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Gag-Pro-Pol polyprotein (Pr160Gag-Pro-Pol) [Cleaved into: Matrix protein p19 (MA); Capsid protein p24 (CA); Nucleocapsid protein p15-pro (NC') (NC-pro); Protease (PR) (EC 3.4.23.-); p1; Reverse transcriptase/ribonuclease H (RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]

 POL_HTL1A               Reviewed;        1462 AA.
P03362; Q85590;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 141.
RecName: Full=Gag-Pro-Pol polyprotein;
AltName: Full=Pr160Gag-Pro-Pol;
Contains:
RecName: Full=Matrix protein p19;
Short=MA;
Contains:
RecName: Full=Capsid protein p24;
Short=CA;
Contains:
RecName: Full=Nucleocapsid protein p15-pro;
Short=NC';
Short=NC-pro;
Contains:
RecName: Full=Protease;
Short=PR;
EC=3.4.23.-;
Contains:
RecName: Full=p1;
Contains:
RecName: Full=Reverse transcriptase/ribonuclease H;
Short=RT;
EC=2.7.7.49;
EC=2.7.7.7;
EC=3.1.26.4;
Contains:
RecName: Full=Integrase;
Short=IN;
EC=2.7.7.- {ECO:0000250|UniProtKB:P03363};
EC=3.1.-.- {ECO:0000250|UniProtKB:P03363};
Name=gag-pro-pol;
Human T-cell leukemia virus 1 (strain Japan ATK-1 subtype A) (HTLV-1).
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Deltaretrovirus.
NCBI_TaxID=11926;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6304725; DOI=10.1073/pnas.80.12.3618;
Seiki M., Hattori S., Hirayama Y., Yoshida M.C.;
"Human adult T-cell leukemia virus: complete nucleotide sequence of
the provirus genome integrated in leukemia cell DNA.";
Proc. Natl. Acad. Sci. U.S.A. 80:3618-3622(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 395-672.
PubMed=3021121; DOI=10.1016/S0006-291X(86)80089-4;
Nam S.H., Hatanaka M.;
"Identification of a protease gene of human T-cell leukemia virus type
I (HTLV-I) and its structural comparison.";
Biochem. Biophys. Res. Commun. 139:129-135(1986).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 635-751.
PubMed=2468487;
Bangham C.R.M., Daenke S., Philips R.E., Cruickshank J.K., Bell J.I.;
"Enzymatic amplification of exogenous and endogenous retroviral
sequences from DNA of patients with tropical spastic paraparesis.";
EMBO J. 7:4179-4184(1988).
[4]
PROTEIN SEQUENCE OF 131-155.
PubMed=6280175; DOI=10.1073/pnas.79.4.1291;
Oroszlan S., Sarngadharan M.G., Copeland T.D., Kalyanaraman V.S.,
Gilden R.V., Gallo R.C.;
"Primary structure analysis of the major internal protein p24 of human
type C T-cell leukemia virus.";
Proc. Natl. Acad. Sci. U.S.A. 79:1291-1294(1982).
[5]
PROTEIN SEQUENCE OF 545-611, AND PROTEOLYTIC PROCESSING OF
POLYPROTEIN.
PubMed=11469799; DOI=10.1006/abbi.2001.2432;
Agbuya P.G., Sherman N.E., Moen L.K.;
"Proteolytic processing of the human T-cell lymphotropic virus 1
reverse transcriptase: identification of the N-terminal cleavage site
by mass spectrometry.";
Arch. Biochem. Biophys. 392:93-102(2001).
[6]
PROTEIN SEQUENCE OF 596-612, AND RIBOSOMAL FRAMESHIFT.
PubMed=8416368;
Nam S.H., Copeland T.D., Hatanaka M., Oroszlan S.;
"Characterization of ribosomal frameshifting for expression of pol
gene products of human T-cell leukemia virus type I.";
J. Virol. 67:196-203(1993).
[7]
PROTEIN SEQUENCE OF 583-590, PROTEOLYTIC PROCESSING OF POLYPROTEIN,
AND MUTAGENESIS OF 573-ILE--PRO-575 AND 581-VAL--LEU-584.
PubMed=12438640; DOI=10.1128/JVI.76.24.13101-13105.2002;
Heidecker G., Hill S., Lloyd P.A., Derse D.;
"A novel protease processing site in the transframe protein of human
T-cell leukemia virus type 1 PR76(gag-pro) defines the N terminus of
RT.";
J. Virol. 76:13101-13105(2002).
[8]
FUNCTION OF PROTEASE.
PubMed=2843670;
Nam S.H., Kidokoro M., Shida H., Hatanaka M.;
"Processing of gag precursor polyprotein of human T-cell leukemia
virus type I by virus-encoded protease.";
J. Virol. 62:3718-3728(1988).
[9]
CHARACTERIZATION OF PROTEASE.
PubMed=10037763; DOI=10.1074/jbc.274.10.6660;
Louis J.M., Oroszlan S., Toezser J.;
"Stabilization from autoproteolysis and kinetic characterization of
the human T-cell leukemia virus type 1 proteinase.";
J. Biol. Chem. 274:6660-6666(1999).
[10]
CHARACTERIZATION OF CAPSID PROTEIN P24.
PubMed=11333909; DOI=10.1128/JVI.75.11.5277-5287.2001;
Rayne F., Bouamr F., Lalanne J., Mamoun R.Z.;
"The NH2-terminal domain of the human T-cell leukemia virus type 1
capsid protein is involved in particle formation.";
J. Virol. 75:5277-5287(2001).
[11]
PROTEOLYTIC PROCESSING OF POLYPROTEIN.
PubMed=12504078; DOI=10.1016/S0006-291X(02)02848-6;
Mariani V.L., Shuker S.B.;
"Identification of the RT-RH/IN cleavage site of HTLV-I.";
Biochem. Biophys. Res. Commun. 300:268-270(2003).
[12]
CHARACTERIZATION OF PROTEASE.
PubMed=15102858; DOI=10.1074/jbc.M401868200;
Kadas J., Weber I.T., Bagossi P., Miklossy G., Boross P., Oroszlan S.,
Toezser J.;
"Narrow substrate specificity and sensitivity toward ligand-binding
site mutations of human T-cell Leukemia virus type 1 protease.";
J. Biol. Chem. 279:27148-27157(2004).
-!- FUNCTION: Matrix protein p19 targets Gag, Gag-Pro and Gag-Pro-Pol
polyproteins to the plasma membrane via a multipartite membrane
binding signal, that includes its myristoylated N-terminus. Also
mediates nuclear localization of the preintegration complex (By
similarity). {ECO:0000250}.
-!- FUNCTION: Capsid protein p24 forms the conical core of the virus
that encapsulates the genomic RNA-nucleocapsid complex.
{ECO:0000250}.
-!- FUNCTION: Nucleocapsid protein p15 is involved in the packaging
and encapsidation of two copies of the genome. {ECO:0000250}.
-!- FUNCTION: The aspartyl protease mediates proteolytic cleavages of
Gag, Gag-Pro and Gag-Pro-Pol polyproteins during or shortly after
the release of the virion from the plasma membrane. Cleavages take
place as an ordered, step-wise cascade to yield mature proteins.
This process is called maturation. Displays maximal activity
during the budding process just prior to particle release from the
cell. Hydrolyzes host EIF4GI in order to shut off the capped
cellular mRNA translation. The resulting inhibition of cellular
protein synthesis serves to ensure maximal viral gene expression
and to evade host immune response (By similarity). {ECO:0000250}.
-!- FUNCTION: Reverse transcriptase (RT) is a multifunctional enzyme
that converts the viral RNA genome into dsDNA in the cytoplasm,
shortly after virus entry into the cell. This enzyme displays a
DNA polymerase activity that can copy either DNA or RNA templates,
and a ribonuclease H (RNase H) activity that cleaves the RNA
strand of RNA-DNA heteroduplexes in a partially processive 3' to
5'-endonucleasic mode. Conversion of viral genomic RNA into dsDNA
requires many steps. A tRNA-Pro binds to the primer-binding site
(PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end
of the tRNA primer to perform a short round of RNA-dependent
minus-strand DNA synthesis. The reading proceeds through the U5
region and ends after the repeated (R) region which is present at
both ends of viral RNA. The portion of the RNA-DNA heteroduplex is
digested by the RNase H, resulting in a ssDNA product attached to
the tRNA primer. This ssDNA/tRNA hybridizes with the identical R
region situated at the 3' end of viral RNA. This template
exchange, known as minus-strand DNA strong stop transfer, can be
either intra- or intermolecular. RT uses the 3' end of this newly
synthesized short ssDNA to perform the RNA-dependent minus-strand
DNA synthesis of the whole template. RNase H digests the RNA
template except for a polypurine tract (PPT) situated at the 5'
end of the genome. It is not clear if both polymerase and RNase H
activities are simultaneous. RNase H probably can proceed both in
a polymerase-dependent (RNA cut into small fragments by the same
RT performing DNA synthesis) and a polymerase-independent mode
(cleavage of remaining RNA fragments by free RTs). Secondly, RT
performs DNA-directed plus-strand DNA synthesis using the PPT that
has not been removed by RNase H as primer. PPT and tRNA primers
are then removed by RNase H. The 3' and 5' ssDNA PBS regions
hybridize to form a circular dsDNA intermediate. Strand
displacement synthesis by RT to the PBS and PPT ends produces a
blunt ended, linear dsDNA copy of the viral genome that includes
long terminal repeats (LTRs) at both ends (By similarity).
{ECO:0000250}.
-!- FUNCTION: Integrase catalyzes viral DNA integration into the host
chromosome, by performing a series of DNA cutting and joining
reactions. This enzyme activity takes place after virion entry
into a cell and reverse transcription of the RNA genome in dsDNA.
The first step in the integration process is 3' processing. This
step requires a complex comprising the viral genome, matrix
protein, and integrase. This complex is called the pre-integration
complex (PIC). The integrase protein removes 2 nucleotides from
each 3' end of the viral DNA, leaving recessed dinucleotides OH's
at the 3' ends. In the second step, the PIC access cell
chromosomes during cell division. The third step, termed strand
transfer, the integrase protein joins the previously processed 3'
ends to the 5'-ends of strands of target cellular DNA at the site
of integration. The 5'-ends are produced by integrase-catalyzed
staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination
intermediate results, with the 5'-ends of the viral DNA strands
and the 3' ends of target DNA strands remaining unjoined, flanking
a gap of 5 bp. The last step is viral DNA integration into host
chromosome. This involves host DNA repair synthesis in which the 5
bp gaps between the unjoined strands (see above) are filled in and
then ligated (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
phosphomonoester. {ECO:0000255|PROSITE-ProRule:PRU00408}.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00405}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 2 magnesium ions for reverse transcriptase polymerase
activity. {ECO:0000250};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity.
{ECO:0000250};
-!- SUBUNIT: Interacts with human TSG101 and NEDD4. These interactions
are essential for budding and release of viral particles (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Matrix protein p19: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Capsid protein p24: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Nucleocapsid protein p15-pro: Virion
{ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=3;
Comment=This strategy of translation probably allows the virus
to modulate the quantity of each viral protein.;
Name=Gag-Pro-Pol polyprotein;
IsoId=P03362-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting at the gag-pro and
gag-pol genes boundaries.;
Name=Gag-Pro polyprotein;
IsoId=P10274-1; Sequence=External;
Note=Produced by -1 ribosomal frameshifting at the gag-pro genes
boundary.;
Name=Gag polyprotein;
IsoId=P03345-1; Sequence=External;
Note=Produced by conventional translation.;
-!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
essential for viral particle release. They can occur individually
or in close proximity within structural proteins. They interacts
with sorting cellular proteins of the multivesicular body (MVB)
pathway. Most of these proteins are class E vacuolar protein
sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III
complexes. Matrix protein p19 contains two L domains: a PTAP/PSAP
motif which interacts with the UEV domain of TSG101, and a PPXY
motif which binds to the WW domains of HECT (homologous to E6-AP
C-terminus) E3 ubiquitin ligases, like NEDD4 (By similarity).
{ECO:0000250}.
-!- DOMAIN: The capsid protein N-terminus seems to be involved in Gag-
Gag interactions. {ECO:0000250}.
-!- PTM: Specific enzymatic cleavages by the viral protease yield
mature proteins. The polyprotein is cleaved during and after
budding, this process is termed maturation. The protease is
autoproteolytically processed at its N- and C-termini.
{ECO:0000269|PubMed:11469799, ECO:0000269|PubMed:12438640,
ECO:0000269|PubMed:12504078}.
-!- PTM: Phosphorylation of the matrix protein p19 by MAPK1 seems to
play a role in budding. {ECO:0000250}.
-!- MISCELLANEOUS: The reverse transcriptase is an error-prone enzyme
that lacks a proof-reading function. High mutations rate is a
direct consequence of this characteristic. RT also displays
frequent template switching leading to high recombination rate.
Recombination mostly occurs between homologous regions of the two
copackaged RNA genomes. If these two RNA molecules derive from
different viral strains, reverse transcription will give rise to
highly recombinated proviral DNAs (By similarity). {ECO:0000250}.
-!- MISCELLANEOUS: HTLV-1 lineages are divided in four clades, A
(Cosmopolitan), B (Central African group), C (Melanesian group)
and D (New Central African group).
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EMBL; J02029; AAA96673.1; ALT_SEQ; Genomic_DNA.
EMBL; M13810; AAA46207.1; ALT_SEQ; Genomic_RNA.
EMBL; X14144; CAA32360.1; -; Genomic_DNA.
PIR; A03961; GNLJGH.
PDB; 1O0J; Model; -; A/B=450-564.
PDB; 1TP1; Model; -; A/B=450-564.
PDB; 2B7F; X-ray; 2.60 A; A/B/C/D/E/F=450-565.
PDB; 4YDG; X-ray; 3.25 A; A/B=450-565.
PDBsum; 1O0J; -.
PDBsum; 1TP1; -.
PDBsum; 2B7F; -.
PDBsum; 4YDG; -.
ProteinModelPortal; P03362; -.
SMR; P03362; -.
PRIDE; P03362; -.
OrthoDB; VOG09000057; -.
BRENDA; 3.4.23.B8; 2706.
EvolutionaryTrace; P03362; -.
Proteomes; UP000007683; Genome.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
Gene3D; 1.10.1200.30; -; 1.
Gene3D; 1.10.185.10; -; 1.
Gene3D; 1.10.375.10; -; 1.
Gene3D; 2.40.70.10; -; 1.
Gene3D; 3.30.420.10; -; 2.
Gene3D; 4.10.60.10; -; 2.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR003139; D_retro_matrix.
InterPro; IPR036989; D_retro_matrix_sf.
InterPro; IPR000721; Gag_p24.
InterPro; IPR036862; Integrase_C_dom_sf_retrovir.
InterPro; IPR001037; Integrase_C_retrovir.
InterPro; IPR001584; Integrase_cat-core.
InterPro; IPR003308; Integrase_Zn-bd_dom_N.
InterPro; IPR001995; Peptidase_A2_cat.
InterPro; IPR021109; Peptidase_aspartic_dom_sf.
InterPro; IPR018061; Retropepsins.
InterPro; IPR008916; Retrov_capsid_C.
InterPro; IPR008919; Retrov_capsid_N.
InterPro; IPR010999; Retrovr_matrix.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR002156; RNaseH_domain.
InterPro; IPR036397; RNaseH_sf.
InterPro; IPR000477; RT_dom.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
Pfam; PF02228; Gag_p19; 1.
Pfam; PF00607; Gag_p24; 1.
Pfam; PF00552; IN_DBD_C; 1.
Pfam; PF02022; Integrase_Zn; 1.
Pfam; PF00075; RNase_H; 1.
Pfam; PF00665; rve; 1.
Pfam; PF00077; RVP; 1.
Pfam; PF00078; RVT_1; 1.
Pfam; PF00098; zf-CCHC; 1.
SMART; SM00343; ZnF_C2HC; 2.
SUPFAM; SSF47353; SSF47353; 1.
SUPFAM; SSF47836; SSF47836; 1.
SUPFAM; SSF47943; SSF47943; 1.
SUPFAM; SSF50122; SSF50122; 1.
SUPFAM; SSF50630; SSF50630; 1.
SUPFAM; SSF53098; SSF53098; 1.
SUPFAM; SSF57756; SSF57756; 1.
PROSITE; PS50175; ASP_PROT_RETROV; 1.
PROSITE; PS00141; ASP_PROTEASE; 1.
PROSITE; PS50994; INTEGRASE; 1.
PROSITE; PS51027; INTEGRASE_DBD; 1.
PROSITE; PS50879; RNASE_H; 1.
PROSITE; PS50878; RT_POL; 1.
PROSITE; PS50158; ZF_CCHC; 1.
1: Evidence at protein level;
3D-structure; Aspartyl protease; Capsid protein; Complete proteome;
Direct protein sequencing; DNA integration; DNA recombination;
DNA-binding; Endonuclease;
Eukaryotic host gene expression shutoff by virus;
Eukaryotic host translation shutoff by virus;
Host gene expression shutoff by virus; Host-virus interaction;
Hydrolase; Lipoprotein; Magnesium; Metal-binding;
Multifunctional enzyme; Myristate; Nuclease; Nucleotidyltransferase;
Phosphoprotein; Protease; Repeat; Ribosomal frameshifting;
RNA-directed DNA polymerase; Transferase; Viral genome integration;
Viral nucleoprotein; Virion; Virus entry into host cell; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed; by host. {ECO:0000250}.
CHAIN 2 1462 Gag-Pro-Pol polyprotein.
/FTId=PRO_0000259828.
CHAIN 2 130 Matrix protein p19. {ECO:0000250}.
/FTId=PRO_0000259829.
CHAIN 131 344 Capsid protein p24. {ECO:0000250}.
/FTId=PRO_0000259830.
CHAIN 345 449 Nucleocapsid protein p15-pro.
{ECO:0000250}.
/FTId=PRO_0000259831.
CHAIN 450 574 Protease. {ECO:0000250}.
/FTId=PRO_0000259832.
PEPTIDE 575 582 p1. {ECO:0000269|PubMed:12438640}.
/FTId=PRO_0000259833.
CHAIN 583 1167 Reverse transcriptase/ribonuclease H.
{ECO:0000250}.
/FTId=PRO_0000038873.
CHAIN 1168 1462 Integrase. {ECO:0000250}.
/FTId=PRO_0000038874.
DOMAIN 476 554 Peptidase A2. {ECO:0000255|PROSITE-
ProRule:PRU00275}.
DOMAIN 614 804 Reverse transcriptase.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
DOMAIN 1031 1165 RNase H. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
DOMAIN 1219 1388 Integrase catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00457}.
ZN_FING 355 372 CCHC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 378 395 CCHC-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
DNA_BIND 1393 1443 Integrase-type. {ECO:0000255|PROSITE-
ProRule:PRU00506}.
MOTIF 118 121 PPXY motif.
MOTIF 124 127 PTAP/PSAP motif.
COMPBIAS 95 144 Pro-rich.
COMPBIAS 657 660 Poly-Ser.
ACT_SITE 481 481 For protease activity; shared with
dimeric partner. {ECO:0000255|PROSITE-
ProRule:PRU10094}.
METAL 680 680 Magnesium; catalytic; for reverse
transcriptase activity. {ECO:0000250}.
METAL 755 755 Magnesium; catalytic; for reverse
transcriptase activity. {ECO:0000250}.
METAL 756 756 Magnesium; catalytic; for reverse
transcriptase activity. {ECO:0000250}.
METAL 1040 1040 Magnesium; catalytic; for RNase H
activity. {ECO:0000250}.
METAL 1074 1074 Magnesium; catalytic; for RNase H
activity. {ECO:0000250}.
METAL 1096 1096 Magnesium; catalytic; for RNase H
activity. {ECO:0000250}.
METAL 1157 1157 Magnesium; catalytic; for RNase H
activity. {ECO:0000250}.
METAL 1230 1230 Magnesium; catalytic; for integrase
activity. {ECO:0000250}.
METAL 1287 1287 Magnesium; catalytic; for integrase
activity. {ECO:0000250}.
SITE 130 131 Cleavage; by viral protease.
{ECO:0000250}.
SITE 344 345 Cleavage; by viral protease.
{ECO:0000250}.
SITE 449 450 Cleavage; by viral protease.
{ECO:0000250}.
SITE 574 575 Cleavage; by viral protease.
{ECO:0000250}.
SITE 582 583 Cleavage; by viral protease.
SITE 1167 1168 Cleavage; by viral protease.
MOD_RES 105 105 Phosphoserine; by host MAPK1.
{ECO:0000250}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000250}.
VARIANT 440 441 LP -> FL.
VARIANT 569 569 R -> G.
VARIANT 621 621 P -> S.
MUTAGEN 573 575 ILP->TAG: Complete loss of cleavage
between protease and p1.
{ECO:0000269|PubMed:12438640}.
MUTAGEN 581 584 VLGL->GAGA: Complete loss of cleavage
between p1 and RT.
{ECO:0000269|PubMed:12438640}.
CONFLICT 545 547 NNW -> GSM (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 569 569 R -> G (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 592 592 Q -> E (in Ref. 5; AA sequence).
{ECO:0000305}.
STRAND 451 453 {ECO:0000244|PDB:2B7F}.
STRAND 456 458 {ECO:0000244|PDB:4YDG}.
STRAND 461 467 {ECO:0000244|PDB:2B7F}.
STRAND 469 471 {ECO:0000244|PDB:2B7F}.
STRAND 474 480 {ECO:0000244|PDB:2B7F}.
STRAND 488 490 {ECO:0000244|PDB:2B7F}.
HELIX 491 493 {ECO:0000244|PDB:2B7F}.
STRAND 500 502 {ECO:0000244|PDB:2B7F}.
STRAND 505 507 {ECO:0000244|PDB:2B7F}.
STRAND 510 521 {ECO:0000244|PDB:2B7F}.
STRAND 523 526 {ECO:0000244|PDB:2B7F}.
STRAND 534 537 {ECO:0000244|PDB:2B7F}.
STRAND 540 542 {ECO:0000244|PDB:2B7F}.
HELIX 552 557 {ECO:0000244|PDB:2B7F}.
STRAND 561 563 {ECO:0000244|PDB:2B7F}.
SEQUENCE 1462 AA; 162512 MW; DCC70251EC729E87 CRC64;
MGQIFSRSAS PIPRPPRGLA AHHWLNFLQA AYRLEPGPSS YDFHQLKKFL KIALETPARI
CPINYSLLAS LLPKGYPGRV NEILHILIQT QAQIPSRPAP PPPSSPTHDP PDSDPQIPPP
YVEPTAPQVL PVMHPHGAPP NHRPWQMKDL QAIKQEVSQA APGSPQFMQT IRLAVQQFDP
TAKDLQDLLQ YLCSSLVASL HHQQLDSLIS EAETRGITGY NPLAGPLRVQ ANNPQQQGLR
REYQQLWLAA FAALPGSAKD PSWASILQGL EEPYHAFVER LNIALDNGLP EGTPKDPILR
SLAYSNANKE CQKLLQARGH TNSPLGDMLR ACQTWTPKDK TKVLVVQPKK PPPNQPCFRC
GKAGHWSRDC TQPRPPPGPC PLCQDPTHWK RDCPRLKPTI PEPEPEEDAL LLDLPADIPH
PKNLHRGGGL TSPPTLQQVL PNQDPASILP VIPLDPARRP VIKAQVDTQT SHPKTIEALL
DTGADMTVLP IALFSSNTPL KNTSVLGAGG QTQDHFKLTS LPVLIRLPFR TTPIVLTSCL
VDTKNNWAII GRDALQQCQG VLYLPEAKRP PVILPIQAPA VLGLEHLPRP PQISQFPLNP
ERLQALQHLV RKALEAGHIE PYTGPGNNPV FPVKKANGTW RFIHDLRATN SLTIDLSSSS
PGPPDLSSLP TTLAHLQTID LRDAFFQIPL PKQFQPYFAF TVPQQCNYGP GTRYAWKVLP
QGFKNSPTLF EMQLAHILQP IRQAFPQCTI LQYMDDILLA SPSHEDLLLL SEATMASLIS
HGLPVSENKT QQTPGTIKFL GQIISPNHLT YDAVPTVPIR SRWALPELQA LLGEIQWVSK
GTPTLRQPLH SLYCALQRHT DPRDQIYLNP SQVQSLVQLR QALSQNCRSR LVQTLPLLGA
IMLTLTGTTT VVFQSKEQWP LVWLHAPLPH TSQCPWGQLL ASAVLLLDKY TLQSYGLLCQ
TIHHNISTQT FNQFIQTSDH PSVPILLHHS HRFKNLGAQT GELWNTFLKT AAPLAPVKAL
MPVFTLSPVI INTAPCLFSD GSTSRAAYIL WDKQILSQRS FPLPPPHKSA QRAELLGLLH
GLSSARSWRC LNIFLDSKYL YHYLRTLALG TFQGRSSQAP FQALLPRLLS RKVVYLHHVR
SHTNLPDPIS RLNALTDALL ITPVLQLSPA ELHSFTHCGQ TALTLQGATT TEASNILRSC
HACRGGNPQH QMPRGHIRRG LLPNHIWQGD ITHFKYKNTL YRLHVWVDTF SGAISATQKR
KETSSEAISS LLQAIAHLGK PSYINTDNGP AYISQDFLNM CTSLAIRHTT HVPYNPTSSG
LVERSNGILK TLLYKYFTDK PDLPMDNALS IALWTINHLN VLTNCHKTRW QLHHSPRLQP
IPETRSLSNK QTHWYYFKLP GLNSRQWKGP QEALQEAAGA ALIPVSASSA QWIPWRLLKR
AACPRPVGGP ADPKEKDLQH HG


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