GAG_AVISN
ID GAG_AVISN Reviewed; 313 AA.
AC P03342;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 02-JUN-2021, entry version 91.
DE RecName: Full=Gag polyprotein;
DE AltName: Full=Core polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p15;
DE Short=MA;
DE Contains:
DE RecName: Full=RNA-binding phosphoprotein p12;
DE AltName: Full=pp12;
DE Contains:
DE RecName: Full=Capsid protein p30;
DE Short=CA;
DE Flags: Fragment;
GN Name=gag;
OS Avian spleen necrosis virus.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX NCBI_TaxID=11899;
OH NCBI_TaxID=8976; Galliformes.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (PROVIRUS).
RX PubMed=6951170; DOI=10.1073/pnas.79.4.1230;
RA O'Rear J.J., Temin H.M.;
RT "Spontaneous changes in nucleotide sequence in proviruses of spleen
RT necrosis virus, an avian retrovirus.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:1230-1234(1982).
RN [2]
RP PROTEIN SEQUENCE OF 200-235.
RX PubMed=6169843; DOI=10.1128/jvi.39.3.845-854.1981;
RA Oroszlan S., Barbacid M., Copeland T.D., Aaronson S.A., Gilden R.V.;
RT "Chemical and Immunological characterization of the major structural
RT protein (p28) of MMC-1, a rhesus monkey endogenous type C virus: homology
RT with the major structural protein of avian reticuloendotheliosis virus.";
RL J. Virol. 39:845-854(1981).
CC -!- FUNCTION: Gag polyprotein plays a role in budding and is processed by
CC the viral protease during virion maturation outside the cell. During
CC budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-
CC like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to
CC Gag binding host factors. Interaction with HECT ubiquitin ligases
CC probably link the viral protein to the host ESCRT pathway and
CC facilitate release (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Matrix protein p15 targets Gag and gag-pol polyproteins to
CC the plasma membrane via a multipartite membrane binding signal, that
CC includes its myristoylated N-terminus. Also mediates nuclear
CC localization of the preintegration complex (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: Capsid protein p30 forms the spherical core of the virion
CC that encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000250}.
CC -!- FUNCTION: Nucleocapsid protein p10 is involved in the packaging and
CC encapsidation of two copies of the genome. Binds with high affinity to
CC conserved elements within the packaging signal, located near the 5'-end
CC of the genome. This binding is dependent on genome dimerization (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Capsid protein p30 is a homohexamer, that further associates
CC as homomultimer. The virus core is composed of a lattice formed from
CC hexagonal rings, each containing six capsid monomers (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Gag polyprotein]: Virion {ECO:0000250}. Host
CC cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p15]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p30]: Virion {ECO:0000305}.
CC -!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
CC essential for viral particle budding. They recruit proteins of the host
CC ESCRT machinery (Endosomal Sorting Complex Required for Transport) or
CC ESCRT-associated proteins. RNA-binding phosphoprotein p12 contains one
CC L domain: a PPXY motif which potentially interacts with the WW domain 3
CC of NEDD4 E3 ubiquitin ligase. Matrix protein p15 contains one L domain:
CC a PTAP/PSAP motif, which potentially interacts with the UEV domain of
CC TSG101 (By similarity). {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages by the viral protease yield mature
CC proteins. The protease is released by autocatalytic cleavage. The
CC polyprotein is cleaved during and after budding, this process is termed
CC maturation (By similarity). {ECO:0000250}.
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DR EMBL; V01200; CAA24513.1; -; Genomic_DNA.
DR PIR; A93904; FOVDA.
DR SMR; P03342; -.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.180; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR InterPro; IPR000840; G_retro_matrix.
DR InterPro; IPR036946; G_retro_matrix_sf.
DR InterPro; IPR003036; Gag_P30.
DR InterPro; IPR008919; Retrov_capsid_N.
DR InterPro; IPR010999; Retrovr_matrix.
DR Pfam; PF01140; Gag_MA; 1.
DR Pfam; PF02093; Gag_p30; 1.
DR SUPFAM; SSF47836; SSF47836; 1.
DR SUPFAM; SSF47943; SSF47943; 1.
PE 1: Evidence at protein level;
KW Capsid protein; Direct protein sequencing; Host cell membrane;
KW Host membrane; Host-virus interaction; Lipoprotein; Membrane; Myristate;
KW RNA-binding; Viral budding; Viral budding via the host ESCRT complexes;
KW Viral matrix protein; Viral nucleoprotein; Viral release from host cell;
KW Virion.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250"
FT CHAIN 2..>313
FT /note="Gag polyprotein"
FT /id="PRO_0000390796"
FT CHAIN 2..?
FT /note="Matrix protein p15"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040821"
FT CHAIN ?..199
FT /note="RNA-binding phosphoprotein p12"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040822"
FT CHAIN 200..>313
FT /note="Capsid protein p30"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040823"
FT REGION 113..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 127..130
FT /note="PTAP/PSAP motif"
FT MOTIF 154..157
FT /note="PPXY motif"
FT COMPBIAS 168..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
FT CONFLICT 210
FT /note="T -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="S -> F (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 313
SQ SEQUENCE 313 AA; 35362 MW; 6712FE769E57C45A CRC64;
MGQAGSKGLL TPLECILKNF SDFKKRAGDY GEDVDSFALR KLCELEWPTF GVGWPKEGTL
DFKVVAAVRN IVFGNPGHPD QVIYITVWTD ITIERPKYLK SCGCKPHRTS KVLLASQKVN
PRRPVLPSAP ESPPRIRRAQ FLDERPLSPA PAPPPPYPEV SAIVEDTREG QQPDSTVMTS
PPHTRSGLEF GAQGPSGMYP LRETGERDMT GRPMRTYVPF TTSDLYNWKN QNPSSFSQAP
DQVISLLESV FYTHQPTWDD CQQLLRTLFT TEERERVRTE SRREVRNDQG VQVTDEREIE
AQFPATRPDW VGS
