ID   GAG_VILVK               Reviewed;         442 AA.
AC   P35955;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   23-FEB-2022, entry version 99.
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 KV1772) (MVV) (Visna lentivirus).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=36374;
OH   NCBI_TaxID=9940; Ovis aries (Sheep).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8382414; DOI=10.1006/viro.1993.1106;
RA   Andresson O.S., Elser J.E., Tobin G.J., Greenwood J.D., Gonda M.A.,
RA   Georgsson G., Andresdottir V., Benediktsdottir E., Carlsdottir H.M.,
RA   Maentylae E.O., Rafnar B., Palsson P.A., Casey J.W., Petursson G.;
RT   "Nucleotide sequence and biological properties of a pathogenic proviral
RT   molecular clone of neurovirulent visna virus.";
RL   Virology 193:89-105(1993).
RN   [2]
RP   PROTEOLYTIC CLEAVAGE (GAG POLYPROTEIN).
RX   PubMed=14694086; DOI=10.1128/jvi.78.2.551-560.2004;
RA   Guo X., Hu J., Whitney J.B., Russell R.S., Liang C.;
RT   "Important role for the CA-NC spacer region in the assembly of bovine
RT   immunodeficiency virus Gag protein.";
RL   J. Virol. 78:551-560(2004).
RN   [3]
RP   RIBOSOMAL FRAMESHIFTING.
RX   PubMed=18495941; DOI=10.1261/rna.1042108;
RA   Pennell S., Manktelow E., Flatt A., Kelly G., Smerdon S.J., Brierley I.;
RT   "The stimulatory RNA of the Visna-Maedi retrovirus ribosomal frameshifting
RT   signal is an unusual pseudoknot with an interstem element.";
RL   RNA 14:1366-1377(2008).
CC   -!- FUNCTION: [Isoform Gag polyprotein]: Mediates, with Gag-Pol
CC       polyprotein, the essential events in virion assembly, including binding
CC       the plasma membrane, making the protein-protein interactions necessary
CC       to create spherical particles, recruiting the viral Env proteins, and
CC       packaging the genomic RNA via direct interactions with the RNA
CC       packaging 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=P35955-1; Sequence=Displayed;
CC       Name=Gag-Pol polyprotein;
CC         IsoId=P35956-1; 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: [Isoform Gag polyprotein]: Specific enzymatic cleavages by the
CC       viral protease yield mature proteins. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform Gag polyprotein]: Produced by conventional
CC       translation. {ECO:0000305|PubMed:18495941}.
CC   -!- SIMILARITY: Belongs to the Ovine/caprine lentivirus group gag
CC       polyprotein family. {ECO:0000305}.
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DR   EMBL; L06906; AAA48358.1; -; Genomic_RNA.
DR   EMBL; S55323; AAB25459.1; -; Genomic_DNA.
DR   SMR; P35955; -.
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   1: Evidence at protein level;
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..143
FT                   /note="Matrix protein p16"
FT                   /id="PRO_0000038808"
FT   CHAIN           144..363
FT                   /note="Capsid protein p25"
FT                   /id="PRO_0000038809"
FT   CHAIN           364..442
FT                   /note="Nucleocapsid protein p14"
FT                   /id="PRO_0000038810"
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:0000305|PubMed:14694086"
SQ   SEQUENCE   442 AA;  49857 MW;  55EE18E951B486FA 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 ALRPQGKAGQ KGVNQKCYNC GKPGHLARQC RQGIICHHCG KRGHMQKDCR
     QKKQQGNNRR GPRVVPSAPP ML