GAG_VILV2
ID GAG_VILV2 Reviewed; 442 AA.
AC P23425;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 23-FEB-2022, entry version 96.
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 / clone LV1-1KS2) (MVV) (Visna lentivirus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11744;
OH NCBI_TaxID=9940; Ovis aries (Sheep).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1847257; DOI=10.1016/0042-6822(91)90488-w;
RA Staskus K.A., Retzel E.F., Lewis E.D., Wietgrefe S.W., Silsby J.L., Cyr S.,
RA Rank J.M., Haase A.T., Fast D., Geiser P.T., Harty J.T., Kong S.H.,
RA Cook R., Lahti C.J., Neufeld T.P., Porter T.E., Shoop E., Zachow K.R.;
RT "Isolation of replication-competent molecular clones of visna virus.";
RL Virology 181:228-240(1991).
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=P23425-1; Sequence=Displayed;
CC Name=Gag-Pol polyprotein;
CC IsoId=P23427-1; 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=AAA17528.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; M60610; AAA17528.1; ALT_INIT; Unassigned_DNA.
DR SMR; P23425; -.
DR TCDB; 1.G.7.1.1; the reovirus fast fusion protein (r-fast) family.
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_0000443357"
FT CHAIN 1..143
FT /note="Matrix protein p16"
FT /id="PRO_0000038805"
FT CHAIN 144..363
FT /note="Capsid protein p25"
FT /id="PRO_0000038806"
FT CHAIN 364..442
FT /note="Nucleocapsid protein p14"
FT /id="PRO_0000038807"
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; 49915 MW; 4713CBC1ED0EECB2 CRC64;
MAKQGSKEKK GYPELKEVIK ATCKIRVGPG KETLTEGNCL WALKTIDFIF EDLKTEPWTI
TKMYTVWDRL KGLTPEETSK REFASLQATL ACIMCSQMGM KPETVQAAKG IISMKEGLQE
NKEAKGEKVE QLYPNLEKHR EVYPIVNLQA GGRSWKAVES VVFQQLQTVA MQHGLVSEDF
ERQLAYYATT WTSKDILEVL VMMPGNRAQK ELIQGKLNEE AERWVRQNPP GPNVLTVDQI
MGVGQTNQQA SQANMDQARQ ICLQWVITAL RSVRHMSHRP GNPMLVKQKN TESYEDFIAR
LLEAIDAEPV MDPIKTYLKV TLSYTNASTD CQKQMDRTLG TRVQQATVEE KMQACRDVGS
EGFKMQLLAQ ALRPQGKAGH KGVNQKCYNC GKPGHLARQC RQGIICHHCG KRGHMQKDCR
QKKQQGNNRR GPRVVPSAPP ML
