POL_WDSV
ID POL_WDSV Reviewed; 1752 AA.
AC O92815;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Gag-Pol polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p10;
DE Short=MA;
DE Contains:
DE RecName: Full=p20;
DE Contains:
DE RecName: Full=Capsid protein p25;
DE Short=CA;
DE Contains:
DE RecName: Full=Nucleocapsid protein p14;
DE Short=NC-pol;
DE Contains:
DE RecName: Full=Protease p15;
DE Short=PR;
DE EC=3.4.23.-;
DE Contains:
DE RecName: Full=Reverse transcriptase/ribonuclease H p90;
DE Short=RT;
DE EC=2.7.7.49;
DE EC=2.7.7.7;
DE EC=3.1.26.4;
DE Contains:
DE RecName: Full=Integrase p46;
DE Short=IN;
DE EC=2.7.7.- {ECO:0000305|PubMed:24124581};
DE EC=3.1.-.- {ECO:0000305|PubMed:24124581};
GN Name=gag-pol;
OS Walleye dermal sarcoma virus (WDSV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Epsilonretrovirus.
OX NCBI_TaxID=39720;
OH NCBI_TaxID=283036; Sander vitreus (Walleye) (Perca vitrea).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], PROTEIN SEQUENCE OF 96-105; 252-266 AND
RP 458-467, AND PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX PubMed=7636975; DOI=10.1128/jvi.69.9.5320-5331.1995;
RA Holzschu D.L., Martineau D., Fodor S.K., Vogt V.M., Bowser P.R.,
RA Casey J.W.;
RT "Nucleotide sequence and protein analysis of a complex piscine retrovirus,
RT walleye dermal sarcoma virus.";
RL J. Virol. 69:5320-5331(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Chappey C.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 585-589, CHARACTERIZATION OF PROTEASE P15, AND
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX PubMed=11932400; DOI=10.1128/jvi.76.9.4341-4349.2002;
RA Fodor S.K., Vogt V.M.;
RT "Characterization of the protease of a fish retrovirus, walleye dermal
RT sarcoma virus.";
RL J. Virol. 76:4341-4349(2002).
RN [4]
RP FUNCTION (INTEGRASE).
RX PubMed=24124581; DOI=10.1371/journal.pone.0076638;
RA Ballandras-Colas A., Naraharisetty H., Li X., Serrao E., Engelman A.;
RT "Biochemical characterization of novel retroviral integrase proteins.";
RL PLoS ONE 8:E76638-E76638(2013).
CC -!- FUNCTION: [Matrix protein p10]: Targets Gag and gag-pol polyproteins to
CC the plasma membrane via a multipartite membrane binding signal, that
CC includes its myristoylated N-terminus. Also mediates nuclear
CC localization of the preintegration complex (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: Capsid protein p25 forms the spherical core of the virion
CC that encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000250}.
CC -!- FUNCTION: [Nucleocapsid protein p14]: Involved in the packaging and
CC encapsidation of two copies of the genome. Binds with high affinity to
CC conserved UCUG elements within the packaging signal, located near the
CC 5'-end of the genome. This binding is dependent on genome dimerization
CC (By similarity). {ECO:0000250}.
CC -!- FUNCTION: [Protease p15]: Mediates proteolytic cleavages of Gag and
CC Gag-Pol polyproteins during or shortly after the release of the virion
CC from the plasma membrane. Cleavages take place as an ordered, step-wise
CC cascade to yield mature proteins. This process is called maturation.
CC Displays maximal activity during the budding process just prior to
CC particle release from the cell (By similarity). {ECO:0000250}.
CC -!- FUNCTION: [Reverse transcriptase/ribonuclease H p90]: Is a
CC multifunctional enzyme that converts the viral dimeric RNA genome into
CC dsDNA in the cytoplasm, shortly after virus entry into the cell. This
CC enzyme displays a DNA polymerase activity that can copy either DNA or
CC RNA templates, and a ribonuclease H (RNase H) activity that cleaves the
CC RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5'
CC endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires
CC many steps. A tRNA binds to the primer-binding site (PBS) situated at
CC the 5' end of the viral RNA. RT uses the 3' end of the tRNA primer to
CC perform a short round of RNA-dependent minus-strand DNA synthesis. The
CC reading proceeds through the U5 region and ends after the repeated (R)
CC region which is present at both ends of viral RNA. The portion of the
CC RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA
CC product attached to the tRNA primer. This ssDNA/tRNA hybridizes with
CC the identical R region situated at the 3' end of viral RNA. This
CC template exchange, known as minus-strand DNA strong stop transfer, can
CC be either intra- or intermolecular. RT uses the 3' end of this newly
CC synthesized short ssDNA to perform the RNA-dependent minus-strand DNA
CC synthesis of the whole template. RNase H digests the RNA template
CC except for a polypurine tract (PPT) situated at the 5' end of the
CC genome. It is not clear if both polymerase and RNase H activities are
CC simultaneous. RNase H probably can proceed both in a polymerase-
CC dependent (RNA cut into small fragments by the same RT performing DNA
CC synthesis) and a polymerase-independent mode (cleavage of remaining RNA
CC fragments by free RTs). Secondly, RT performs DNA-directed plus-strand
CC DNA synthesis using the PPT that has not been removed by RNase H as
CC primers. PPT and tRNA primers are then removed by RNase H. The 3' and
CC 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate.
CC Strand displacement synthesis by RT to the PBS and PPT ends produces a
CC blunt ended, linear dsDNA copy of the viral genome that includes long
CC terminal repeats (LTRs) at both ends (By similarity). {ECO:0000250}.
CC -!- FUNCTION: [Integrase p46]: Catalyzes viral DNA integration into the
CC host chromosome, by performing a series of DNA cutting and joining
CC reactions. This enzyme activity takes place after virion entry into a
CC cell and reverse transcription of the RNA genome in dsDNA. The first
CC step in the integration process is 3' processing. This step requires a
CC complex comprising the viral genome, matrix protein and integrase. This
CC complex is called the pre-integration complex (PIC). The integrase
CC protein removes 2 nucleotides from each 3' end of the viral DNA,
CC leaving recessed CA OH's at the 3' ends. In the second step that
CC requires cell division, the PIC enters cell nucleus. In the third step,
CC termed strand transfer, the integrase protein joins the previously
CC processed 3' ends to the 5' ends of strands of target cellular DNA at
CC the site of integration. The last step is viral DNA integration into
CC host chromosome. {ECO:0000269|PubMed:24124581}.
CC -!- FUNCTION: [Gag-Pol polyprotein]: Plays a role in budding and is
CC processed by the viral protease during virion maturation outside the
CC cell. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00408};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions for reverse transcriptase polymerase
CC activity. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity.
CC {ECO:0000250};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Magnesium ions are required for integrase activity. Binds at least
CC 1, maybe 2 magnesium ions. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0 for protease p14.;
CC -!- SUBUNIT: Capsid protein p25 is a homohexamer, that further associates
CC as homomultimer. The virus core is composed of a lattice formed from
CC hexagonal rings, each containing six capsid monomers. The protease is a
CC homodimer, whose active site consists of two apposed aspartic acid
CC residues. The reverse transcriptase is a monomer (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane
CC {ECO:0000305}; Lipid-anchor {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p25]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p14]: Virion {ECO:0000305}.
CC -!- PTM: Specific enzymatic cleavages by the viral protease yield mature
CC proteins. The protease is released by autocatalytic cleavage. The
CC polyprotein is cleaved during and after budding, this process is termed
CC maturation (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: This protein is translated as a gag-pol fusion protein
CC by episodic readthrough of the gag protein termination codon.
CC Readthrough of the terminator codon TAG occurs between the codons for
CC 582-Ala and 584-Asp (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: The nucleocapsid protein p14 released from Pol
CC polyprotein (NC-pol) is a few amino acids longer than the nucleocapsid
CC protein p14 released from Gag polyprotein (NC-gag). {ECO:0000250}.
CC -!- MISCELLANEOUS: The reverse transcriptase is an error-prone enzyme that
CC lacks a proof-reading function. High mutations rate is a direct
CC consequence of this characteristic. RT also displays frequent template
CC swiching leading to high recombination rate. Recombination mostly
CC occurs between homologous regions of the two copackaged RNA genomes. If
CC these two RNA molecules derive from different viral strains, reverse
CC transcription will give rise to highly recombinated proviral DNAs.
CC {ECO:0000255|PROSITE-ProRule:PRU00405}.
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DR EMBL; L41838; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AF033822; AAC82611.1; -; Genomic_RNA.
DR PIR; T09394; T09394.
DR RefSeq; NP_045937.2; NC_001867.1.
DR MEROPS; A02.063; -.
DR GeneID; 1403495; -.
DR Proteomes; UP000007081; Genome.
DR Proteomes; UP000008337; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; -; 1.
DR Gene3D; 3.30.420.10; -; 2.
DR Gene3D; 3.30.70.270; -; 2.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR040643; MLVIN_C.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR018061; Retropepsins.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR041577; RT_RNaseH_2.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF18697; MLVIN_C; 1.
DR Pfam; PF00075; RNase_H; 1.
DR Pfam; PF17919; RT_RNaseH_2; 1.
DR Pfam; PF00665; rve; 1.
DR Pfam; PF00077; RVP; 1.
DR Pfam; PF00078; RVT_1; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR SUPFAM; SSF53098; SSF53098; 2.
DR SUPFAM; SSF56672; SSF56672; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
DR PROSITE; PS50878; RT_POL; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Capsid protein; Coiled coil; Direct protein sequencing;
KW DNA integration; DNA recombination; DNA-binding;
KW DNA-directed DNA polymerase; Endonuclease; Host cell membrane;
KW Host membrane; Hydrolase; Lipoprotein; Magnesium; Membrane; Metal-binding;
KW Multifunctional enzyme; Myristate; Nuclease; Nucleotidyltransferase;
KW Phosphoprotein; Protease; Reference proteome;
KW RNA suppression of termination; RNA-binding; RNA-directed DNA polymerase;
KW Transferase; Viral matrix protein; Viral nucleoprotein; Virion; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..1752
FT /note="Gag-Pol polyprotein"
FT /id="PRO_0000410592"
FT CHAIN 2..95
FT /note="Matrix protein p10"
FT /id="PRO_0000410593"
FT CHAIN 96..251
FT /note="p20"
FT /id="PRO_0000410594"
FT CHAIN 252..457
FT /note="Capsid protein p25"
FT /id="PRO_0000410595"
FT CHAIN 458..584
FT /note="Nucleocapsid protein p14"
FT /id="PRO_0000410596"
FT CHAIN 585..722
FT /note="Protease p15"
FT /id="PRO_0000410597"
FT CHAIN 723..1372
FT /note="Reverse transcriptase/ribonuclease H p90"
FT /evidence="ECO:0000250"
FT /id="PRO_0000410598"
FT CHAIN 1373..1752
FT /note="Integrase p46"
FT /evidence="ECO:0000250"
FT /id="PRO_0000410599"
FT DOMAIN 618..694
FT /note="Peptidase A2"
FT DOMAIN 793..977
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 1222..1368
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT DOMAIN 1482..1638
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT ZN_FING 501..518
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 171..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 154..185
FT /evidence="ECO:0000255"
FT COMPBIAS 171..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 623
FT /note="Protease; shared with dimeric partner"
FT /evidence="ECO:0000250"
FT BINDING 861
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for reverse transcriptase
FT activity"
FT /evidence="ECO:0000250"
FT BINDING 928
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for reverse transcriptase
FT activity"
FT /evidence="ECO:0000250"
FT BINDING 929
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for reverse transcriptase
FT activity"
FT /evidence="ECO:0000250"
FT BINDING 1231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="for RNase H activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 1269
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="for RNase H activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 1290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="for RNase H activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 1360
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="for RNase H activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 1493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /ligand_note="catalytic; for integrase activity"
FT /evidence="ECO:0000250"
FT BINDING 1550
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /ligand_note="catalytic; for integrase activity"
FT /evidence="ECO:0000250"
FT SITE 95..96
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 251..252
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 457..458
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 584..585
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 722..723
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 1372..1373
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1752 AA; 196265 MW; A9DEF76316FBE4E0 CRC64;
MGNSSSTPPP SALKNSDLFK TMLRTQYSGS VKTRRINQDI KKQYPLWPDQ GTCATKHWEQ
AVLIPLDSVS EETAKVLNFL RVKIQARKGE TARQMTAHTI KKLIVGTIDK NKQQTEILQK
TDESDEEMDT TNTMLFIARN KRERIAQQQQ ADLAAQQQVL LLQREQQREQ REKDIKKRDE
KKKKLLPDTT QKVEQTDIGE ASSSDASAQK PISTDNNPDL KVDGVLTRSQ HTTVPSNITI
KKDGTSVQYQ HPIRNYPTGE GNLTAQVRNP FRPLELQQLR KDCPALPEGI PQLAEWLTQT
MAIYNCDEAD VEQLARVIFP TPVRQIAGVI NGHAAANTAA KIQNYVTACR QHYPAVCDWG
TIQAFTYKPP QTAHEYVKHA EIIFKNNSGL EWQHATVPFI NMVVQGLPPK VTRSLMSGNP
DWSTKTIPQI IPLMQHYLNL QSRQDAKIKQ TPLVLQLAMP AQTMNGNKGY VGSYPTNEPY
YSFQQQQRPA PRAPPGNVPS NTCFFCKQPG HWKADCPNKT RNLRNMGNMG RGGRMGGPPY
RSQPYPAFIQ PPQNHQNQYN GRMDRSQLQA SAQEWLPGTY PAXDPIDCPY EKSGTKTTQD
VITTKNAEIM VTVNHTKIPM LVDTGACLTA IGGAATVVPD LKLTNTEIIA VGISAEPVPH
VLAKPTKIQI ENTNIDISPW YNPDQTFHIL GRDTLSKMRA IVSFEKNGEM TVLLPPTYHK
QLSCQTKNTL NIDEYLLQFP DQLWASLPTD IGRMLVPPIT IKIKDNASLP SIRQYPLPKD
KTEGLRPLIS SLENQGILIK CHSPCNTPIF PIKKAGRDEY RMIHDLRAIN NIVAPLTAVV
ASPTTVLSNL APSLHWFTVI DLSNAFFSVP IHKDSQYLFA FTFEGHQYTW TVLPQGFIHS
PTLFSQALYQ SLHKIKFKIS SEICIYMDDV LIASKDRDTN LKDTAVMLQH LASEGHKVSK
KKLQLCQQEV VYLGQLLTPE GRKILPDRKV TVSQFQQPTT IRQIRAFLGL VGYCRHWIPE
FSIHSKFLEK QLKKDTAEPF QLDDQQVEAF NKLKHAITTA PVLVVPDPAK PFQLYTSHSE
HASIAVLTQK HAGRTRPIAF LSSKFDAIES GLPPCLKACA SIHRSLTQAD SFILGAPLII
YTTHAICTLL QRDRSQLVTA SRFSKWEADL LRPELTFVAC SAVSPAHLYM QSCENNIPPH
DCVLLTHTIS RPRPDLSDLP IPDPDMTLFS DGSYTTGRGG AAVVMHRPVT DDFIIIHQQP
GGASAQTAEL LALAAACHLA TDKTVNIYTD SRYAYGVVHD FGHLWMHRGF VTSAGTPIKN
HKEIEYLLKQ IMKPKQVSVI KIEAHTKGVS MEVRGNAAAD EAAKNAVFLV QRVLKKGDAL
ASTDLVMEYS ETDEKFTAGA ELHDGVFMRG DLIVPPLEML HAILLAIHGV SHTHKGGIMS
YFSKFWTHPK ASQTIDLILG HCQICLKHNP KYKSRLQGHR PLPSRPFAHL QIDFVQMCVK
KPMYALVIID VFSKWPEIIP CNKEDAKTVC DILMKDIIPR WGLPDQIDSD QGTHFTAKIS
QELTHSIGVA WKLHCPGHPR SSGIVERTNR TLKSKIIKAQ EQLQLSKWTE VLPYVLLEMR
ATPKKHGLSP HEIVMGRPMK TTYLSDMSPL WATDTLVTYM NKLTRQLSAY HQQVVDQWPS
TSLPPGPEPG SWCMLRNPKK SSNWEGPFLI LLSTPTAVKV EGRPTWIHLD HCKLLRSSLS
SSLGGPVNQL LS
