GAG_RSVSB
ID GAG_RSVSB Reviewed; 701 AA.
AC O92954;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Gag polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p19;
DE Contains:
DE RecName: Full=p2A;
DE Contains:
DE RecName: Full=p2B;
DE Contains:
DE RecName: Full=p10;
DE Contains:
DE RecName: Full=Capsid protein p27, alternate cleaved 1;
DE Contains:
DE RecName: Full=Capsid protein p27, alternate cleaved 2;
DE Contains:
DE RecName: Full=Spacer peptide;
DE Short=SP;
DE AltName: Full=p3;
DE Contains:
DE RecName: Full=Nucleocapsid protein p12;
DE Contains:
DE RecName: Full=Protease p15;
DE EC=3.4.23.-;
GN Name=gag;
OS Rous sarcoma virus (strain Schmidt-Ruppin B) (RSV-SRB).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX NCBI_TaxID=269447;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Schmidt-Ruppin B;
RA Bouck J., Skalka A.M., Katz R.A.;
RT "Complete nucleotide sequence of avian sarcoma virus.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP STRUCTURE BY NMR OF 239-479.
RX PubMed=10669613; DOI=10.1006/jmbi.1999.3475;
RA Campos-Olivas R., Newman J.L., Summers M.F.;
RT "Solution structure and dynamics of the Rous sarcoma virus capsid protein
RT and comparison with capsid proteins of other retroviruses.";
RL J. Mol. Biol. 296:633-649(2000).
CC -!- FUNCTION: [Gag polyprotein]: The p10 domain folds back and interacts
CC with the capsid protein domain during Gag polyprotein assembly in the
CC immature particle (before the maturation cleavage that splits the 2
CC domains). {ECO:0000250|UniProtKB:P03322}.
CC -!- FUNCTION: Capsid protein p27: Self-associates to form the irregular
CC polyhedron core composed of hexamers and pentamers, that encapsulates
CC the genomic RNA-nucleocapsid complex. Assembles as a tube in vitro.
CC {ECO:0000250|UniProtKB:P03322}.
CC -!- FUNCTION: [Nucleocapsid protein p12]: Binds strongly to viral nucleic
CC acids and promote their aggregation. Also destabilizes the nucleic
CC acids duplexes via highly structured zinc-binding motifs.
CC {ECO:0000305}.
CC -!- FUNCTION: [Spacer peptide]: Plays a role in the oligomerization of the
CC Gag polyprotein and in the stabilization of the immature particle.
CC Essential layering element during tube assembly.
CC {ECO:0000250|UniProtKB:P03322}.
CC -!- FUNCTION: [Protease p15]: Aspartyl protease that mediates proteolytic
CC cleavages of Gag and Gag-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. {ECO:0000255|PROSITE-
CC ProRule:PRU00275}.
CC -!- SUBUNIT: [Protease p15]: Active as a homodimer.
CC {ECO:0000250|UniProtKB:P03322}.
CC -!- SUBUNIT: [Capsid protein p27, alternate cleaved 1]: Homodimer.
CC Homomultimer. {ECO:0000250|UniProtKB:P03322}.
CC -!- SUBUNIT: [Capsid protein p27, alternate cleaved 2]: Homodimer.
CC Homomultimer. {ECO:0000250|UniProtKB:P03322}.
CC -!- SUBUNIT: [Gag polyprotein]: Homohexamer. Interacts (via p2B domain)
CC with host PACSIN2; this interaction probably allows PACSIN2 recruitment
CC to viral assembly sites (Probable). {ECO:0000250|UniProtKB:P03322}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p19]: Virion
CC {ECO:0000250|UniProtKB:P03322}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p27, alternate cleaved 1]: Virion
CC {ECO:0000250|UniProtKB:P03322}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p27, alternate cleaved 2]: Virion
CC {ECO:0000250|UniProtKB:P03322}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p12]: Virion
CC {ECO:0000250|UniProtKB:P03322}.
CC -!- SUBCELLULAR LOCATION: [Gag polyprotein]: Host nucleus, host nucleolus
CC {ECO:0000250|UniProtKB:P03322}. Host nucleus, host nucleoplasm
CC {ECO:0000250|UniProtKB:P03322}. Note=Shuttles between nucleoplasm and
CC nucleolus. {ECO:0000250|UniProtKB:P03322}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Comment=Translation results in the formation of the Gag polyprotein.
CC Ribosomal frameshifting at the gag/pol genes boundary produces the
CC Gag-Pol polyprotein.;
CC Name=Gag polyprotein;
CC IsoId=O92954-1; Sequence=Displayed;
CC Name=Gag-Pol polyprotein;
CC IsoId=O92956-1; Sequence=External;
CC -!- DOMAIN: [Gag polyprotein]: Late-budding domains (L domains) are short
CC sequence motifs essential for viral particle release. They can occur
CC individually or in close proximity within structural proteins. They
CC interacts with sorting cellular proteins of the multivesicular body
CC (MVB) pathway. Most of these proteins are class E vacuolar protein
CC sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes.
CC P2B contains two L domains: a PPXY motif which probably binds to the WW
CC domains of HECT (homologous to E6-AP C-terminus) E3 ubiquitin ligases
CC and a LYPX(n)L domain which is known to bind the Alix adaptator
CC protein. {ECO:0000250|UniProtKB:P03322}.
CC -!- DOMAIN: [Gag polyprotein]: Contains a nuclear export signal in p10 and
CC a nucleolar localization signal in nucleocapsid protein p12.
CC {ECO:0000250|UniProtKB:P03322}.
CC -!- DOMAIN: Capsid protein p27: Proton-driven dimerization of the C-
CC terminus facilitates capsid assembly. {ECO:0000250|UniProtKB:P03322}.
CC -!- PTM: [Gag polyprotein]: Specific enzymatic cleavages in vivo yield
CC mature proteins. The cleavage at the C-terminus of the Capsid protein
CC p27 is slowly trimmed by the viral protease, sometimes being cut
CC internally thereby generating the short version of the capsid protein
CC and a capsid protein C-terminally extended by 3 amino acids in a ratio
CC of 2:1. {ECO:0000250|UniProtKB:P03322}.
CC -!- MISCELLANEOUS: [Isoform Gag polyprotein]: Produced by conventional
CC translation. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF052428; AAC08987.1; -; Genomic_DNA.
DR PDB; 1D1D; NMR; -; A=239-479.
DR PDBsum; 1D1D; -.
DR BMRB; O92954; -.
DR SMR; O92954; -.
DR MEROPS; A02.015; -.
DR EvolutionaryTrace; O92954; -.
DR Proteomes; UP000159275; Genome.
DR GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0044095; C:host cell nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0046797; P:viral procapsid maturation; IEA:UniProtKB-KW.
DR CDD; cd05482; HIV_retropepsin_like; 1.
DR Gene3D; 1.10.1200.30; -; 1.
DR Gene3D; 1.10.150.90; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR Gene3D; 2.40.70.10; -; 1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR004028; Gag_M.
DR InterPro; IPR000721; Gag_p24_N.
DR InterPro; IPR012344; Matrix_HIV/RSV_N.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR034170; Retropepsin-like_cat_dom.
DR InterPro; IPR018061; Retropepsins.
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 Pfam; PF00607; Gag_p24; 1.
DR Pfam; PF02813; Retro_M; 1.
DR Pfam; PF00077; RVP; 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; SSF57756; SSF57756; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aspartyl protease; Capsid protein; Host nucleus; Hydrolase;
KW Metal-binding; Protease; Repeat; Ribosomal frameshifting;
KW Viral capsid assembly; Viral capsid maturation; Viral matrix protein;
KW Viral release from host cell; Virion; Zinc; Zinc-finger.
FT CHAIN 1..701
FT /note="Gag polyprotein"
FT /id="PRO_0000442112"
FT CHAIN 1..155
FT /note="Matrix protein p19"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT /id="PRO_5000054139"
FT CHAIN 156..166
FT /note="p2A"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT /id="PRO_0000397081"
FT CHAIN 167..177
FT /note="p2B"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT /id="PRO_0000397082"
FT CHAIN 178..239
FT /note="p10"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT /id="PRO_5000054140"
FT CHAIN 240..479
FT /note="Capsid protein p27, alternate cleaved 2"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT /id="PRO_5000054141"
FT CHAIN 240..476
FT /note="Capsid protein p27, alternate cleaved 1"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT /id="PRO_0000442113"
FT PEPTIDE 480..488
FT /note="Spacer peptide"
FT /id="PRO_0000397083"
FT CHAIN 489..577
FT /note="Nucleocapsid protein p12"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT /id="PRO_5000054142"
FT CHAIN 578..701
FT /note="Protease p15"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT /id="PRO_5000054143"
FT DOMAIN 609..690
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT ZN_FING 507..524
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 533..550
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 128..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..259
FT /note="Involved in capsid protein dimerization"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT REGION 290..298
FT /note="Involved in capsid protein dimerization"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT REGION 351..362
FT /note="Involved in capsid protein dimerization"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT REGION 544..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 172..175
FT /note="PPXY motif"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT MOTIF 180..184
FT /note="LYPX(n)L motif"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT MOTIF 219..229
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT MOTIF 524..527
FT /note="Nuclear/nucleolar localization signal"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT ACT_SITE 614
FT /note="For protease activity; shared with dimeric partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT SITE 155..156
FT /note="Cleavage; by viral protease p15"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT SITE 166..167
FT /note="Cleavage; by viral protease p15"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT SITE 177..178
FT /note="Cleavage; by viral protease p15"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT SITE 239..240
FT /note="Cleavage; by viral protease p15"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT SITE 418
FT /note="Involved in capsid protein dimerization upon
FT acidification"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT SITE 430
FT /note="Involved in capsid protein dimerization upon
FT acidification"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT SITE 476..477
FT /note="Cleavage; by viral protease p15"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT SITE 479..480
FT /note="Cleavage; by viral protease p15"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT SITE 488..489
FT /note="Cleavage; by viral protease p15"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT SITE 577..578
FT /note="Cleavage; by viral protease p15"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT HELIX 255..268
FT /evidence="ECO:0007829|PDB:1D1D"
FT HELIX 274..283
FT /evidence="ECO:0007829|PDB:1D1D"
FT HELIX 289..299
FT /evidence="ECO:0007829|PDB:1D1D"
FT HELIX 302..325
FT /evidence="ECO:0007829|PDB:1D1D"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:1D1D"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:1D1D"
FT HELIX 342..346
FT /evidence="ECO:0007829|PDB:1D1D"
FT TURN 350..354
FT /evidence="ECO:0007829|PDB:1D1D"
FT HELIX 356..362
FT /evidence="ECO:0007829|PDB:1D1D"
FT HELIX 367..384
FT /evidence="ECO:0007829|PDB:1D1D"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:1D1D"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:1D1D"
FT HELIX 403..415
FT /evidence="ECO:0007829|PDB:1D1D"
FT TURN 421..425
FT /evidence="ECO:0007829|PDB:1D1D"
FT HELIX 426..432
FT /evidence="ECO:0007829|PDB:1D1D"
FT HELIX 438..445
FT /evidence="ECO:0007829|PDB:1D1D"
FT HELIX 456..465
FT /evidence="ECO:0007829|PDB:1D1D"
SQ SEQUENCE 701 AA; 74753 MW; 1004047C574057C7 CRC64;
MEAVIKVISS ACKTYCGKTS PSKKEIGAML SLLQKEGLLM SPSDLYSPGS WDPITAALSQ
RAMVLGKSGE LKTWGLVLGA LKAAREEQVT SEQAKFWLGL GGGRVSPPGP ECIEKPATER
RIDKGEEVGE TTVQRDAKMA PEETATPKTV GTSCYHCGTA IGCNCATASA PPPPYVGSGL
YPSLAGVGEQ QGQGGDTPRG AEQPRAEPGH AGLAPGPALT DWARIREELA STGPPVVAMP
VVIKTEGPAW TPLEPKLITR LADTVRTKGL RSPITMAEVE ALMSSPLLPH DVTNLMRVIL
GPAPYALWMD AWGVQLQTVI AAATRDPRHP ANGQGRGERT NLDRLKGLAD GMVGNPQGQA
ALLRPGELVA ITASALQAFR EVARLAEPAG PWADITQGPS ESFVDFANRL IKAVEGSDLP
PSARAPVIID CFRQKSQPDI QQLIRAAPST LTTPGEIIKY VLDRQKIAPL TDQGIAAAMS
SAIQPLVMAV VNRERDGQTG SGGRARRLCY TCGSPGHYQA QCPKKRKSGN SRERCQLCDG
MGHNAKQCRR RDSNQGQRPG RGLSSGPWPV SEQPAVSLAM TMEHKDRPLV RVILTNTGSH
PVKQRSVYIT ALLDSGADIT IISEEDWPTD WPVVDTANPQ IHGIGGGIPM RKSRDMIELG
VINRDGSLER PLLLFPAVAM VRGSILGRDC LQGLGLRLTN L
