ID   Q72497_9HIV1            Unreviewed;       500 AA.
AC   Q72497;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 180.
DE   RecName: Full=Gag polyprotein {ECO:0000256|RuleBase:RU004487};
DE   Contains:
DE     RecName: Full=Matrix protein p17 {ECO:0000256|RuleBase:RU004487};
DE              Short=MA {ECO:0000256|RuleBase:RU004487};
GN   Name=gag {ECO:0000313|EMBL:AAB60571.1};
OS   Human immunodeficiency virus 1.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11676 {ECO:0000313|EMBL:AAB60571.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1] {ECO:0000313|EMBL:AAB60571.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NL4-3 {ECO:0000313|EMBL:AAB60571.1};
RX   PubMed=3016298;
RA   Adachi A., Gendelman H.E., Koenig S., Folks T., Willey R., Rabson A.,
RA   Martin M.A.;
RT   "Production of acquired immunodeficiency syndrome-associated retrovirus in
RT   human and nonhuman cells transfected with an infectious molecular clone.";
RL   J. Virol. 59:284-291(1986).
RN   [2] {ECO:0000313|EMBL:AAB60571.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NL4-3 {ECO:0000313|EMBL:AAB60571.1};
RX   PubMed=7483282; DOI=10.1006/viro.1995.1548;
RA   Salminen M.O., Koch C., Sanders-Buell E., Ehrenberg P.K., Michael N.L.,
RA   Carr J.K., Burke D.S., McCutchan F.E.;
RT   "Recovery of virtually full-length HIV-1 provirus of diverse subtypes from
RT   primary virus cultures using the polymerase chain reaction.";
RL   Virology 213:80-86(1995).
RN   [3] {ECO:0000313|EMBL:AAB60571.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NL4-3 {ECO:0000313|EMBL:AAB60571.1};
RA   Salminen M.S.;
RL   Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0007829|PDB:1L6N}
RP   STRUCTURE BY NMR OF 1-283.
RX   PubMed=12032547; DOI=10.1038/nsb806;
RA   Tang C., Ndassa Y., Summers M.F.;
RT   "Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag
RT   polyprotein.";
RL   Nat. Struct. Biol. 9:537-543(2002).
RN   [5] {ECO:0007829|PDB:1M9C, ECO:0007829|PDB:1M9E}
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 133-278.
RX   PubMed=12730686; DOI=10.1038/nsb927;
RA   Howard B.R., Vajdos F.F., Li S., Sundquist W.I., Hill C.P.;
RT   "Structural insights into the catalytic mechanism of cyclophilin A.";
RL   Nat. Struct. Biol. 10:475-481(2003).
RN   [6] {ECO:0007829|PDB:3OBU, ECO:0007829|PDB:3OBX}
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 453-461.
RX   PubMed=21070952; DOI=10.1016/j.str.2010.08.010;
RA   Im Y.J., Kuo L., Ren X., Burgos P.V., Zhao X.Z., Liu F., Burke T.R.,
RA   Bonifacino J.S., Freed E.O., Hurley J.H.;
RT   "Crystallographic and functional analysis of the ESCRT-I /HIV-1 Gag PTAP
RT   interaction.";
RL   Structure 18:1536-1547(2010).
RN   [7] {ECO:0007829|PDB:3P0A}
RP   X-RAY CRYSTALLOGRAPHY (5.95 ANGSTROMS) OF 133-363.
RX   PubMed=21248851; DOI=10.1038/nature09640;
RA   Pornillos O., Ganser-Pornillos B.K., Yeager M.;
RT   "Atomic-level modelling of the HIV capsid.";
RL   Nature 469:424-427(2011).
RN   [8] {ECO:0007829|PDB:5I4T}
RP   X-RAY CRYSTALLOGRAPHY (3.27 ANGSTROMS) OF 278-377.
RX   PubMed=27416583; DOI=10.7554/eLife.17063;
RA   Wagner J.M., Zadrozny K.K., Chrustowicz J., Purdy M.D., Yeager M.,
RA   Ganser-Pornillos B.K., Pornillos O.;
RT   "Crystal structure of an HIV assembly and maturation switch. .";
RL   Elife 5:e17063-e17063(2016).
RN   [9] {ECO:0007829|PDB:5MCZ, ECO:0007829|PDB:5MD0}
RP   STRUCTURE BY ELECTRON MICROSCOPY (8.00 ANGSTROMS) OF 280-353 AND 133-279.
RX   PubMed=27980210; DOI=10.1126/science.aah4972;
RA   Mattei S., Glass B., Hagen W.J., Krausslich H.G., Briggs J.A.;
RT   "The structure and flexibility of conical HIV-1 capsids determined within
RT   intact virions.";
RL   Science 354:1434-1437(2016).
CC   -!- INTERACTION:
CC       Q72497; P62937: PPIA; Xeno; NbExp=7; IntAct=EBI-1036263, EBI-437708;
CC   -!- SUBCELLULAR LOCATION: [Matrix protein p17]: Virion membrane
CC       {ECO:0000256|RuleBase:RU004487}; Lipid-anchor
CC       {ECO:0000256|RuleBase:RU004487}. Host nucleus
CC       {ECO:0000256|RuleBase:RU004487}. Host cytoplasm
CC       {ECO:0000256|RuleBase:RU004487}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}. Virion
CC       {ECO:0000256|RuleBase:RU004487}. Host cytoplasm
CC       {ECO:0000256|RuleBase:RU004487}. Host nucleus
CC       {ECO:0000256|RuleBase:RU004487}.
CC   -!- PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral
CC       protease yield mature proteins. {ECO:0000256|RuleBase:RU004487}.
CC   -!- SIMILARITY: Belongs to the primate lentivirus group gag polyprotein
CC       family. {ECO:0000256|ARBA:ARBA00008364}.
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DR   EMBL; U26942; AAB60571.1; -; Genomic_DNA.
DR   PDB; 1L6N; NMR; -; A=1-283.
DR   PDB; 1M9C; X-ray; 2.00 A; C/D=133-278.
DR   PDB; 1M9E; X-ray; 1.72 A; C/D=133-278.
DR   PDB; 1M9F; X-ray; 1.73 A; C/D=133-278.
DR   PDB; 1M9X; X-ray; 1.70 A; C/D/G/H=133-278.
DR   PDB; 1M9Y; X-ray; 1.90 A; C/D/G/H=133-278.
DR   PDB; 3OBU; X-ray; 1.60 A; B=453-461.
DR   PDB; 3OBX; X-ray; 1.60 A; B=453-461.
DR   PDB; 3P0A; X-ray; 5.95 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=133-363.
DR   PDB; 5I4T; X-ray; 3.27 A; G/H/I/J/K/L=278-377.
DR   PDB; 5MCZ; EM; 8.20 A; A/B/C/D/E/F/G/W=280-353, H/I/J/a/b/f=133-279.
DR   PDB; 5MD0; EM; 8.40 A; A/B/C/D/E/F/G/W=280-353, H/I/J/a/b/f=133-279.
DR   PDB; 5MD1; EM; 8.20 A; A/B/C/D/E/F/G/W=280-353, H/I/J/a/b/f=133-279.
DR   PDB; 5MD2; EM; 8.60 A; A/B/C/D/E/F/G/W=280-353, H/I/J/a/b/f=133-279.
DR   PDB; 5MD3; EM; 8.50 A; A/B/C/D/E/F/G/W=280-353, H/I/J/a/b/f=133-279.
DR   PDB; 5MD4; EM; 8.40 A; A/B/C/D/E/F/G/W=280-353, H/I/J/a/b/f=133-279.
DR   PDB; 5MD5; EM; 8.20 A; A/B/C/D/E/F/G/W=280-353, H/I/J/a/b/f=133-279.
DR   PDB; 5MD6; EM; 8.10 A; A/B/C/D/E/F/G/W=280-353, H/I/J/a/b/f=133-279.
DR   PDB; 5MD7; EM; 8.40 A; A/B/C/D/E/F/G/W=280-353, H/I/J/a/b/f=133-279.
DR   PDB; 5MD8; EM; 8.60 A; A/B/C/D/E/F/G/W=280-353, H/I/J/a/b/f=133-279.
DR   PDB; 5MD9; EM; 8.00 A; A/B/C/D/E/F/G/W=280-353, H/I/J/a/b/f=133-279.
DR   PDB; 5MDA; EM; 8.40 A; A/B/C/D/E/F/G/W=280-353, H/I/J/a/b/f=133-279.
DR   PDB; 5MDB; EM; 8.40 A; A/B/C/D/E/F/G/W=280-353, H/I/J/a/b/f=133-279.
DR   PDB; 5MDC; EM; 8.40 A; A/B/C/D/E/F/G/W=280-353, H/I/J/a/b/f=133-279.
DR   PDB; 5MDD; EM; 8.50 A; A/B/C/D/E/F/G/W=280-353, H/I/J/a/b/f=133-279.
DR   PDB; 5MDE; EM; 8.40 A; A/B/C/D/E/F/G/W=280-353, H/I/J/a/b/f=133-279.
DR   PDB; 5MDF; EM; 8.50 A; A/B/C/D/E/F/G/W=280-353, H/I/J/a/b/f=133-279.
DR   PDB; 5MDG; EM; 8.70 A; A/B/C/D/E/F/G/W=280-353, H/I/J/a/b/f=133-279.
DR   PDBsum; 1L6N; -.
DR   PDBsum; 1M9C; -.
DR   PDBsum; 1M9E; -.
DR   PDBsum; 1M9F; -.
DR   PDBsum; 1M9X; -.
DR   PDBsum; 1M9Y; -.
DR   PDBsum; 3OBU; -.
DR   PDBsum; 3OBX; -.
DR   PDBsum; 3P0A; -.
DR   PDBsum; 5I4T; -.
DR   PDBsum; 5MCZ; -.
DR   PDBsum; 5MD0; -.
DR   PDBsum; 5MD1; -.
DR   PDBsum; 5MD2; -.
DR   PDBsum; 5MD3; -.
DR   PDBsum; 5MD4; -.
DR   PDBsum; 5MD5; -.
DR   PDBsum; 5MD6; -.
DR   PDBsum; 5MD7; -.
DR   PDBsum; 5MD8; -.
DR   PDBsum; 5MD9; -.
DR   PDBsum; 5MDA; -.
DR   PDBsum; 5MDB; -.
DR   PDBsum; 5MDC; -.
DR   PDBsum; 5MDD; -.
DR   PDBsum; 5MDE; -.
DR   PDBsum; 5MDF; -.
DR   PDBsum; 5MDG; -.
DR   EMDB; EMD-3477; -.
DR   EMDB; EMD-3479; -.
DR   EMDB; EMD-3480; -.
DR   EMDB; EMD-3481; -.
DR   EMDB; EMD-3482; -.
DR   EMDB; EMD-3484; -.
DR   EMDB; EMD-3485; -.
DR   SMR; Q72497; -.
DR   DIP; DIP-36777N; -.
DR   IntAct; Q72497; 3.
DR   DrugBank; DB08231; Myristic acid.
DR   EvolutionaryTrace; Q72497; -.
DR   Proteomes; UP000160754; Genome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1200.30; -; 1.
DR   Gene3D; 6.10.250.390; -; 1.
DR   Gene3D; 1.10.375.10; Human Immunodeficiency Virus Type 1 Capsid Protein; 1.
DR   Gene3D; 1.10.150.90; Immunodeficiency lentiviruses, gag gene matrix protein p17; 1.
DR   Gene3D; 1.20.5.760; Single helix bin; 1.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR   InterPro; IPR045345; Gag_p24_C.
DR   InterPro; IPR014817; Gag_p6.
DR   InterPro; IPR000071; Lentvrl_matrix_N.
DR   InterPro; IPR012344; Matrix_HIV/RSV_N.
DR   InterPro; IPR008916; Retrov_capsid_C.
DR   InterPro; IPR008919; Retrov_capsid_N.
DR   InterPro; IPR010999; Retrovr_matrix.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PANTHER; PTHR40389; ENDOGENOUS RETROVIRUS GROUP K MEMBER 24 GAG POLYPROTEIN-RELATED; 1.
DR   PANTHER; PTHR40389:SF3; IGE-BINDING PROTEIN; 1.
DR   Pfam; PF00540; Gag_p17; 1.
DR   Pfam; PF00607; Gag_p24; 1.
DR   Pfam; PF19317; Gag_p24_C; 1.
DR   Pfam; PF08705; Gag_p6; 1.
DR   Pfam; PF00098; zf-CCHC; 2.
DR   PRINTS; PR00234; HIV1MATRIX.
DR   SMART; SM00343; ZnF_C2HC; 2.
DR   SUPFAM; SSF47836; Retroviral matrix proteins; 1.
DR   SUPFAM; SSF47353; Retrovirus capsid dimerization domain-like; 1.
DR   SUPFAM; SSF47943; Retrovirus capsid protein, N-terminal core domain; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   PROSITE; PS50158; ZF_CCHC; 2.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:1L6N, ECO:0007829|PDB:1M9C};
KW   Capsid protein {ECO:0000256|ARBA:ARBA00022561,
KW   ECO:0000256|RuleBase:RU004487};
KW   Host cytoplasm {ECO:0000256|ARBA:ARBA00023200,
KW   ECO:0000256|RuleBase:RU004487};
KW   Host nucleus {ECO:0000256|ARBA:ARBA00022562,
KW   ECO:0000256|RuleBase:RU004487};
KW   Host-virus interaction {ECO:0000256|ARBA:ARBA00022581,
KW   ECO:0000256|RuleBase:RU004487};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004487}; Myristate {ECO:0000256|ARBA:ARBA00022707};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Ribosomal frameshifting {ECO:0000256|ARBA:ARBA00022758};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU004487};
KW   Viral budding {ECO:0000256|ARBA:ARBA00022637};
KW   Viral budding via the host ESCRT complexes {ECO:0000256|ARBA:ARBA00022462};
KW   Viral nucleoprotein {ECO:0000256|ARBA:ARBA00023086,
KW   ECO:0000256|RuleBase:RU004487};
KW   Viral release from host cell {ECO:0000256|ARBA:ARBA00022612};
KW   Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|RuleBase:RU004487};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004487};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00047}.
FT   DOMAIN          391..406
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   DOMAIN          413..428
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   REGION          106..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          438..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   500 AA;  55847 MW;  08F450AC834088C6 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 TPSQRQEPID
     KELYPLASLR SLFGSDPSSQ
//