ID   GAG_VILV                Reviewed;         442 AA.
AC   P03352;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   23-FEB-2022, entry version 103.
DE   RecName: Full=Gag polyprotein;
DE   Contains:
DE     RecName: Full=Matrix protein p16;
DE   Contains:
DE     RecName: Full=Capsid protein p25;
DE   Contains:
DE     RecName: Full=Nucleocapsid protein p14;
GN   Name=gag;
OS   Maedi visna virus (strain 1514) (MVV) (Visna lentivirus).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11742;
OH   NCBI_TaxID=9940; Ovis aries (Sheep).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2410140; DOI=10.1016/s0092-8674(85)80132-x;
RA   Sonigo P., Alizon M., Staskus K., Klatzmann D., Cole S., Danos O.,
RA   Retzel E., Tiollais P., Haase A., Wain-Hobson S.;
RT   "Nucleotide sequence of the visna lentivirus: relationship to the AIDS
RT   virus.";
RL   Cell 42:369-382(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2824836; DOI=10.1128/jvi.61.12.4046-4054.1987;
RA   Braun M.J., Clements J.E., Gonda M.A.;
RT   "The visna virus genome: evidence for a hypervariable site in the env gene
RT   and sequence homology among lentivirus envelope proteins.";
RL   J. Virol. 61:4046-4054(1987).
CC   -!- FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the
CC       essential events in virion assembly, including binding the plasma
CC       membrane, making the protein-protein interactions necessary to create
CC       spherical particles, recruiting the viral Env proteins, and packaging
CC       the genomic RNA via direct interactions with the RNA packaging
CC       sequence. {ECO:0000250|UniProtKB:P04585}.
CC   -!- FUNCTION: [Matrix protein p16]: Targets the polyprotein to the plasma
CC       membrane. {ECO:0000250|UniProtKB:P12497}.
CC   -!- FUNCTION: [Capsid protein p25]: Forms the core that encapsulates the
CC       genomic RNA-nucleocapsid complex in the virion.
CC       {ECO:0000250|UniProtKB:P04585}.
CC   -!- FUNCTION: [Nucleocapsid protein p14]: Encapsulates and protects viral
CC       dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc
CC       fingers. Acts as a nucleic acid chaperone which is involved in
CC       rearrangement of nucleic acid secondary structure during gRNA
CC       retrotranscription. Also facilitates template switch leading to
CC       recombination. {ECO:0000250|UniProtKB:P04585}.
CC   -!- SUBCELLULAR LOCATION: [Matrix protein p16]: Virion {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein p25]: Virion {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p14]: Virion {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC       Name=Gag polyprotein;
CC         IsoId=P03352-1; Sequence=Displayed;
CC       Name=Gag-Pol polyprotein;
CC         IsoId=P03370-1; Sequence=External;
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. Nucleocapsid protein p14 contains one L
CC       domain: a PTAP/PSAP motif, which interacts with the UEV domain of
CC       TSG101. {ECO:0000305}.
CC   -!- PTM: [Gag polyprotein]: Specific enzymatic cleavages by the viral
CC       protease yield mature proteins. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform Gag polyprotein]: Produced by conventional
CC       translation. {ECO:0000250|UniProtKB:P35956}.
CC   -!- SIMILARITY: Belongs to the Ovine/caprine lentivirus group gag
CC       polyprotein family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA17520.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; M10608; AAA17520.1; ALT_INIT; Unassigned_DNA.
DR   EMBL; A15114; CAA01213.1; -; Unassigned_RNA.
DR   SMR; P03352; -.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; 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; 1.10.375.10; -; 1.
DR   InterPro; IPR045345; Gag_p24_C.
DR   InterPro; IPR000721; Gag_p24_N.
DR   InterPro; IPR008916; Retrov_capsid_C.
DR   InterPro; IPR008919; Retrov_capsid_N.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   Pfam; PF00607; Gag_p24; 1.
DR   Pfam; PF19317; Gag_p24_C; 1.
DR   Pfam; PF00098; zf-CCHC; 2.
DR   SMART; SM00343; ZnF_C2HC; 2.
DR   SUPFAM; SSF47943; SSF47943; 1.
DR   SUPFAM; SSF57756; SSF57756; 1.
DR   PROSITE; PS50158; ZF_CCHC; 2.
PE   3: Inferred from homology;
KW   Capsid protein; Host-virus interaction; Metal-binding; Repeat;
KW   Ribosomal frameshifting; Viral budding;
KW   Viral budding via the host ESCRT complexes; Viral release from host cell;
KW   Virion; Zinc; Zinc-finger.
FT   CHAIN           1..442
FT                   /note="Gag polyprotein"
FT                   /id="PRO_0000443355"
FT   CHAIN           1..143
FT                   /note="Matrix protein p16"
FT                   /id="PRO_0000038799"
FT   CHAIN           144..363
FT                   /note="Capsid protein p25"
FT                   /id="PRO_0000038800"
FT   CHAIN           364..442
FT                   /note="Nucleocapsid protein p14"
FT                   /id="PRO_0000038801"
FT   ZN_FING         385..402
FT                   /note="CCHC-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   ZN_FING         404..421
FT                   /note="CCHC-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   REGION          420..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           436..439
FT                   /note="PTAP/PSAP motif"
FT   SITE            363..364
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P35955"
SQ   SEQUENCE   442 AA;  49866 MW;  55F93FD951B49FE3 CRC64;
     MAKQGSKEKK GYPELKEVIK ATCKIRVGPG KETLTEGNCL WALKTIDFIF EDLKTEPWTI
     TKMYTVWDRL KGLTPEETSK REFASLQATL ACIMCSQMGM KPETVQAAKG IISMKEGLHE
     NKEAKGEKVE QLYPNLEKHR EVYPIVNLQA GGRSWKAVES VVFQQLQTVA MQHGLVSEDF
     ERQLAYYATT WTSKDILEVL AMMPGNRAQK ELIQGKLNEE AERWVRQNPP GPNVLTVDQI
     MGVGQTNQQA SQANMDQARQ ICLQWVITAL RSVRHMSHRP GNPMLVKQKN TESYEDFIAR
     LLEAIDAEPV TDPIKTYLKV TLSYTNASTD CQKQMDRTLG TRVQQATVEE KMQACRDVGS
     EGFKMQLLAQ ALRPQGKAGH KGVNQKCYNC GKPGHLARQC RQGIICHHCG KRGHMQKDCR
     QKKQQGNNRR GPRVVPSAPP ML