POL1_CPMVS
ID POL1_CPMVS Reviewed; 1866 AA.
AC P03600;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=RNA1 polyprotein;
DE AltName: Full=B RNA polyprotein;
DE AltName: Full=Bottom component polyprotein;
DE AltName: Full=Genome polyprotein B;
DE AltName: Full=P1;
DE Contains:
DE RecName: Full=Protease cofactor;
DE AltName: Full=32 kDa protein;
DE Contains:
DE RecName: Full=Putative helicase;
DE EC=3.6.4.-;
DE AltName: Full=58 kDa protein;
DE AltName: Full=Membrane-binding protein;
DE AltName: Full=NTP-binding protein;
DE Short=NTB;
DE Contains:
DE RecName: Full=Viral genome-linked protein;
DE AltName: Full=VPg;
DE Contains:
DE RecName: Full=Picornain 3C-like protease;
DE Short=3C-like protease;
DE EC=3.4.22.- {ECO:0000269|PubMed:16789216};
DE AltName: Full=24 kDa protein;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase {ECO:0000255|PROSITE-ProRule:PRU00539};
DE EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539, ECO:0000269|PubMed:1431806};
DE AltName: Full=87 kDa protein;
OS Cowpea mosaic virus (strain SB) (CPMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Secoviridae; Comovirinae; Comovirus.
OX NCBI_TaxID=928299;
OH NCBI_TaxID=3821; Cajanus cajan (Pigeon pea) (Cajanus indicus).
OH NCBI_TaxID=3829; Crotalaria juncea (Sunn hemp).
OH NCBI_TaxID=3917; Vigna unguiculata (Cowpea).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16453487; DOI=10.1002/j.1460-2075.1983.tb01731.x;
RA Lomonossoff G.P., Shanks M.;
RT "The nucleotide sequence of cowpea mosaic virus B RNA.";
RL EMBO J. 2:2253-2258(1983).
RN [2]
RP PROTEIN SEQUENCE OF 920-922, IDENTIFICATION (VIRAL GENOME-LINKED PROTEIN),
RP AND FUNCTION (VIRAL GENOME-LINKED PROTEIN).
RX PubMed=16453534; DOI=10.1002/j.1460-2075.1984.tb02021.x;
RA Zabel P., Moerman M., Lomonossoff G., Shanks M., Beyreuther K.;
RT "Cowpea mosaic virus VPg: sequencing of radiochemically modified protein
RT allows mapping of the gene on B RNA.";
RL EMBO J. 3:1629-1634(1984).
RN [3]
RP PROTEIN SEQUENCE OF 2-39; 327-349; 948-979 AND 1156-1178, AND PROTEOLYTIC
RP CLEAVAGE (RNA1 POLYPROTEIN).
RX PubMed=16789257; DOI=10.1128/jvi.59.1.50-58.1986;
RA Wellink J., Rezelman G., Goldbach R., Beyreuther K.;
RT "Determination of the proteolytic processing sites in the polyprotein
RT encoded by the bottom-component RNA of cowpea mosaic virus.";
RL J. Virol. 59:50-58(1986).
RN [4]
RP PROTEOLYTIC CLEAVAGE (RNA1 POLYPROTEIN), CATALYTIC ACTIVITY (PICORNAIN
RP 3C-LIKE PROTEASE), AND FUNCTION (PICORNAIN 3C-LIKE PROTEASE).
RX PubMed=16789216; DOI=10.1128/jvi.41.1.8-17.1982;
RA Franssen H., Goldbach R., Broekhuijsen M., Moerman M., van Kammen A.;
RT "Expression of Middle-Component RNA of Cowpea Mosaic Virus: In Vitro
RT Generation of a Precursor to Both Capsid Proteins by a Bottom-Component
RT RNA-Encoded Protease from Infected Cells.";
RL J. Virol. 41:8-17(1982).
RN [5]
RP COVALENT RNA LINKAGE AT SER-920 (VPG), AND URIDYLYLATION (VIRAL
RP GENOME-LINKED PROTEIN).
RA Jaegle M., Wellink J., Goldbach R.;
RT "The genome-linked protein of cowpea mosaic virus is bound to the 5'
RT terminus of virus RNA by a phosphodiester linkage to serine.";
RL J. Gen. Virol. 68:627-632(1987).
RN [6]
RP FUNCTION (PICORNAIN 3C-LIKE PROTEASE).
RX PubMed=16453750; DOI=10.1002/j.1460-2075.1987.tb04789.x;
RA Verver J., Goldbach R., Garcia J.A., Vos P.;
RT "In vitro expression of a full-length DNA copy of cowpea mosaic virus B
RT RNA: identification of the B RNA encoded 24-kd protein as a viral
RT protease.";
RL EMBO J. 6:549-554(1987).
RN [7]
RP ACTIVE SITE (PICORNAIN 3C-LIKE PROTEASE), AND MUTAGENESIS OF CYS-1113.
RX PubMed=1887592; DOI=10.1016/0042-6822(91)90444-g;
RA Dessens J.T., Lomonossoff G.P.;
RT "Mutational analysis of the putative catalytic triad of the cowpea mosaic
RT virus 24K protease.";
RL Virology 184:738-746(1991).
RN [8]
RP FUNCTION (PROTEASE COFACTOR).
RX PubMed=1413528; DOI=10.1016/0042-6822(92)90168-o;
RA Peters S.A., Voorhorst W.G., Wery J., Wellink J., van Kammen A.;
RT "A regulatory role for the 32K protein in proteolytic processing of cowpea
RT mosaic virus polyproteins.";
RL Virology 191:81-89(1992).
RN [9]
RP CATALYTIC ACTIVITY (RNA-DIRECTED RNA POLYMERASE), FUNCTION (RNA-DIRECTED
RP RNA POLYMERASE), AND PROTEOLYTIC CLEAVAGE (RNA1 POLYPROTEIN).
RX PubMed=1431806; DOI=10.1099/0022-1317-73-11-2775;
RA van Bokhoven H., van Lent J.W., Custers R., Vlak J.M., Wellink J.,
RA van Kammen A.;
RT "Synthesis of the complete 200K polyprotein encoded by cowpea mosaic virus
RT B-RNA in insect cells.";
RL J. Gen. Virol. 73:2775-2784(1992).
RN [10]
RP MUTAGENESIS OF LYS-500 AND ASP-545, AND PROTEOLYTIC CLEAVAGE (RNA1
RP POLYPROTEIN).
RX PubMed=7964626; DOI=10.1099/0022-1317-75-11-3167;
RA Peters S.A., Verver J., Nollen E.A., van Lent J.W., Wellink J.,
RA van Kammen A.;
RT "The NTP-binding motif in cowpea mosaic virus B polyprotein is essential
RT for viral replication.";
RL J. Gen. Virol. 75:3167-3176(1994).
RN [11]
RP FUNCTION (PICORNAIN 3C-LIKE PROTEASE).
RX PubMed=8811039; DOI=10.1099/0022-1317-77-9-2365;
RA Shanks M., Dessens J.T., Lomonossoff G.P.;
RT "The 24 kDa proteinases of comoviruses are virus-specific in cis as well as
RT in trans.";
RL J. Gen. Virol. 77:2365-2369(1996).
RN [12]
RP SUBCELLULAR LOCATION (RNA-DIRECTED RNA POLYMERASE).
RX PubMed=10864669; DOI=10.1128/jvi.74.14.6556-6563.2000;
RA Carette J.E., Stuiver M., Van Lent J., Wellink J., Van Kammen A.;
RT "Cowpea mosaic virus infection induces a massive proliferation of
RT endoplasmic reticulum but not Golgi membranes and is dependent on de novo
RT membrane synthesis.";
RL J. Virol. 74:6556-6563(2000).
RN [13]
RP FUNCTION (VIRAL GENOME-LINKED PROTEIN), AND MUTAGENESIS OF
RP 920-SER--LYS-922; 928-MET-GLN-929; 934-ASN--VAL-936; 939-LYS--VAL-942;
RP 945-ASP-ALA-946 AND GLN-947.
RX PubMed=11883002; DOI=10.1006/viro.2001.1137;
RA Carette J.E., Kujawa A., Guhl K., Verver J., Wellink J., Van Kammen A.;
RT "Mutational analysis of the genome-linked protein of cowpea mosaic virus.";
RL Virology 290:21-29(2001).
RN [14]
RP FUNCTION (PROTEASE COFACTOR), FUNCTION (PUTATIVE HELICASE), SUBCELLULAR
RP LOCATION (PROTEASE COFACTOR), AND SUBCELLULAR LOCATION (PUTATIVE HELICASE).
RX PubMed=12021362; DOI=10.1128/jvi.76.12.6293-6301.2002;
RA Carette J.E., van Lent J., MacFarlane S.A., Wellink J., van Kammen A.;
RT "Cowpea mosaic virus 32- and 60-kilodalton replication proteins target and
RT change the morphology of endoplasmic reticulum membranes.";
RL J. Virol. 76:6293-6301(2002).
CC -!- FUNCTION: [Picornain 3C-like protease]: Thiol protease that cleaves the
CC RNA1 and RNA2 polyproteins. {ECO:0000269|PubMed:16453750,
CC ECO:0000269|PubMed:16789216, ECO:0000269|PubMed:8811039}.
CC -!- FUNCTION: [Viral genome-linked protein]: Plays a role in RNA
CC replication. It is covalently linked to the 5'terminus of both viral
CC single-stranded RNA1 and RNA2 molecules. {ECO:0000269|PubMed:11883002,
CC ECO:0000269|PubMed:16453534}.
CC -!- FUNCTION: [Protease cofactor]: Down-regulates the RNA1 polyprotein
CC processing and enhances trans-cleavage of RNA2 polyproteins
CC (PubMed:1413528). The protease cofactor and the putative helicase seem
CC to target the replication complexes to ER membranes. Their physical
CC association causes the membrane rearrangement of host ER that may
CC result in formation of the small membranous vesicles that are the site
CC of viral RNA synthesis (PubMed:12021362). {ECO:0000269|PubMed:12021362,
CC ECO:0000269|PubMed:1413528}.
CC -!- FUNCTION: [Putative helicase]: The protease cofactor and the putative
CC helicase seem to target the replication complexes to ER membranes.
CC Their physical association causes the membrane rearrangement of host ER
CC that may result in formation of the small membranous vesicles that are
CC the site of viral RNA synthesis. {ECO:0000269|PubMed:12021362}.
CC -!- FUNCTION: [RNA-directed RNA polymerase]: Replicates the viral genome.
CC {ECO:0000305|PubMed:1431806}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- SUBCELLULAR LOCATION: [Putative helicase]: Host membrane {ECO:0000305};
CC Single-pass membrane protein {ECO:0000305}. Host cytoplasm, host
CC perinuclear region {ECO:0000269|PubMed:12021362}.
CC -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host endoplasmic
CC reticulum {ECO:0000269|PubMed:10864669}.
CC -!- SUBCELLULAR LOCATION: [Protease cofactor]: Host cytoplasm, host
CC perinuclear region {ECO:0000269|PubMed:12021362}.
CC -!- PTM: [RNA1 polyprotein]: Specific enzymatic cleavages by picornain 3C-
CC like protease in vivo yield mature proteins (PubMed:16789216,
CC PubMed:16789257, PubMed:7964626, PubMed:1431806). Picornain 3C-like
CC protease is autocatalytically processed. {ECO:0000269|PubMed:1431806,
CC ECO:0000269|PubMed:16789216, ECO:0000269|PubMed:16789257,
CC ECO:0000269|PubMed:7964626}.
CC -!- PTM: [Viral genome-linked protein]: Uridylylated by the polymerase and
CC is covalently linked to the 5'-end of genomic RNA. This uridylylated
CC form acts as a nucleotide-peptide primer for the polymerase.
CC {ECO:0000269|Ref.5}.
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DR EMBL; X00206; CAA25029.1; -; Genomic_RNA.
DR PIR; A04211; GNWE2C.
DR RefSeq; NP_613283.1; NC_003549.1.
DR BMRB; P03600; -.
DR SMR; P03600; -.
DR MEROPS; C03.003; -.
DR GeneID; 956628; -.
DR KEGG; vg:956628; -.
DR Proteomes; UP000008589; Genome.
DR GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IDA:UniProtKB.
DR GO; GO:0039690; P:positive stranded viral RNA replication; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0070613; P:regulation of protein processing; IDA:UniProtKB.
DR GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
DR GO; GO:0018259; P:RNA-protein covalent cross-linking via peptidyl-serine; IMP:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0019082; P:viral protein processing; IDA:UniProtKB.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR044067; PCV_3C_PRO.
DR InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR Pfam; PF00548; Peptidase_C3; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00910; RNA_helicase; 1.
DR PRINTS; PR00918; CALICVIRUSNS.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51874; PCV_3C_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Covalent protein-RNA linkage; Direct protein sequencing;
KW Helicase; Host cytoplasm; Host endoplasmic reticulum; Host membrane;
KW Hydrolase; Membrane; Nucleotide-binding; Nucleotidyltransferase;
KW Phosphoprotein; Protease; Reference proteome; RNA-directed RNA polymerase;
KW Thiol protease; Transferase; Transmembrane; Transmembrane helix;
KW Viral RNA replication.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16789257"
FT CHAIN 2..1866
FT /note="RNA1 polyprotein"
FT /id="PRO_0000445834"
FT CHAIN 2..326
FT /note="Protease cofactor"
FT /id="PRO_0000037006"
FT CHAIN 327..919
FT /note="Putative helicase"
FT /id="PRO_0000037007"
FT CHAIN 920..947
FT /note="Viral genome-linked protein"
FT /id="PRO_0000037008"
FT CHAIN 948..1155
FT /note="Picornain 3C-like protease"
FT /id="PRO_0000037009"
FT CHAIN 1156..1866
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000037010"
FT TRANSMEM 897..917
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 462..633
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 945..1150
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 1429..1559
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ACT_SITE 987
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222,
FT ECO:0000269|PubMed:1887592"
FT ACT_SITE 1023
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222,
FT ECO:0000269|PubMed:1887592"
FT ACT_SITE 1113
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222,
FT ECO:0000269|PubMed:1887592"
FT BINDING 494..501
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551,
FT ECO:0000305|PubMed:7964626"
FT SITE 326..327
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:16789257"
FT SITE 919..920
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000305|PubMed:16453534"
FT SITE 947..948
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:16789257"
FT SITE 1155..1156
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:16789257"
FT MOD_RES 920
FT /note="O-(5'-phospho-RNA)-serine"
FT /evidence="ECO:0000269|Ref.5"
FT MUTAGEN 500
FT /note="K->T: Complete loss of viral replication; reduced
FT ATP-binding by the RNA-directed RNA polymerase; no effect
FT on polyprotein processing."
FT /evidence="ECO:0000269|PubMed:7964626"
FT MUTAGEN 545
FT /note="D->P: Complete loss of viral replication; no effect
FT on polyprotein processing."
FT /evidence="ECO:0000269|PubMed:7964626"
FT MUTAGEN 920..922
FT /note="SRK->GRS: Increased efficiency of cleavage between
FT the putative helicase and VPg. Complete loss of
FT infectivity."
FT /evidence="ECO:0000269|PubMed:11883002"
FT MUTAGEN 920..921
FT /note="SR->YG: Slightly decreased efficiency of cleavage
FT between the putative helicase and VPg. Complete loss of
FT infectivity."
FT MUTAGEN 920
FT /note="S->T: Decreased efficiency of cleavage between the
FT putative helicase and VPg. Complete loss of infectivity."
FT MUTAGEN 928..929
FT /note="MQ->VA: No effect on infectivity."
FT /evidence="ECO:0000269|PubMed:11883002"
FT MUTAGEN 934..936
FT /note="NNV->RNI: 80% decrease of infectivity."
FT /evidence="ECO:0000269|PubMed:11883002"
FT MUTAGEN 939..942
FT /note="KRRV->RKRN: Complete loss of infectivity."
FT /evidence="ECO:0000269|PubMed:11883002"
FT MUTAGEN 945..946
FT /note="DA->EG: 50% decrease of infectivity. Replicative
FT proteins display a uniform cytoplasmic distribution,
FT instead of the normal accumulation near the nucleus."
FT /evidence="ECO:0000269|PubMed:11883002"
FT MUTAGEN 947
FT /note="Q->H: Strongly decreased efficiency of cleavage
FT between VPg and 3C-like protease. Complete loss of
FT infectivity."
FT /evidence="ECO:0000269|PubMed:11883002"
FT MUTAGEN 1113
FT /note="C->S: Reduced protease activity."
FT /evidence="ECO:0000269|PubMed:1887592"
SQ SEQUENCE 1866 AA; 209810 MW; 0D4CD8A11C0B2976 CRC64;
MGLPEYEADS EALLSQLTIE FTPGMTVSSL LAQVTTNDFH SAIEFFAAEK AVDIEGVHYN
AYMQQIRKNP SLLRISVVAY AFHVSDMVAE TMSYDVYEFL YKHYALFISN LVTRTLRFKE
LLLFCKQQFL EKMQASIVWA PELEQYLQVE GDAVAQGVSQ LLYKMVTWVP TFVRGAVDWS
VDAILVSFRK HFEKMVQEYV PMAHRVCSWL SQLWDKIVQW ISQASETMGW FLDGCRDLMT
WGIATLATCS ALSLVEKLLV AMGFLVEPFG LSGIFLRTGV VAAACYNYGT NSKGFAEMMA
LLSLAANCVS TVIVGGFFPG EKDNAQSSPV ILLEGLAGQM QNFCETTLVS VGKTCTAVNA
ISTCCGNLKA LAGRILGMLR DFIWKTLGFE TRFLADASLL FGEDVDGWLK AISDLRDQFI
AKSYCSQDEM MQILVLLEKG RQMRKSGLSK GGISPAIINL ILKGINDLEQ LNRSCSVQGV
RGVRKMPFTI FFQGKSRTGK SLLMSQVTKD FQDHYGLGGE TVYSRNPCDQ YWSGYRRQPF
VLMDDFAAVV TEPSAEAQMI NLISSAPYPL NMAGLEEKGI CFDSQFVFVS TNFLEVSPEA
KVRDDEAFKN RRHVIVQVSN DPAKAYDAAN FASNQIYTIL AWKDGRYNTV CVIEDYDELV
AYLLTRSQQH AEEQEKNLAN MMKSATFESH FKSLVEVLEL GSMISAGFDI IRPEKLPSEA
KEKRVLYSIP YNGEYCNALI DDNYNVTCWF GECVGNPEQL SKYSEKMLLG AYEFLLCSES
LNVVIQAHLK EMVCPHHYDK ELNFIGKIGE TYYHNQMVSN IGSMQKWHRA ILFGIGVLLG
KEKEKTWYQV QVANVKQALY DMYTKEIRDW PMPIKVTCGI VLAAIGGSAF WKVFQQLVGS
GNGPVLMGVA AGAFSAEPQS RKPNRFDMQQ YRYNNVPLKR RVWADAQMSL DQSSVAIMSK
CRANLVFGGT NLQIVMVPGR RFLACKHFFT HIKTKLRVEI VMDGRRYYHQ FDPANIYDIP
DSELVLYSHP SLEDVSHSCW DLFCWDPDKE LPSVFGADFL SCKYNKFGGF YEAQYADIKV
RTKKECLTIQ SGNYVNKVSR YLEYEAPTIP EDCGSLVIAH IGGKHKIVGV HVAGIQGKIG
CASLLPPLEP IAQAQGAEEY FDFLPAEENV SSGVAMVAGL KQGVYIPLPT KTALVETPSE
WHLDTPCDKV PSILVPTDPR IPAQHEGYDP AKSGVSKYSQ PMSALDPELL GEVANDVLEL
WHDCAVDWDD FGEVSLEEAL NGCEGVEYME RIPLATSEGF PHILSRNGKE KGKRRFVQGD
DCVVSLIPGT TVAKAYEELE ASAHRFVPAL VGIECPKDEK LPMRKVFDKP KTRCFTILPM
EYNLVVRRKF LNFVRFIMAN RHRLSCQVGI NPYSMEWSRL AARMKEKGND VLCCDYSSFD
GLLSKQVMDV IASMINELCG GEDQLKNARR NLLMACCSRL AICKNTVWRV ECGIPSGFPM
TVIVNSIFNE ILIRYHYKKL MREQQAPELM VQSFDKLIGL VTYGDDNLIS VNAVVTPYFD
GKKLKQSLAQ GGVTITDGKD KTSLELPFRR LEECDFLKRT FVQRSSTIWD APEDKASLWS
QLHYVNCNNC EKEVAYLTNV VNVLRELYMH SPREATEFRR KVLKKVSWIT SGDLPTLAQL
QEFYEYQRQQ GGADNNDTCD LLTSVDLLGP PLSFEKEAMH GCKVSEEIVT KNLAYYDFKR
KGEDEVVFLF NTLYPQSSLP DGCHSVTWSQ GSGRGGLPTQ SWMSYNISRK DSNINKIIRT
AVSSKKRVIF CARDNMVPVN IVALLCAVRN KLMPTAVSNA TLVKVMENAK AFKFLPEEFN
FAFSDV
