OAS1B_MOUSE
ID OAS1B_MOUSE Reviewed; 376 AA.
AC Q60856; A8YPE5; A8YPE7; A8YPE8; A8YPE9; E9QKP6; Q78ZX0; Q8JZN0; Q8JZN4;
AC Q8VI98;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Inactive 2'-5'-oligoadenylate synthase 1B;
DE Short=(2-5')oligo(A) synthase 1B;
DE Short=2-5A synthase 1B;
DE AltName: Full=2'-5'-oligoadenylate synthase-like protein 1;
GN Name=Oas1b; Synonyms=Flv, Oias2;
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] (TRUNCATED FORM), FUNCTION, TISSUE SPECIFICITY,
RP VARIANT ALA-65, AND VARIANT GLN-190.
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=12396720; DOI=10.1089/10799900260286696;
RA Kakuta S., Shibata S., Iwakura Y.;
RT "Genomic structure of the mouse 2',5'-oligoadenylate synthetase gene
RT family.";
RL J. Interferon Cytokine Res. 22:981-993(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (LONG AND TRUNCATED FORM), FUNCTION, TISSUE
RP SPECIFICITY, POLYMORPHISM, VARIANT ALA-65, VARIANT GLN-190, VARIANT
RP ARG-266, VARIANT THR-322, VARIANT PRO-336, AND VARIANT PHE-354.
RC STRAIN=C3H/He, and C3H/RV;
RX PubMed=12080145; DOI=10.1073/pnas.142287799;
RA Perelygin A.A., Scherbik S.V., Zhulin I.B., Stockman B.M., Li Y.,
RA Brinton M.A.;
RT "Positional cloning of the murine flavivirus resistance gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9322-9327(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (LONG AND TRUNCATED FORM), POLYMORPHISM, VARIANT
RP PHE-45, VARIANT CYS-63, VARIANT ALA-65, VARIANT TYR-83, VARIANT TYR-103,
RP VARIANT PHE-111, VARIANT GLN-118, VARIANT LEU-176, VARIANT LEU-183, VARIANT
RP THR-184, VARIANT GLN-190, VARIANT HIS-206, VARIANT ARG-266, VARIANT
RP PRO-336, VARIANT ALA-347, VARIANT THR-350, AND VARIANT PHE-354.
RC STRAIN=BALB/cJ, and MBT/Pas;
RX PubMed=12186974; DOI=10.1073/pnas.172195399;
RA Mashimo T., Lucas M., Simon-Chazottes D., Frenkiel M.P., Montagutelli X.,
RA Ceccaldi P.E., Deubel V., Guenet J.L., Despres P.;
RT "A nonsense mutation in the gene encoding 2'-5'-oligoadenylate
RT synthetase/L1 isoform is associated with West Nile virus susceptibility in
RT laboratory mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11311-11316(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (LONG FORM), VARIANT SER-36, VARIANT PHE-45,
RP VARIANT GLN-47, VARIANT GLY-50, VARIANT CYS-63, VARIANT ALA-65, VARIANT
RP TYR-83, VARIANT ARG-90, VARIANT TYR-103, VARIANT ILE-105, VARIANT PHE-111,
RP VARIANT GLN-118, VARIANT VAL-151, VARIANT LEU-176, VARIANT GLU-181, VARIANT
RP LEU-183, VARIANT THR-184, VARIANT HIS-206, VARIANT ARG-266, VARIANT
RP LEU-277, VARIANT PRO-278, VARIANT VAL-291, VARIANT VAL-299, VARIANT
RP VAL-305, VARIANT PRO-336, VARIANT ALA-347, VARIANT THR-350, VARIANT
RP PHE-354, AND VARIANT LEU-368.
RC STRAIN=BID, DHA, MPR, PWD/PhJ, and TEH;
RX PubMed=18460447; DOI=10.1093/molbev/msn106;
RA Ferguson W., Dvora S., Gallo J., Orth A., Boissinot S.;
RT "Long-term balancing selection at the west nile virus resistance gene,
RT Oas1b, maintains transspecific polymorphisms in the house mouse.";
RL Mol. Biol. Evol. 25:1609-1618(2008).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ALA-65, AND VARIANT
RP GLN-190.
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ALA-65, AND VARIANT
RP GLN-190.
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 58-249, VARIANT ALA-65, AND VARIANT GLN-190.
RX PubMed=1709495; DOI=10.1093/nar/19.8.1917;
RA Rutherford M.N., Kumar A., Nissim A., Chebath J., Williams B.R.G.;
RT "The murine 2-5A synthetase locus: three distinct transcripts from two
RT linked genes.";
RL Nucleic Acids Res. 19:1917-1924(1991).
RN [8]
RP FUNCTION.
RX PubMed=16371364; DOI=10.1074/jbc.m508649200;
RA Kajaste-Rudnitski A., Mashimo T., Frenkiel M.P., Guenet J.L., Lucas M.,
RA Despres P.;
RT "The 2',5'-oligoadenylate synthetase 1b is a potent inhibitor of West Nile
RT virus replication inside infected cells.";
RL J. Biol. Chem. 281:4624-4637(2006).
RN [9]
RP REVIEW.
RX PubMed=17024523; DOI=10.1007/s00239-006-0073-3;
RA Perelygin A.A., Zharkikh A.A., Scherbik S.V., Brinton M.A.;
RT "The mammalian 2'-5' oligoadenylate synthetase gene family: evidence for
RT concerted evolution of paralogous Oas1 genes in Rodentia and
RT Artiodactyla.";
RL J. Mol. Evol. 63:562-576(2006).
RN [10]
RP FUNCTION, AND POLYMORPHISM.
RX PubMed=17904183; DOI=10.1016/j.virol.2007.08.017;
RA Scherbik S.V., Kluetzman K., Perelygin A.A., Brinton M.A.;
RT "Knock-in of the Oas1b(r) allele into a flavivirus-induced disease
RT susceptible mouse generates the resistant phenotype.";
RL Virology 368:232-237(2007).
RN [11]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH OSBPL1A AND ABCF3.
RX PubMed=22623793; DOI=10.1128/jvi.00333-12;
RA Courtney S.C., Di H., Stockman B.M., Liu H., Scherbik S.V., Brinton M.A.;
RT "Identification of novel host cell binding partners of Oas1b, the protein
RT conferring resistance to flavivirus-induced disease in mice.";
RL J. Virol. 86:7953-7963(2012).
RN [12]
RP INDUCTION.
RX PubMed=22305621; DOI=10.1016/j.virol.2011.11.025;
RA Pulit-Penaloza J.A., Scherbik S.V., Brinton M.A.;
RT "Activation of Oas1a gene expression by type I IFN requires both STAT1 and
RT STAT2 while only STAT2 is required for Oas1b activation.";
RL Virology 425:71-81(2012).
RN [13]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=27663720; DOI=10.1016/j.meegid.2016.09.018;
RA Elkhateeb E., Tag-El-Din-Hassan H.T., Sasaki N., Torigoe D., Morimatsu M.,
RA Agui T.;
RT "The role of mouse 2',5'-oligoadenylate synthetase 1 paralogs.";
RL Infect. Genet. Evol. 45:393-401(2016).
CC -!- FUNCTION: Does not have 2'-5'-OAS activity, but can bind double-
CC stranded RNA (PubMed:12396720, PubMed:27663720). The full-length
CC protein displays antiviral activity against flaviviruses such as west
CC Nile virus (WNV) via an alternative antiviral pathway independent of
CC RNase L (PubMed:12080145, PubMed:16371364, PubMed:17904183,
CC PubMed:27663720). The truncated form of the protein lacks antiviral
CC activity (PubMed:12080145, PubMed:16371364, PubMed:17904183).
CC {ECO:0000269|PubMed:12080145, ECO:0000269|PubMed:12396720,
CC ECO:0000269|PubMed:16371364, ECO:0000269|PubMed:17904183,
CC ECO:0000269|PubMed:27663720}.
CC -!- SUBUNIT: Interacts with OSBPL1A and ABCF3.
CC {ECO:0000269|PubMed:22623793}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:22623793}; Single-pass type IV membrane protein
CC {ECO:0000305|PubMed:22623793}.
CC -!- TISSUE SPECIFICITY: Highly expressed in lung, spleen and thymus
CC (PubMed:12396720, PubMed:12186974). Also detected at lower levels in
CC heart, kidney, liver, lung, skeletal muscle, testes, uterus and ovaries
CC (PubMed:12396720, PubMed:12186974, PubMed:27663720).
CC {ECO:0000269|PubMed:12186974, ECO:0000269|PubMed:12396720,
CC ECO:0000269|PubMed:27663720}.
CC -!- DEVELOPMENTAL STAGE: Detected 1 week after birth in developing skin,
CC testes, ovary, kidney and lung. {ECO:0000269|PubMed:27663720}.
CC -!- INDUCTION: Up-regulated by the type I interferon IFNB1, in a STAT2-
CC dependent manner (PubMed:22305621). Induced by
CC polyinosinic:polycytidylic acid (poly I:C) (PubMed:12396720,
CC PubMed:27663720). {ECO:0000269|PubMed:12396720,
CC ECO:0000269|PubMed:22305621, ECO:0000269|PubMed:27663720}.
CC -!- POLYMORPHISM: A nonsense mutation in exon 4 results in a premature stop
CC codon leading to a truncated form which determines the
CC resistant/susceptible phenotype of the mice to flaviviruses. Mice
CC encoding the full-length protein show a flavivirus resistance phenotype
CC (Flv(r)), whereas mice encoding a C-terminally truncated protein show a
CC flavivirus susceptible phenotype (Flv(s)).
CC {ECO:0000269|PubMed:12080145, ECO:0000269|PubMed:12186974,
CC ECO:0000269|PubMed:17904183}.
CC -!- SIMILARITY: Belongs to the 2-5A synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB84129.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA39455.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB067529; BAB84129.1; ALT_FRAME; mRNA.
DR EMBL; AF328926; AAM47542.1; -; mRNA.
DR EMBL; AF418004; AAM47544.1; -; mRNA.
DR EMBL; AF418005; AAM47545.1; -; mRNA.
DR EMBL; AF481734; AAM49738.1; -; Genomic_DNA.
DR EMBL; AF466822; AAM97603.1; -; mRNA.
DR EMBL; AF466823; AAM97604.1; -; mRNA.
DR EMBL; AM887907; CAP12708.1; -; Genomic_DNA.
DR EMBL; AM887915; CAP12714.1; -; Genomic_DNA.
DR EMBL; AM887917; CAP12716.1; -; Genomic_DNA.
DR EMBL; AM887918; CAP12717.1; -; Genomic_DNA.
DR EMBL; AM887919; CAP12718.1; -; Genomic_DNA.
DR EMBL; AC115937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466529; EDL19747.1; -; Genomic_DNA.
DR EMBL; X55982; CAA39455.1; ALT_FRAME; mRNA.
DR PIR; S15661; S15661.
DR RefSeq; NP_001077394.1; NM_001083925.1.
DR AlphaFoldDB; Q60856; -.
DR SMR; Q60856; -.
DR BioGRID; 204822; 2.
DR PaxDb; Q60856; -.
DR PeptideAtlas; Q60856; -.
DR PRIDE; Q60856; -.
DR DNASU; 23961; -.
DR GeneID; 23961; -.
DR KEGG; mmu:23961; -.
DR UCSC; uc008zie.1; mouse.
DR CTD; 23961; -.
DR MGI; MGI:97430; Oas1b.
DR InParanoid; Q60856; -.
DR BRENDA; 2.7.7.84; 3474.
DR BioGRID-ORCS; 23961; 0 hits in 19 CRISPR screens.
DR ChiTaRS; Oas1g; mouse.
DR PRO; PR:Q60856; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q60856; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0001730; F:2'-5'-oligoadenylate synthetase activity; IBA:GO_Central.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
DR GO; GO:0060700; P:regulation of ribonuclease activity; IBA:GO_Central.
DR GO; GO:0009615; P:response to virus; IDA:UniProtKB.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR018952; 2-5-oligoAdlate_synth_1_dom2/C.
DR InterPro; IPR026774; 2-5A_synthase.
DR InterPro; IPR006117; 2-5OAS_C_CS.
DR InterPro; IPR043519; NT_sf.
DR PANTHER; PTHR11258; PTHR11258; 1.
DR Pfam; PF10421; OAS1_C; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS00833; 25A_SYNTH_2; 1.
DR PROSITE; PS50152; 25A_SYNTH_3; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; Endoplasmic reticulum; Immunity; Innate immunity;
KW Membrane; Reference proteome; RNA-binding; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..376
FT /note="Inactive 2'-5'-oligoadenylate synthase 1B"
FT /id="PRO_0000160261"
FT TOPO_DOM 1..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..370
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..376
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT VARIANT 36
FT /note="A -> S (in strain: BID, DHA, MPR)"
FT /evidence="ECO:0000269|PubMed:18460447"
FT VARIANT 45
FT /note="S -> F (in strain: MBT/Pas, PWD/Phj)"
FT /evidence="ECO:0000269|PubMed:12186974,
FT ECO:0000269|PubMed:18460447"
FT VARIANT 47
FT /note="R -> Q (in strain: DHA)"
FT /evidence="ECO:0000269|PubMed:18460447"
FT VARIANT 50
FT /note="V -> G (in strain: DHA)"
FT /evidence="ECO:0000269|PubMed:18460447"
FT VARIANT 63
FT /note="G -> C (in strain: BID, DHA, MPR, MBT/Pas, PWD/Phj)"
FT /evidence="ECO:0000269|PubMed:12186974,
FT ECO:0000269|PubMed:18460447"
FT VARIANT 65
FT /note="T -> A (in strain: BALB/c, BID, C57BL/6J, C3H/He,
FT MBT/Pas, PWD/Phj)"
FT /evidence="ECO:0000269|PubMed:12080145,
FT ECO:0000269|PubMed:12186974, ECO:0000269|PubMed:12396720,
FT ECO:0000269|PubMed:1709495, ECO:0000269|PubMed:18460447,
FT ECO:0000269|PubMed:19468303, ECO:0000269|Ref.6"
FT VARIANT 83
FT /note="S -> Y (in strain: BID, DHA, MPR, MBT/Pas, PWD/Phj)"
FT /evidence="ECO:0000269|PubMed:12186974,
FT ECO:0000269|PubMed:18460447"
FT VARIANT 90
FT /note="Q -> R (in strain: DHA)"
FT /evidence="ECO:0000269|PubMed:18460447"
FT VARIANT 103
FT /note="C -> Y (in strain: MBT/Pas, PWD/Phj)"
FT /evidence="ECO:0000269|PubMed:12186974,
FT ECO:0000269|PubMed:18460447"
FT VARIANT 105
FT /note="V -> I (in strain: DHA)"
FT /evidence="ECO:0000269|PubMed:18460447"
FT VARIANT 111
FT /note="C -> F (in strain: MPR, DHA, MBT/Pas, PWD/Phj)"
FT /evidence="ECO:0000269|PubMed:12186974,
FT ECO:0000269|PubMed:18460447"
FT VARIANT 118
FT /note="H -> Q (in strain: MPR, MBT/Pas, PWD/Phj)"
FT /evidence="ECO:0000269|PubMed:12186974,
FT ECO:0000269|PubMed:18460447"
FT VARIANT 151
FT /note="L -> V (in strain: BID, MPR)"
FT /evidence="ECO:0000269|PubMed:18460447"
FT VARIANT 176
FT /note="P -> L (in strain: MBT/Pas, PWD/Phj)"
FT /evidence="ECO:0000269|PubMed:12186974,
FT ECO:0000269|PubMed:18460447"
FT VARIANT 181
FT /note="K -> E (in strain: DHA)"
FT /evidence="ECO:0000269|PubMed:18460447"
FT VARIANT 183
FT /note="S -> L (in strain: BID, MBT/Pas, PWD/Phj)"
FT /evidence="ECO:0000269|PubMed:12186974,
FT ECO:0000269|PubMed:18460447"
FT VARIANT 184
FT /note="I -> T (in strain: BID, DHA, MBT/Pas, PWD/Phj)"
FT /evidence="ECO:0000269|PubMed:12186974,
FT ECO:0000269|PubMed:18460447"
FT VARIANT 190
FT /note="R -> Q (in strain: BALB/c, C57BL/6J, C3H/He)"
FT /evidence="ECO:0000269|PubMed:12080145,
FT ECO:0000269|PubMed:12186974, ECO:0000269|PubMed:12396720,
FT ECO:0000269|PubMed:1709495, ECO:0000269|PubMed:19468303,
FT ECO:0000269|Ref.6"
FT VARIANT 206
FT /note="R -> H (in strain: MBT/Pas, PWD/Phj)"
FT /evidence="ECO:0000269|PubMed:12186974,
FT ECO:0000269|PubMed:18460447"
FT VARIANT 253..376
FT /note="Missing (in the truncated form)"
FT VARIANT 266
FT /note="Q -> R (in strain: BID, C3H/RV, DHA, MPR, MBT/Pas,
FT PWD/Phj)"
FT /evidence="ECO:0000269|PubMed:12080145,
FT ECO:0000269|PubMed:12186974, ECO:0000269|PubMed:18460447"
FT VARIANT 277
FT /note="H -> L (in strain: BID)"
FT /evidence="ECO:0000269|PubMed:18460447"
FT VARIANT 278
FT /note="Q -> P (in strain: DHA)"
FT /evidence="ECO:0000269|PubMed:18460447"
FT VARIANT 291
FT /note="D -> V (in strain: DHA)"
FT /evidence="ECO:0000269|PubMed:18460447"
FT VARIANT 299
FT /note="A -> V (in strain: MPR)"
FT /evidence="ECO:0000269|PubMed:18460447"
FT VARIANT 305
FT /note="I -> V (in strain: MPR)"
FT /evidence="ECO:0000269|PubMed:18460447"
FT VARIANT 322
FT /note="A -> T (in strain: C3H/RV)"
FT /evidence="ECO:0000269|PubMed:12080145"
FT VARIANT 336
FT /note="S -> P (in strain: C3H/RV, DHA, MPR, MBT/Pas, PWD/
FT Phj)"
FT /evidence="ECO:0000269|PubMed:12080145,
FT ECO:0000269|PubMed:12186974, ECO:0000269|PubMed:18460447"
FT VARIANT 347
FT /note="G -> A (in strain: DHA, MBT/Pas, PWD/Phj)"
FT /evidence="ECO:0000269|PubMed:12186974,
FT ECO:0000269|PubMed:18460447"
FT VARIANT 350
FT /note="M -> T (in strain: BID, DHA, MBT/Pas, PWD/Phj)"
FT /evidence="ECO:0000269|PubMed:12186974,
FT ECO:0000269|PubMed:18460447"
FT VARIANT 354
FT /note="L -> F (in strain: BID, C3H/RV, DHA, MPR, MBT/Pas,
FT PWD/Phj)"
FT /evidence="ECO:0000269|PubMed:12080145,
FT ECO:0000269|PubMed:12186974, ECO:0000269|PubMed:18460447"
FT VARIANT 368
FT /note="F -> L (in strain: MPR)"
FT /evidence="ECO:0000269|PubMed:18460447"
FT CONFLICT 58..60
FT /note="GVK -> VFQ (in Ref. 7; CAA39455)"
FT /evidence="ECO:0000305"
FT CONFLICT 234..235
FT /note="VY -> LD (in Ref. 1; BAB84129 and 7; CAA39455)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 43620 MW; 0733589FC702D4C7 CRC64;
MEQDLRSIPA SKLDKFIENH LPDTSFCADL REVIDALCAL LKDRSFRGPV RRMRASKGVK
GKGTTLKGRS DADLVVFLNN LTSFEDQLNQ QGVLIKEIKK QLCEVQHERR CGVKFEVHSL
RSPNSRALSF KLSAPDLLKE VKFDVLPAYD LLDHLNILKK PNQQFYANLI SGRTPPGKEG
KLSICFMGLR KYFLNCRPTK LKRLIRLVTH WYQLCKEKLG DPLPPQYALE LLTVYAWEYG
SRVTKFNTAQ GFRTVLELVT KYKQLQIYWT VYYDFRHQEV SEYLHQQLKK DRPVILDPAD
PTRNIAGLNP KDWRRLAGEA AAWLQYPCFK YRDGSSVCSW EVPTEVGVPM KYLLCRIFWL
LFWSLFHFIF GKTSSG
