POL_HTL32
ID POL_HTL32 Reviewed; 1440 AA.
AC Q0R5R2;
DT 14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Gag-Pro-Pol polyprotein;
DE AltName: Full=Pr160Gag-Pro-Pol;
DE Contains:
DE RecName: Full=Matrix protein p19;
DE Short=MA;
DE Contains:
DE RecName: Full=Capsid protein p24;
DE Short=CA;
DE Contains:
DE RecName: Full=Nucleocapsid protein p15-pro;
DE Short=NC';
DE Short=NC-pro;
DE Contains:
DE RecName: Full=Protease;
DE Short=PR;
DE EC=3.4.23.-;
DE Contains:
DE RecName: Full=p1;
DE Contains:
DE RecName: Full=Reverse transcriptase/ribonuclease H;
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;
DE Short=IN;
DE EC=2.7.7.- {ECO:0000250|UniProtKB:P03363};
DE EC=3.1.-.- {ECO:0000250|UniProtKB:P03363};
GN Name=gag-pro-pol;
OS Human T-cell leukemia virus 3 (strain 2026ND) (HTLV-3).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Deltaretrovirus.
OX NCBI_TaxID=402036;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16840323; DOI=10.1128/jvi.00690-06;
RA Switzer W.M., Qari S.H., Wolfe N.D., Burke D.S., Folks T.M., Heneine W.;
RT "Ancient origin and molecular features of the novel human T-lymphotropic
RT virus type 3 revealed by complete genome analysis.";
RL J. Virol. 80:7427-7438(2006).
CC -!- FUNCTION: Matrix protein p19 targets Gag, Gag-Pro and Gag-Pro-Pol
CC polyproteins to the plasma membrane via a multipartite membrane binding
CC signal, that includes its myristoylated N-terminus. Also mediates
CC nuclear localization of the preintegration complex (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: Capsid protein p24 forms the conical core of the virus that
CC encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000250}.
CC -!- FUNCTION: Nucleocapsid protein p15 is involved in the packaging and
CC encapsidation of two copies of the genome. {ECO:0000250}.
CC -!- FUNCTION: The aspartyl protease mediates proteolytic cleavages of Gag,
CC Gag-Pro and Gag-Pro-Pol polyproteins during or shortly after the
CC release of the virion from the plasma membrane. Cleavages take place as
CC an ordered, step-wise cascade to yield mature proteins. This process is
CC called maturation. Displays maximal activity during the budding process
CC just prior to particle release from the cell. Hydrolyzes host EIF4GI in
CC order to shut off the capped cellular mRNA translation. The resulting
CC inhibition of cellular protein synthesis serves to ensure maximal viral
CC gene expression and to evade host immune response (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: Reverse transcriptase (RT) is a multifunctional enzyme that
CC converts the viral RNA genome into dsDNA in the cytoplasm, shortly
CC after virus entry into the cell. This enzyme displays a DNA polymerase
CC activity that can copy either DNA or RNA templates, and a ribonuclease
CC H (RNase H) activity that cleaves the RNA strand of RNA-DNA
CC heteroduplexes in a partially processive 3' to 5'-endonucleasic mode.
CC Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA-
CC Pro binds to the primer-binding site (PBS) situated at the 5'-end of
CC the viral RNA. RT uses the 3' end of the tRNA primer to perform a short
CC round of RNA-dependent minus-strand DNA synthesis. The reading proceeds
CC through the U5 region and ends after the repeated (R) region which is
CC present at both ends of viral RNA. The portion of the RNA-DNA
CC heteroduplex is digested by the RNase H, resulting in a ssDNA product
CC attached to the tRNA primer. This ssDNA/tRNA hybridizes with the
CC identical R region situated at the 3' end of viral RNA. This template
CC exchange, known as minus-strand DNA strong stop transfer, can be either
CC intra- or intermolecular. RT uses the 3' end of this newly synthesized
CC short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of
CC the whole template. RNase H digests the RNA template except for a
CC polypurine tract (PPT) situated at the 5' end of the genome. It is not
CC clear if both polymerase and RNase H activities are simultaneous. RNase
CC H probably can proceed both in a polymerase-dependent (RNA cut into
CC small fragments by the same RT performing DNA synthesis) and a
CC polymerase-independent mode (cleavage of remaining RNA fragments by
CC free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis
CC using the PPT that has not been removed by RNase H as primer. PPT and
CC tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS
CC regions hybridize to form a circular dsDNA intermediate. Strand
CC displacement synthesis by RT to the PBS and PPT ends produces a blunt
CC 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 catalyzes viral DNA integration into the host
CC 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.
CC This 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 dinucleotides OH's at the 3' ends. In the second step,
CC the PIC access cell chromosomes during cell division. 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 5'-ends are produced by integrase-
CC catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination
CC intermediate results, with the 5'-ends of the viral DNA strands and the
CC 3' ends of target DNA strands remaining unjoined, flanking a gap of 5
CC bp. The last step is viral DNA integration into host chromosome. This
CC involves host DNA repair synthesis in which the 5 bp gaps between the
CC unjoined strands (see above) are filled in and then ligated (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00408};
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 -!- 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 -!- SUBUNIT: Interacts with human TSG101. This interaction is essential for
CC budding and release of viral particles (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p15-pro]: Virion
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=3;
CC Comment=This strategy of translation probably allows the virus to
CC modulate the quantity of each viral protein.;
CC Name=Gag-Pol polyprotein;
CC IsoId=Q0R5R2-1; Sequence=Displayed;
CC Name=Gag-Pro polyprotein;
CC IsoId=Q0R5R3-1; Sequence=External;
CC Name=Gag polyprotein;
CC IsoId=Q0R5R4-1; Sequence=External;
CC -!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
CC essential for viral particle release. They can occur individually or in
CC close proximity within structural proteins. They interacts with sorting
CC cellular proteins of the multivesicular body (MVB) pathway. Most of
CC these proteins are class E vacuolar protein sorting factors belonging
CC to ESCRT-I, ESCRT-II or ESCRT-III complexes. Matrix protein p19
CC contains two L domains: a PTAP/PSAP motif which interacts with the UEV
CC domain of TSG101, and a PPXY motif which binds to the WW domains of
CC HECT (homologous to E6-AP C-terminus) E3 ubiquitin ligases (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The capsid protein N-terminus seems to be involved in Gag-Gag
CC interactions. {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages by the viral protease yield mature
CC proteins. The polyprotein is cleaved during and after budding, this
CC process is termed maturation. The protease is autoproteolytically
CC processed at its N- and C-termini (By similarity). {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 switching 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 (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform Gag-Pol polyprotein]: Produced by -1 ribosomal
CC frameshifting at the gag-pol genes boundary.
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DR EMBL; DQ093792; AAZ77658.1; -; Genomic_DNA.
DR SMR; Q0R5R2; -.
DR PRIDE; Q0R5R2; -.
DR Proteomes; UP000008029; Genome.
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-EC.
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:0005198; F:structural molecule activity; IEA:InterPro.
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:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.30; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR Gene3D; 2.40.70.10; -; 1.
DR Gene3D; 3.30.420.10; -; 2.
DR Gene3D; 3.30.70.270; -; 2.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR003139; D_retro_matrix.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR045345; Gag_p24_C.
DR InterPro; IPR000721; Gag_p24_N.
DR InterPro; IPR001037; Integrase_C_retrovir.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR003308; Integrase_Zn-bd_dom_N.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR018061; Retropepsins.
DR InterPro; IPR008916; Retrov_capsid_C.
DR InterPro; IPR008919; Retrov_capsid_N.
DR InterPro; IPR010999; Retrovr_matrix.
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; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF02228; Gag_p19; 1.
DR Pfam; PF00607; Gag_p24; 1.
DR Pfam; PF19317; Gag_p24_C; 1.
DR Pfam; PF00552; IN_DBD_C; 1.
DR Pfam; PF02022; Integrase_Zn; 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; 2.
DR SUPFAM; SSF47836; SSF47836; 1.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS51027; INTEGRASE_DBD; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
DR PROSITE; PS50878; RT_POL; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 3: Inferred from homology;
KW Aspartyl protease; Capsid protein; DNA integration; DNA recombination;
KW DNA-binding; Endonuclease;
KW Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host translation shutoff by virus;
KW Host gene expression shutoff by virus; Host-virus interaction; Hydrolase;
KW Lipoprotein; Magnesium; Metal-binding; Multifunctional enzyme; Myristate;
KW Nuclease; Nucleotidyltransferase; Protease; Reference proteome; Repeat;
KW Ribosomal frameshifting; RNA-directed DNA polymerase; Transferase;
KW Viral genome integration; Viral nucleoprotein; Virion;
KW Virus entry into host cell; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250"
FT CHAIN 2..1440
FT /note="Gag-Pro-Pol polyprotein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000259842"
FT CHAIN 2..123
FT /note="Matrix protein p19"
FT /evidence="ECO:0000250"
FT /id="PRO_0000259843"
FT CHAIN 124..337
FT /note="Capsid protein p24"
FT /evidence="ECO:0000250"
FT /id="PRO_0000259844"
FT CHAIN 338..430
FT /note="Nucleocapsid protein p15-pro"
FT /evidence="ECO:0000250"
FT /id="PRO_0000259845"
FT CHAIN 431..553
FT /note="Protease"
FT /evidence="ECO:0000250"
FT /id="PRO_0000259846"
FT PEPTIDE 554..561
FT /note="p1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000259847"
FT CHAIN 562..1145
FT /note="Reverse transcriptase/ribonuclease H"
FT /evidence="ECO:0000250"
FT /id="PRO_0000259848"
FT CHAIN 1146..1440
FT /note="Integrase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000259849"
FT DOMAIN 457..535
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT DOMAIN 593..783
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 1010..1143
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT DOMAIN 1197..1366
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT ZN_FING 349..366
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 372..389
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT DNA_BIND 1371..1420
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00506"
FT REGION 95..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 98..101
FT /note="PTAP/PSAP motif"
FT MOTIF 109..112
FT /note="PPXY motif"
FT ACT_SITE 462
FT /note="For protease activity; shared with dimeric partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT BINDING 659
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 734
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 735
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 1019
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for RNase H activity"
FT /evidence="ECO:0000250"
FT BINDING 1052
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for RNase H activity"
FT /evidence="ECO:0000250"
FT BINDING 1074
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for RNase H activity"
FT /evidence="ECO:0000250"
FT BINDING 1135
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for RNase H activity"
FT /evidence="ECO:0000250"
FT BINDING 1208
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 1265
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 123..124
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 337..338
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 430..431
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 553..554
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 561..562
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 1145..1146
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 1440 AA; 159835 MW; F0405D849037FB9B CRC64;
MGKTYSSPIN PIPKAPKGLA IHHWLNFLQA AYRLQPGPSE FDFHQLRKFL KLAIKTPVWL
NPINYSVLAG LIPKNYPGRV HEIVAILIQE TPAREAPPSA PLAEDPQKPP PYPEQAQEAS
QCLPILHPHG APAAHRPWQM KDLQAIKQEV SSSAPGSPQF MQTIRLAVQQ FDPTAKDLHD
LLQYLCSSLV ASLHHQQLET LIAQAETQGI TGYNPLAGPL RIQANNPNQQ GLRKEYQNLW
LSAFSALPGN TKDPTWAAIL QGPEEPFGSF VERLNVALDN GLPEGTPKDP ILRSLAYSNA
NKECQKLLQA RGQTNSPLGE MLRACQTWTP RDKNKILMVQ PKKTPPPNQP CFRCGQVGHW
SRDCKQPRPP PGPCPVCQDP THWKRDCPQL KTDTRDSEDL LLDLPCEAPN VRERKNLLRG
GGLASPRTIL PLIPLSQQKQ PTLHIQVSFS NTPPVSVQAL LDTGADITVL PACLCPPDSN
LQDTTVLGAG GPSTNKFKIL PCPVHIHLPF RRQPVTLTAC LIDINNQWTI LGRDALQQCQ
SSLYLADQPS KVLPVLAPKL IGLEHLPPPP EVSQFPLNPE RLQALTDLVS RALEAKHIEP
YQGPGNNPIF PVKKPNGKWR FIHDLRATNS VTRDLASPSP GPPDLTSLPQ GLPHLRTIDL
TDAFFQIPLP TIFQPYFAFT LPQPNNYGPG TRYSWRVLPQ GFKNSPTLFE QQLSHILTPV
RKTFPNSLII QYMDDILLAS PAPGELAALT DKVTNALTKE GLPLSPEKTQ ATPGPIHFLG
QVISQDCITY ETLPSINVKS TWSLAELQSM LGELQWVSKG TPVLRSSLHQ LYLALRGHRD
PRDTIKLTSI QVQALRTIQK ALTLNCRSRL VNQLPILALI MLRPTGTTAV LFQTKQKWPL
VWLHTPHPAT SLRPWGQLLA NAVIILDKYS LQHYGQVCKS FHHNISNQAL TYYLHTSDQS
SVAILLQHSH RFHNLGAQPS GPWRSLLQMP QIFQNIDVLR PPFTISPVVI NHAPCLFSDG
SASKAAFIIW DRQVIHQQVL SLPSTCSAQA GELFGLLAGL QKSQPWVALN IFLDSKFLIG
HLRRMALGAF PGPSTQCELH TQLLPLLQGK TVYVHHVRSH TLLQDPISRL NEATDALMLA
PLLPLDPTTL HQLTHCNPYA LRNHGATASE AHAIVQACHT CKVINPQGRL PQGYIRRGHA
PNDIWQGDVT HLQYKRYKYC LLVWVDTYSG AVSVSCRRKE TGSDCVASLL VAISILGKPQ
NINTDNGAAY LSQEFQQFCN SLAIKHSTHI PYNPTSSGLV ERTNGILKTL ISKYLLDNHH
LPLETAVSKS LWTINHLNVL PSCQKTRWQL HQAQPLPPVP EDTLPPHTSP KWYYYKIPGL
TNSRWSGPVQ SLKEAAGAAL IPVGGSYLWI PWRLLKRGIC PRPESSAAVD PKTRDHQLHG
