.;
RT "Mapping of the receptor-binding domain and amino acids critical for
RT attachment in the spike protein of avian coronavirus infectious bronchitis
RT virus.";
RL Virology 448:26-32(2014).
RN [8]
RP GLYCOSYLATION AT ASN-212; ASN-237; ASN-247; ASN-276; ASN-513; ASN-591;
RP ASN-1051 AND ASN-1074.
RX PubMed=29035787; DOI=10.1016/j.virol.2017.10.003;
RA Zheng J., Yamada Y., Fung T.S., Huang M., Chia R., Liu D.X.;
RT "Identification of N-linked glycosylation sites in the spike protein and
RT their functional impact on the replication and infectivity of coronavirus
RT infectious bronchitis virus in cell culture.";
RL Virology 513:65-74(2018).
CC -!- FUNCTION: [Spike protein S1]: Attaches the virion to the host cell
CC membrane by interacting with sialic acids, initiating the infection.
CC {ECO:0000255|HAMAP-Rule:MF_04098, ECO:0000269|PubMed:16537586,
CC ECO:0000269|PubMed:24314633}.
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 3 conformational states:
CC pre-fusion native state, pre-hairpin intermediate state, and post-
CC fusion hairpin state. During viral and target cell membrane fusion, the
CC coiled coil regions (heptad repeats) assume a trimer-of-hairpins
CC structure, positioning the fusion peptide in close proximity to the C-
CC terminal region of the ectodomain. The formation of this structure
CC appears to drive apposition and subsequent fusion of viral and target
CC cell membranes. {ECO:0000255|HAMAP-Rule:MF_04098}.
CC -!- FUNCTION: [Spike protein S2']: Acts as a viral fusion peptide after S2
CC cleavage occurring upon virus endocytosis. {ECO:0000255|HAMAP-
CC Rule:MF_04098}.
CC -!- SUBUNIT: Homotrimer; each monomer consists of a S1 and a S2 subunit.
CC The resulting peplomers protrude from the virus surface as spikes.
CC {ECO:0000255|HAMAP-Rule:MF_04098}.
CC -!- INTERACTION:
CC P11223; O00303: EIF3F; Xeno; NbExp=2; IntAct=EBI-25497861, EBI-711990;
CC -!- SUBCELLULAR LOCATION: [Spike protein S2]: Virion membrane
CC {ECO:0000255|HAMAP-Rule:MF_04098}; Single-pass type I membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04098}. Host endoplasmic reticulum-Golgi
CC intermediate compartment membrane {ECO:0000255|HAMAP-Rule:MF_04098};
CC Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04098}.
CC Note=Accumulates in the endoplasmic reticulum-Golgi intermediate
CC compartment, where it participates in virus particle assembly. Some S
CC oligomers may be transported to the plasma membrane, where they may
CC mediate cell-cell fusion. {ECO:0000255|HAMAP-Rule:MF_04098}.
CC -!- SUBCELLULAR LOCATION: [Spike protein S1]: Virion membrane
CC {ECO:0000255|HAMAP-Rule:MF_04098}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04098}. Host endoplasmic reticulum-Golgi
CC intermediate compartment membrane {ECO:0000255|HAMAP-Rule:MF_04098};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04098}.
CC Note=Accumulates in the endoplasmic reticulum-Golgi intermediate
CC compartment, where it participates in virus particle assembly. Some S
CC oligomers may be transported to the plasma membrane, where they may
CC mediate cell-cell fusion. S1 is not anchored to the viral envelope, but
CC associates with the extravirion surface through its binding to S2.
CC {ECO:0000255|HAMAP-Rule:MF_04098}.
CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum localization
CC for type I membrane proteins. {ECO:0000255|HAMAP-Rule:MF_04098}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. The
CC precursor is processed into S1 and S2 by host cell furin or furin-like
CC protease to yield the mature S1 and S2 proteins. The cleavage site
CC between S1 and S2 requires the optimal sequence [KR]-X-[KR]-R.
CC Additionally, a second cleavage leads to the release of a fusion
CC peptide after viral attachment to host cell receptor.
CC {ECO:0000255|HAMAP-Rule:MF_04098, ECO:0000269|PubMed:19553314}.
CC -!- SIMILARITY: Belongs to the gammacoronaviruses spike protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04098}.
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DR EMBL; M95169; AAA70235.1; -; Genomic_RNA.
DR EMBL; X02342; CAA26201.1; -; Genomic_RNA.
DR EMBL; DQ001342; AAY21248.1; -; mRNA.
DR EMBL; DQ001339; AAY24433.1; -; Genomic_RNA.
DR PIR; S14939; S14939.
DR RefSeq; NP_040831.1; NC_001451.1.
DR SMR; P11223; -.
DR ELM; P11223; -.
DR IntAct; P11223; 1.
DR iPTMnet; P11223; -.
DR GeneID; 1489741; -.
DR KEGG; vg:1489741; -.
DR Proteomes; UP000006717; Genome.
DR GO; GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IDA:UniProtKB.
DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IEA:InterPro.
DR HAMAP; MF_04098; GAMMA_CORONA_SPIKE; 1.
DR InterPro; IPR043607; CoV_S1_C.
DR InterPro; IPR043473; S2_sf_CoV.
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; PF19209; CoV_S1_C; 1.
DR Pfam; PF01601; CoV_S2; 1.
DR Pfam; PF19214; CoV_S2_C; 1.
DR SUPFAM; SSF111474; SSF111474; 2.
DR PROSITE; PS51923; COV_S2_HR1; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Coiled coil;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein; Host membrane;
KW Host-virus interaction; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral envelope protein; Viral penetration into host cytoplasm; Virion;
KW Virulence; Virus endocytosis by host; Virus entry into host cell.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CHAIN 19..1162
FT /note="Spike glycoprotein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT /id="PRO_0000037162"
FT CHAIN 19..537
FT /note="Spike protein S1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098,
FT ECO:0000269|PubMed:29035787"
FT /id="PRO_0000037163"
FT CHAIN 538..1162
FT /note="Spike protein S2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098,
FT ECO:0000269|PubMed:29035787"
FT /id="PRO_0000037164"
FT CHAIN 691..1162
FT /note="Spike protein S2'"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098,
FT ECO:0000269|PubMed:29035787"
FT /id="PRO_0000444092"
FT TOPO_DOM 19..1095
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT TRANSMEM 1096..1116
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT TOPO_DOM 1117..1162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT REGION 769..874
FT /note="Heptad repeat 1 (HR1)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01271"
FT REGION 1024..1105
FT /note="Heptad repeat 2 (HR2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01272"
FT COILED 822..866
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT COILED 1055..1083
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT MOTIF 1159..1162
FT /note="Di-lysine motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT SITE 537..538
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098,
FT ECO:0000269|PubMed:19553314"
FT SITE 690..691
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098,
FT ECO:0000269|PubMed:19553314"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098,
FT ECO:0000269|PubMed:29035787"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098,
FT ECO:0000269|PubMed:29035787"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098,
FT ECO:0000269|PubMed:29035787"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098,
FT ECO:0000269|PubMed:29035787"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098,
FT ECO:0000269|PubMed:29035787"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 579
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098,
FT ECO:0000269|PubMed:29035787"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 676
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 714
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 947
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 960
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 979
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 1014
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 1038
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 1051
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098,
FT ECO:0000269|PubMed:29035787"
FT CARBOHYD 1074
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098,
FT ECO:0000269|PubMed:29035787"
FT VARIANT 122
FT /note="L -> I (in strain: Isolate Vero cell-adapted p36 and
FT Isolate Vero cell-adapted p65)"
FT VARIANT 130
FT /note="L -> F (in strain: Isolate Vero cell-adapted p36 and
FT Isolate Vero cell-adapted p65)"
FT VARIANT 364
FT /note="K -> R (in strain: Isolate Vero cell-adapted p36 and
FT Isolate Vero cell-adapted p65)"
FT VARIANT 405
FT /note="G -> D (in strain: Isolate Vero cell-adapted p36 and
FT Isolate Vero cell-adapted p65)"
FT VARIANT 421
FT /note="N -> H (in strain: Isolate Vero cell-adapted p36 and
FT Isolate Vero cell-adapted p65)"
FT VARIANT 623
FT /note="K -> N (in strain: Isolate Vero cell-adapted p36 and
FT Isolate Vero cell-adapted p65)"
FT VARIANT 683
FT /note="N -> T (in strain: Isolate Vero cell-adapted p36 and
FT Isolate Vero cell-adapted p65)"
FT VARIANT 689
FT /note="K -> R (in strain: Isolate Vero cell-adapted p36 and
FT Isolate Vero cell-adapted p65)"
FT VARIANT 692
FT /note="L -> V (in strain: Isolate Vero cell-adapted p36 and
FT Isolate Vero cell-adapted p65)"
FT VARIANT 709
FT /note="N -> D (in strain: Isolate Vero cell-adapted p36 and
FT Isolate Vero cell-adapted p65)"
FT VARIANT 723
FT /note="F -> L (in strain: Isolate Vero cell-adapted p36 and
FT Isolate Vero cell-adapted p65)"
FT VARIANT 1012
FT /note="S -> I (in strain: Isolate Vero cell-adapted p36 and
FT Isolate Vero cell-adapted p65)"
FT MUTAGEN 1159
FT /note="K->A: Localizes exclusively to the cell membrane."
FT /evidence="ECO:0000269|PubMed:15140989"
FT MUTAGEN 1160
FT /note="K->A: Localizes exclusively to the cell membrane."
FT /evidence="ECO:0000269|PubMed:15140989"
SQ SEQUENCE 1162 AA; 128047 MW; 0BAAD58113C8EBD5 CRC64;
MLVTPLLLVT LLCALCSAVL YDSSSYVYYY QSAFRPPSGW HLQGGAYAVV NISSEFNNAG
SSSGCTVGII HGGRVVNASS IAMTAPSSGM AWSSSQFCTA HCNFSDTTVF VTHCYKHGGC
PLTGMLQQNL IRVSAMKNGQ LFYNLTVSVA KYPTFRSFQC VNNLTSVYLN GDLVYTSNET
IDVTSAGVYF KAGGPITYKV MREVKALAYF VNGTAQDVIL CDGSPRGLLA CQYNTGNFSD
GFYPFTNSSL VKQKFIVYRE NSVNTTCTLH NFIFHNETGA NPNPSGVQNI QTYQTKTAQS
GYYNFNFSFL SSFVYKESNF MYGSYHPSCK FRLETINNGL WFNSLSVSIA YGPLQGGCKQ
SVFKGRATCC YAYSYGGPSL CKGVYSGELD HNFECGLLVY VTKSGGSRIQ TATEPPVITQ
NNYNNITLNT CVDYNIYGRT GQGFITNVTD SAVSYNYLAD AGLAILDTSG SIDIFVVQGE
YGLNYYKVNP CEDVNQQFVV SGGKLVGILT SRNETGSQLL ENQFYIKITN GTRRFRRSIT
ENVANCPYVS YGKFCIKPDG SIATIVPKQL EQFVAPLFNV TENVLIPNSF NLTVTDEYIQ
TRMDKVQINC LQYVCGSSLD CRKLFQQYGP VCDNILSVVN SVGQKEDMEL LNFYSSTKPA
GFNTPVLSNV STGEFNISLL LTNPSSRRKR SLIEDLLFTS VESVGLPTND AYKNCTAGPL
GFFKDLACAR EYNGLLVLPP IITAEMQALY TSSLVASMAF GGITAAGAIP FATQLQARIN
HLGITQSLLL KNQEKIAASF NKAIGHMQEG FRSTSLALQQ IQDVVSKQSA ILTETMASLN
KNFGAISSVI QEIYQQFDAI QANAQVDRLI TGRLSSLSVL ASAKQAEYIR VSQQRELATQ
KINECVKSQS IRYSFCGNGR HVLTIPQNAP NGIVFIHFSY TPDSFVNVTA IVGFCVKPAN
ASQYAIVPAN GRGIFIQVNG SYYITARDMY MPRAITAGDV VTLTSCQANY VSVNKTVITT
FVDNDDFDFN DELSKWWNDT KHELPDFDKF NYTVPILDID SEIDRIQGVI QGLNDSLIDL
EKLSILKTYI KWPWYVWLAI AFATIIFILI LGWVFFMTGC CGCCCGCFGI MPLMSKCGKK
SSYYTTFDND VVTEQYRPKK SV
