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Gag polyprotein (Pr55Gag) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Spacer peptide 2 (SP2) (p1); p6-gag]

 GAG_HV1N5               Reviewed;         500 AA.
P12493;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
20-JUN-2018, entry version 164.
RecName: Full=Gag polyprotein;
AltName: Full=Pr55Gag;
Contains:
RecName: Full=Matrix protein p17;
Short=MA;
Contains:
RecName: Full=Capsid protein p24;
Short=CA;
Contains:
RecName: Full=Spacer peptide 1 {ECO:0000303|PubMed:22334652};
Short=SP1;
AltName: Full=p2;
Contains:
RecName: Full=Nucleocapsid protein p7;
Short=NC;
Contains:
RecName: Full=Spacer peptide 2 {ECO:0000303|PubMed:22334652};
Short=SP2;
AltName: Full=p1;
Contains:
RecName: Full=p6-gag;
Name=gag;
Human immunodeficiency virus type 1 group M subtype B (isolate NY5)
(HIV-1).
Viruses; Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
NCBI_TaxID=11698;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Clone pNL4-3;
Buckler C.E., Buckler-White A.J., Willey R.L., McCoy J.;
Submitted (JUN-1988) to the EMBL/GenBank/DDBJ databases.
[2]
INTERACTION OF MATRIX PROTEIN P17 WITH GP41.
PubMed=8918455;
Cosson P.;
"Direct interaction between the envelope and matrix proteins of HIV-
1.";
EMBO J. 15:5783-5788(1996).
[3]
INTERACTION OF CAPSID PROTEIN WITH HUMAN PPIA/CYPA.
PubMed=8980234; DOI=10.1016/S0092-8674(00)81823-1;
Gamble T.R., Vajdos F.F., Yoo S., Worthylake D.K., Houseweart M.,
Sundquist W.I., Hill C.P.;
"Crystal structure of human cyclophilin A bound to the amino-terminal
domain of HIV-1 capsid.";
Cell 87:1285-1294(1996).
[4]
INTERACTION OF P6-GAG WITH HUMAN TSG101, AND FUNCTION (P6-GAG).
PubMed=11427703; DOI=10.1073/pnas.131059198;
VerPlank L., Bouamr F., LaGrassa T.J., Agresta B., Kikonyogo A.,
Leis J., Carter C.A.;
"Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the
L domain in HIV type 1 Pr55(Gag).";
Proc. Natl. Acad. Sci. U.S.A. 98:7724-7729(2001).
[5]
INTERACTION OF P6-GAG WITH HUMAN TSG101, AND FUNCTION (P6-GAG).
PubMed=11595185; DOI=10.1016/S0092-8674(01)00506-2;
Garrus J.E., von Schwedler U.K., Pornillos O.W., Morham S.G.,
Zavitz K.H., Wang H.E., Wettstein D.A., Stray K.M., Cote M.,
Rich R.L., Myszka D.G., Sundquist W.I.;
"Tsg101 and the vacuolar protein sorting pathway are essential for
HIV-1 budding.";
Cell 107:55-65(2001).
[6]
SUBCELLULAR LOCATION OF GAG POLYPROTEIN.
PubMed=14722309; DOI=10.1128/JVI.78.3.1552-1563.2004;
Ono A., Freed E.O.;
"Cell-type-dependent targeting of human immunodeficiency virus type 1
assembly to the plasma membrane and the multivesicular body.";
J. Virol. 78:1552-1563(2004).
[7]
INTERACTION OF MATRIX PROTEIN P17 WITH HUMAN AP3D1.
PubMed=15766529; DOI=10.1016/j.cell.2004.12.023;
Dong X., Li H., Derdowski A., Ding L., Burnett A., Chen X.,
Peters T.R., Dermody T.S., Woodruff E., Wang J.J., Spearman P.;
"AP-3 directs the intracellular trafficking of HIV-1 Gag and plays a
key role in particle assembly.";
Cell 120:663-674(2005).
[8]
INTERACTION OF MATRIX PROTEIN P17 WITH PHOSPHATIDYLINOSITOL
4,5-BISPHOSPHATE, AND FUNCTION (MATRIX PROTEIN P17).
PubMed=16840558; DOI=10.1073/pnas.0602818103;
Saad J.S., Miller J., Tai J., Kim A., Ghanam R.H., Summers M.F.;
"Structural basis for targeting HIV-1 Gag proteins to the plasma
membrane for virus assembly.";
Proc. Natl. Acad. Sci. U.S.A. 103:11364-11369(2006).
[9]
MUTAGENESIS OF SER-9; SER-67; SER-72 AND SER-77.
PubMed=19059618; DOI=10.1016/j.virol.2008.10.047;
Bhatia A.K., Kaushik R., Campbell N.A., Pontow S.E., Ratner L.;
"Mutation of critical serine residues in HIV-1 matrix result in an
envelope incorporation defect which can be rescued by truncation of
the gp41 cytoplasmic tail.";
Virology 384:233-241(2009).
[10]
LATE-BUDDING DOMAINS, INTERACTION OF P6-GAG WITH HOST TSG101,
INTERACTION OF P6-GAG WITH HOST PDCD6IP/AIP1, AND FUNCTION (P6-GAG).
PubMed=19282983; DOI=10.1371/journal.ppat.1000339;
Dussupt V., Javid M.P., Abou-Jaoude G., Jadwin J.A., de La Cruz J.,
Nagashima K., Bouamr F.;
"The nucleocapsid region of HIV-1 Gag cooperates with the PTAP and
LYPXnL late domains to recruit the cellular machinery necessary for
viral budding.";
PLoS Pathog. 5:E1000339-E1000339(2009).
[11]
INTERACTION OF MATRIX PROTEIN P17 WITH RAT CALM1.
PubMed=21799007; DOI=10.1074/jbc.M111.273623;
Samal A.B., Ghanam R.H., Fernandez T.F., Monroe E.B., Saad J.S.;
"NMR, biophysical, and biochemical studies reveal the minimal
Calmodulin binding domain of the HIV-1 matrix protein.";
J. Biol. Chem. 286:33533-33543(2011).
[12]
PROTEOLYTIC PROCESSING OF GAG POLYPROTEIN.
PubMed=22334652; DOI=10.1074/jbc.M112.339374;
Lee S.K., Potempa M., Kolli M., Ozen A., Schiffer C.A., Swanstrom R.;
"Context surrounding processing sites is crucial in determining
cleavage rate of a subset of processing sites in HIV-1 Gag and Gag-
Pro-Pol polyprotein precursors by viral protease.";
J. Biol. Chem. 287:13279-13290(2012).
[13]
INTERACTION OF CAPSID WITH HUMAN NUP153.
STRAIN=Clone pNL4-3;
PubMed=24130490; DOI=10.1371/journal.ppat.1003693;
Matreyek K.A., Yucel S.S., Li X., Engelman A.;
"Nucleoporin NUP153 phenylalanine-glycine motifs engage a common
binding pocket within the HIV-1 capsid protein to mediate lentiviral
infectivity.";
PLoS Pathog. 9:E1003693-E1003693(2013).
[14]
SUBUNIT (CAPSID PROTEIN P24).
PubMed=24066695; DOI=10.1021/ja406246z;
Deshmukh L., Schwieters C.D., Grishaev A., Ghirlando R., Baber J.L.,
Clore G.M.;
"Structure and dynamics of full-length HIV-1 capsid protein in
solution.";
J. Am. Chem. Soc. 135:16133-16147(2013).
[15]
INTERACTION OF MATRIX PROTEIN P17 WITH RNA, AND FUNCTION (MATRIX
PROTEIN P17).
PubMed=23552424; DOI=10.1128/JVI.00075-13;
Chukkapalli V., Inlora J., Todd G.C., Ono A.;
"Evidence in support of RNA-mediated inhibition of phosphatidylserine-
dependent HIV-1 Gag membrane binding in cells.";
J. Virol. 87:7155-7159(2013).
[16]
PHOSPHORYLATION AT SER-148 (CAPSID PROTEIN P24), AND FUNCTION (CAPSID
PROTEIN P24).
PubMed=24509437; DOI=10.1099/vir.0.060053-0;
Dochi T., Nakano T., Inoue M., Takamune N., Shoji S., Sano K.,
Misumi S.;
"Phosphorylation of human immunodeficiency virus type 1 capsid protein
at serine 16, required for peptidyl-prolyl isomerase-dependent
uncoating, is mediated by virion-incorporated extracellular signal-
regulated kinase 2.";
J. Gen. Virol. 95:1156-1166(2014).
[17]
REVIEW.
PubMed=12873766; DOI=10.1016/S0005-2736(03)00163-9;
Scarlata S., Carter C.;
"Role of HIV-1 Gag domains in viral assembly.";
Biochim. Biophys. Acta 1614:62-72(2003).
[18] {ECO:0000244|PDB:1GWP}
STRUCTURE BY NMR OF 133-283.
PubMed=12032547; DOI=10.1038/nsb806;
Tang C., Ndassa Y., Summers M.F.;
"Structure of the N-terminal 283-residue fragment of the immature HIV-
1 Gag polyprotein.";
Nat. Struct. Biol. 9:537-543(2002).
[19] {ECO:0000244|PDB:2C55}
STRUCTURE BY NMR OF 449-500.
PubMed=16234236; DOI=10.1074/jbc.M507375200;
Fossen T., Wray V., Bruns K., Rachmat J., Henklein P., Tessmer U.,
Maczurek A., Klinger P., Schubert U.;
"Solution structure of the human immunodeficiency virus type 1 p6
protein.";
J. Biol. Chem. 280:42515-42527(2005).
-!- FUNCTION: Gag polyprotein: Mediates, with Gag-Pol polyprotein, the
essential events in virion assembly, including binding the plasma
membrane, making the protein-protein interactions necessary to
create spherical particles, recruiting the viral Env proteins, and
packaging the genomic RNA via direct interactions with the RNA
packaging sequence (Psi). {ECO:0000250|UniProtKB:P04591}.
-!- FUNCTION: Matrix protein p17: Targets the polyprotein to the
plasma membrane via a multipartite membrane-binding signal, that
includes its myristoylated N-terminus (PubMed:16840558). Matrix
protein is part of the pre-integration complex. Implicated in the
release from host cell mediated by Vpu. Binds to RNA
(PubMed:23552424). {ECO:0000250, ECO:0000269|PubMed:16840558,
ECO:0000269|PubMed:23552424}.
-!- FUNCTION: Capsid protein p24: Forms the conical core that
encapsulates the genomic RNA-nucleocapsid complex in the virion.
Most core are conical, with only 7% tubular. The core is
constituted by capsid protein hexamer subunits. The core is
disassembled soon after virion entry (By similarity). Host
restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral
capsids and cause premature capsid disassembly, leading to blocks
in reverse transcription. Capsid restriction by TRIM5 is one of
the factors which restricts HIV-1 to the human species. Host PIN1
apparently facilitates the virion uncoating (PubMed:24509437). On
the other hand, interactions with PDZD8 or CYPA stabilize the
capsid. {ECO:0000250, ECO:0000250|UniProtKB:P04591,
ECO:0000269|PubMed:24509437}.
-!- FUNCTION: Nucleocapsid protein p7: Encapsulates and protects viral
dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its
zinc fingers. Acts as a nucleic acid chaperone which is involved
in rearangement of nucleic acid secondary structure during gRNA
retrotranscription. Also facilitates template switch leading to
recombination. As part of the polyprotein, participates in gRNA
dimerization, packaging, tRNA incorporation and virion assembly.
{ECO:0000250|UniProtKB:P04591}.
-!- FUNCTION: p6-gag: Plays a role in budding of the assembled
particle by interacting with the host class E VPS proteins TSG101
and PDCD6IP/AIP1. {ECO:0000269|PubMed:11427703,
ECO:0000269|PubMed:11595185, ECO:0000269|PubMed:19282983}.
-!- SUBUNIT: Gag polyprotein: Homotrimer; further assembles as
hexamers of trimers (By similarity). Oligomerization possibly
creates a central hole into which the cytoplasmic tail of the gp41
envelope protein may be inserted. Gag polyprotein: Interacts with
host TRIM22; this interaction seems to disrupt proper trafficking
of Gag polyprotein and may interfere with budding (By similarity).
Gag polyprotein: Interacts with host PDZD8 (By similarity). Matrix
protein p17: Homotrimer; further assembles as hexamers of trimers
(By similarity). Matrix protein p17: Interacts with gp41 (via C-
terminus) (PubMed:8918455). Matrix protein p17: Interacts with
host CALM1; this interaction induces a conformational change in
the Matrix protein, triggering exposure of the myristate group
(PubMed:21799007). Matrix protein p17: Interacts with host AP3D1;
this interaction allows the polyprotein trafficking to
multivesicular bodies during virus assembly (PubMed:15766529).
Matrix protein p17: Part of the pre-integration complex (PIC)
which is composed of viral genome, matrix protein, Vpr and
integrase (By similarity). Capsid protein p24: Homodimer; the
homodimer further multimerizes as homohexamers or homopentamers
(PubMed:24066695). Capsid protein p24: Interacts with human
PPIA/CYPA; this interaction stabilizes the capsid
(PubMed:8980234). Capsid protein p24: Interacts with human NUP153
(PubMed:24130490). Capsid protein p24: Interacts with host PDZD8;
this interaction stabilizes the capsid (By similarity). Capsid
protein p24: Interacts with monkey TRIM5; this interaction
destabilizes the capsid (By similarity). p6-gag interacts with
Vpr; this interaction allows Vpr incorporation into the virion (By
similarity). p6-gag interacts with host TSG101 (PubMed:11427703,
PubMed:11595185). p6-gag interacts with host
PDCD6IP/AIP1(PubMed:19282983). {ECO:0000250|UniProtKB:P03347,
ECO:0000250|UniProtKB:P03348, ECO:0000250|UniProtKB:P04591,
ECO:0000269|PubMed:11427703, ECO:0000269|PubMed:11595185,
ECO:0000269|PubMed:15766529, ECO:0000269|PubMed:19282983,
ECO:0000269|PubMed:21799007, ECO:0000269|PubMed:24066695,
ECO:0000269|PubMed:24130490, ECO:0000269|PubMed:8918455,
ECO:0000269|PubMed:8980234}.
-!- SUBCELLULAR LOCATION: Gag polyprotein: Host cell membrane; Lipid-
anchor {ECO:0000269|PubMed:14722309}. Host endosome, host
multivesicular body. Note=These locations are probably linked to
virus assembly sites. The main location is the cell membrane, but
under some circumstances, late endosomal compartments can serve as
productive sites for virion assembly.
{ECO:0000269|PubMed:14722309}.
-!- SUBCELLULAR LOCATION: Matrix protein p17: Virion membrane; Lipid-
anchor {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Capsid protein p24: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Nucleocapsid protein p7: Virion
{ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Comment=Translation results in the formation of the Gag
polyprotein most of the time. Ribosomal frameshifting at the
gag-pol genes boundary occurs at low frequency and produces the
Gag-Pol polyprotein. This strategy of translation probably
allows the virus to modulate the quantity of each viral protein.
Maintenance of a correct Gag to Gag-Pol ratio is essential for
RNA dimerization and viral infectivity.;
Name=Gag polyprotein;
IsoId=P12493-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=Gag-Pol polyprotein;
IsoId=P12497-1; Sequence=External;
Note=Produced by -1 ribosomal frameshifting.;
-!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
essential for viral particle budding. They recruit proteins of the
host ESCRT machinery (Endosomal Sorting Complex Required for
Transport) or ESCRT-associated proteins. p6-gag contains two L
domains: a PTAP/PSAP motif, which interacts with the UEV domain of
TSG101 and a LYPX(n)L motif which interacts with PDCD6IP/AIP1.
{ECO:0000269|PubMed:19282983}.
-!- PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the
viral protease yield mature proteins.
{ECO:0000269|PubMed:22334652}.
-!- PTM: Matrix protein p17: Tyrosine phosphorylated presumably in the
virion by a host kinase. Phosphorylation is apparently not a major
regulator of membrane association. {ECO:0000250|UniProtKB:P04591}.
-!- PTM: Capsid protein p24: Phosphorylated possibly by host MAPK1;
this phosphorylation is necessary for Pin1-mediated virion
uncoating. {ECO:0000269|PubMed:24509437}.
-!- PTM: Nucleocapsid protein p7: Methylated by host PRMT6, impairing
its function by reducing RNA annealing and the initiation of
reverse transcription. {ECO:0000250|UniProtKB:P03347}.
-!- MISCELLANEOUS: The infectious clone pNL4-3 is a chimeric provirus
that consists of DNA from HIV isolates NY5 (5' half) and BRU (3'
half).
-!- MISCELLANEOUS: HIV-1 lineages are divided in three main groups, M
(for Major), O (for Outlier), and N (for New, or Non-M, Non-O).
The vast majority of strains found worldwide belong to the group
M. Group O seems to be endemic to and largely confined to Cameroon
and neighboring countries in West Central Africa, where these
viruses represent a small minority of HIV-1 strains. The group N
is represented by a limited number of isolates from Cameroonian
persons. The group M is further subdivided in 9 clades or subtypes
(A to D, F to H, J and K).
-!- SIMILARITY: Belongs to the primate lentivirus group gag
polyprotein family. {ECO:0000305}.
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EMBL; M19921; AAA44987.1; -; Genomic_RNA.
PDB; 1GWP; NMR; -; A=133-283.
PDB; 2C55; NMR; -; A=449-500.
PDB; 3GV2; X-ray; 7.00 A; A/B/C/D/E/F=133-351.
PDB; 4U0A; X-ray; 2.05 A; A=133-363.
PDB; 4U0B; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=133-363.
PDB; 4U0C; X-ray; 1.77 A; A=133-363.
PDB; 4U0D; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L=133-363.
PDB; 4U0E; X-ray; 2.04 A; A=133-363.
PDB; 4U0F; X-ray; 2.22 A; A=133-363.
PDB; 4XFX; X-ray; 2.43 A; A=133-363.
PDB; 4XFY; X-ray; 2.80 A; A=133-363.
PDB; 4XFZ; X-ray; 2.70 A; A=133-363.
PDB; 4XRO; X-ray; 2.01 A; A=133-363.
PDB; 4XRQ; X-ray; 1.95 A; A=133-363.
PDB; 5HGL; X-ray; 3.10 A; A/B/C/D/E/F=133-363.
PDB; 5HGM; X-ray; 2.04 A; A=133-363.
PDB; 5HGN; X-ray; 1.90 A; A=133-363.
PDB; 5HGO; X-ray; 2.00 A; A=133-363.
PDB; 5HGP; X-ray; 1.95 A; A=133-363.
PDB; 5IRT; NMR; -; A/B=133-363.
PDB; 5JPA; X-ray; 1.70 A; A=133-363.
PDB; 5L93; EM; 3.90 A; A/B/C=148-371.
PDB; 5O2U; X-ray; 2.76 A; A/C=1-500.
PDB; 5TSV; X-ray; 2.50 A; A/B=133-363.
PDB; 5TSX; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L=133-363.
PDB; 5UPW; EM; 5.00 A; A/B/C/D/E/F=133-353.
PDBsum; 1GWP; -.
PDBsum; 2C55; -.
PDBsum; 3GV2; -.
PDBsum; 4U0A; -.
PDBsum; 4U0B; -.
PDBsum; 4U0C; -.
PDBsum; 4U0D; -.
PDBsum; 4U0E; -.
PDBsum; 4U0F; -.
PDBsum; 4XFX; -.
PDBsum; 4XFY; -.
PDBsum; 4XFZ; -.
PDBsum; 4XRO; -.
PDBsum; 4XRQ; -.
PDBsum; 5HGL; -.
PDBsum; 5HGM; -.
PDBsum; 5HGN; -.
PDBsum; 5HGO; -.
PDBsum; 5HGP; -.
PDBsum; 5IRT; -.
PDBsum; 5JPA; -.
PDBsum; 5L93; -.
PDBsum; 5O2U; -.
PDBsum; 5TSV; -.
PDBsum; 5TSX; -.
PDBsum; 5UPW; -.
DisProt; DP00101; -.
ProteinModelPortal; P12493; -.
SMR; P12493; -.
iPTMnet; P12493; -.
Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
EvolutionaryTrace; P12493; -.
PRO; PR:P12493; -.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0072494; C:host multivesicular body; IEA:UniProtKB-SubCell.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
Gene3D; 1.10.1200.30; -; 1.
Gene3D; 1.10.150.90; -; 1.
Gene3D; 1.10.375.10; -; 1.
InterPro; IPR000721; Gag_p24.
InterPro; IPR014817; Gag_p6.
InterPro; IPR000071; Lentvrl_matrix_N.
InterPro; IPR012344; Matrix_HIV/RSV_N.
InterPro; IPR008916; Retrov_capsid_C.
InterPro; IPR008919; Retrov_capsid_N.
InterPro; IPR010999; Retrovr_matrix.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
Pfam; PF00540; Gag_p17; 1.
Pfam; PF00607; Gag_p24; 1.
Pfam; PF08705; Gag_p6; 1.
Pfam; PF00098; zf-CCHC; 2.
PRINTS; PR00234; HIV1MATRIX.
SMART; SM00343; ZnF_C2HC; 2.
SUPFAM; SSF47836; SSF47836; 1.
SUPFAM; SSF47943; SSF47943; 1.
SUPFAM; SSF57756; SSF57756; 1.
PROSITE; PS50158; ZF_CCHC; 2.
1: Evidence at protein level;
3D-structure; AIDS; Capsid protein; Host cell membrane;
Host cytoplasm; Host endosome; Host membrane; Host nucleus;
Host-virus interaction; Lipoprotein; Membrane; Metal-binding;
Methylation; Myristate; Phosphoprotein; Repeat;
Ribosomal frameshifting; RNA-binding; Viral budding;
Viral budding via the host ESCRT complexes; Viral nucleoprotein;
Viral release from host cell; Virion; Zinc; Zinc-finger.
INIT_MET 1 1 Removed; by host. {ECO:0000250}.
CHAIN 2 500 Gag polyprotein.
/FTId=PRO_0000261226.
CHAIN 2 132 Matrix protein p17. {ECO:0000250}.
/FTId=PRO_0000038559.
CHAIN 133 363 Capsid protein p24. {ECO:0000250}.
/FTId=PRO_0000038560.
PEPTIDE 364 377 Spacer peptide 1. {ECO:0000250}.
/FTId=PRO_0000038561.
CHAIN 378 432 Nucleocapsid protein p7. {ECO:0000250}.
/FTId=PRO_0000038562.
PEPTIDE 433 448 Spacer peptide 2. {ECO:0000250}.
/FTId=PRO_0000038563.
CHAIN 449 500 p6-gag. {ECO:0000250}.
/FTId=PRO_0000038564.
ZN_FING 390 407 CCHC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 411 428 CCHC-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
REGION 7 31 Interaction with Gp41.
{ECO:0000269|PubMed:8918455}.
REGION 8 43 Interaction with host CALM1.
{ECO:0000250|UniProtKB:P04591}.
REGION 12 19 Interaction with host AP3D1.
{ECO:0000269|PubMed:15766529}.
REGION 14 33 Interaction with membrane
phosphatidylinositol 4,5-bisphosphate and
RNA. {ECO:0000269|PubMed:16840558}.
REGION 73 77 Interaction with membrane
phosphatidylinositol 4,5-bisphosphate.
{ECO:0000269|PubMed:16840558}.
REGION 189 227 Interaction with host PPIA/CYPA and
NUP153. {ECO:0000250|UniProtKB:P12493}.
REGION 189 227 Interaction with human PPIA/CYPA and
NUP153. {ECO:0000269|PubMed:24130490,
ECO:0000269|PubMed:8980234}.
REGION 217 225 PPIA/CYPA-binding loop.
{ECO:0000250|UniProtKB:P04591}.
REGION 277 363 Dimerization/Multimerization of capsid
protein p24.
{ECO:0000250|UniProtKB:P04591}.
MOTIF 16 22 Nuclear export signal. {ECO:0000250}.
MOTIF 26 32 Nuclear localization signal.
{ECO:0000250}.
MOTIF 455 458 PTAP/PSAP motif.
MOTIF 483 492 LYPX(n)L motif.
SITE 132 133 Cleavage; by viral protease.
{ECO:0000250}.
SITE 363 364 Cleavage; by viral protease.
{ECO:0000250}.
SITE 377 378 Cleavage; by viral protease.
{ECO:0000250}.
SITE 432 433 Cleavage; by viral protease.
{ECO:0000250}.
SITE 448 449 Cleavage; by viral protease.
{ECO:0000250}.
MOD_RES 148 148 Phosphoserine; by host MAPK1.
{ECO:0000269|PubMed:24509437}.
MOD_RES 387 387 Asymmetric dimethylarginine; in
Nucleocapsid protein p7; by host PRMT6.
{ECO:0000250}.
MOD_RES 409 409 Asymmetric dimethylarginine; in
Nucleocapsid protein p7; by host PRMT6.
{ECO:0000250}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000250}.
MUTAGEN 9 9 S->A: Loss of ability to fuse with target
cell membranes and infect host cell.
{ECO:0000269|PubMed:19059618}.
MUTAGEN 67 67 S->A: Loss of ability to fuse with target
cell membranes and infect host cell.
{ECO:0000269|PubMed:19059618}.
MUTAGEN 72 72 S->A: Loss of ability to fuse with target
cell membranes and infect host cell.
{ECO:0000269|PubMed:19059618}.
MUTAGEN 77 77 S->A: Loss of ability to fuse with target
cell membranes and infect host cell.
{ECO:0000269|PubMed:19059618}.
STRAND 134 136 {ECO:0000244|PDB:5JPA}.
STRAND 138 144 {ECO:0000244|PDB:5JPA}.
HELIX 149 162 {ECO:0000244|PDB:5JPA}.
HELIX 168 175 {ECO:0000244|PDB:5JPA}.
TURN 176 178 {ECO:0000244|PDB:5JPA}.
HELIX 181 189 {ECO:0000244|PDB:5JPA}.
HELIX 195 215 {ECO:0000244|PDB:5JPA}.
STRAND 225 227 {ECO:0000244|PDB:4XFY}.
HELIX 233 236 {ECO:0000244|PDB:5JPA}.
STRAND 239 241 {ECO:0000244|PDB:5JPA}.
HELIX 243 250 {ECO:0000244|PDB:5JPA}.
STRAND 252 254 {ECO:0000244|PDB:5JPA}.
HELIX 258 277 {ECO:0000244|PDB:5JPA}.
HELIX 282 284 {ECO:0000244|PDB:5JPA}.
HELIX 293 307 {ECO:0000244|PDB:5JPA}.
TURN 308 310 {ECO:0000244|PDB:4XRQ}.
TURN 311 313 {ECO:0000244|PDB:4U0C}.
HELIX 319 324 {ECO:0000244|PDB:5JPA}.
HELIX 328 337 {ECO:0000244|PDB:5JPA}.
HELIX 343 349 {ECO:0000244|PDB:5JPA}.
TURN 350 352 {ECO:0000244|PDB:5O2U}.
TURN 463 465 {ECO:0000244|PDB:2C55}.
HELIX 466 468 {ECO:0000244|PDB:2C55}.
STRAND 474 476 {ECO:0000244|PDB:2C55}.
STRAND 480 484 {ECO:0000244|PDB:2C55}.
HELIX 487 490 {ECO:0000244|PDB:2C55}.
HELIX 492 494 {ECO:0000244|PDB:2C55}.
SEQUENCE 500 AA; 55819 MW; 08ECC125834088C6 CRC64;
MGARASVLSG GELDKWEKIR LRPGGKKQYK LKHIVWASRE LERFAVNPGL LETSEGCRQI
LGQLQPSLQT GSEELRSLYN TIAVLYCVHQ RIDVKDTKEA LDKIEEEQNK SKKKAQQAAA
DTGNNSQVSQ NYPIVQNLQG QMVHQAISPR TLNAWVKVVE EKAFSPEVIP MFSALSEGAT
PQDLNTMLNT VGGHQAAMQM LKETINEEAA EWDRLHPVHA GPIAPGQMRE PRGSDIAGTT
STLQEQIGWM THNPPIPVGE IYKRWIILGL NKIVRMYSPT SILDIRQGPK EPFRDYVDRF
YKTLRAEQAS QEVKNWMTET LLVQNANPDC KTILKALGPG ATLEEMMTAC QGVGGPGHKA
RVLAEAMSQV TNPATIMIQK GNFRNQRKTV KCFNCGKEGH IAKNCRAPRK KGCWKCGKEG
HQMKDCTERQ ANFLGKIWPS HKGRPGNFLQ SRPEPTAPPE ESFRFGEETT TPSQKQEPID
KELYPLASLR SLFGSDPSSQ


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