GAG_SMRVH
ID GAG_SMRVH Reviewed; 740 AA.
AC P21411;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 23-FEB-2022, entry version 98.
DE RecName: Full=Gag polyprotein;
DE AltName: Full=Core polyprotein;
DE AltName: Full=Pr72;
DE Contains:
DE RecName: Full=Matrix protein p19;
DE Contains:
DE RecName: Full=Core protein p16;
DE Contains:
DE RecName: Full=Capsid protein p35;
DE AltName: Full=Capsid protein p34;
DE Contains:
DE RecName: Full=Probable nucleocapsid protein p10;
GN Name=gag;
OS Squirrel monkey retrovirus (SMRV-H) (SMRV-HLB).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus.
OX NCBI_TaxID=11856;
OH NCBI_TaxID=40674; Mammalia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], PROTEIN SEQUENCE OF 319-346, AND
RP PROTEOLYTIC CLEAVAGE (GAG POLYPROTEIN).
RX PubMed=3201749; DOI=10.1016/s0042-6822(88)90109-2;
RA Oda T., Ikeda S., Watanabe S., Hatsushika M., Akiyama K., Mitsunobu F.;
RT "Molecular cloning, complete nucleotide sequence, and gene structure of the
RT provirus genome of a retrovirus produced in a human lymphoblastoid cell
RT line.";
RL Virology 167:468-476(1988).
RN [2]
RP PROTEOLYTIC CLEAVAGE (GAG POLYPROTEIN).
RX PubMed=448794; DOI=10.1128/jvi.29.3.1035-1043.1979;
RA Devare S.G., Stephenson J.R.;
RT "Primate retroviruses: intracistronic mapping of type D viral gag gene by
RT use of nonconditional replication mutants.";
RL J. Virol. 29:1035-1043(1979).
RN [3]
RP RIBOSOMAL FRAMESHIFT.
RX PubMed=24298557; DOI=10.1155/2013/984028;
RA Huang X., Cheng Q., Du Z.;
RT "A genome-wide analysis of RNA pseudoknots that stimulate efficient -1
RT ribosomal frameshifting or readthrough in animal viruses.";
RL Biomed. Res. Int. 2013:984028-984028(2013).
CC -!- FUNCTION: Matrix protein p10: Matrix protein. {ECO:0000305}.
CC -!- FUNCTION: Nucleocapsid protein p14: Nucleocapsid protein.
CC {ECO:0000305}.
CC -!- FUNCTION: Capsid protein p27: capsid protein. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p35]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=3;
CC Name=Gag polyprotein;
CC IsoId=P21411-1; Sequence=Displayed;
CC Name=Gag-Pro polyprotein;
CC IsoId=P21407-1; Sequence=External;
CC Name=Gag-Pro-Pol polyprotein;
CC IsoId=P03364-1; 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 Gag-p35 contains one L domain: a PTAP/PSAP motif, which interacts with
CC the UEV domain of TSG101 (Potential). {ECO:0000305}.
CC -!- PTM: [Gag polyprotein]: Myristoylated. Myristoylation of the matrix
CC (MA) domain mediates the transport and binding of Gag polyproteins to
CC the host plasma membrane and is required for the assembly of viral
CC particles. {ECO:0000250|UniProtKB:P10258}.
CC -!- PTM: [Gag polyprotein]: Specific enzymatic cleavages in vivo yield
CC mature proteins. {ECO:0000269|PubMed:448794,
CC ECO:0000305|PubMed:3201749}.
CC -!- MISCELLANEOUS: [Isoform Gag polyprotein]: Produced by conventional
CC translation. {ECO:0000305|PubMed:24298557}.
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DR EMBL; M23385; AAA66451.1; -; Genomic_RNA.
DR PIR; A31827; FOLJHD.
DR RefSeq; NP_041259.1; NC_001514.1. [P21411-1]
DR SMR; P21411; -.
DR GeneID; 1491964; -.
DR KEGG; vg:1491964; -.
DR Proteomes; UP000007223; Genome.
DR GO; GO:0019013; C:viral nucleocapsid; 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:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.30; -; 1.
DR Gene3D; 1.10.150.490; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR InterPro; IPR003322; B_retro_matrix.
DR InterPro; IPR038124; B_retro_matrix_sf.
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; IPR010999; Retrovr_matrix.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF02337; Gag_p10; 1.
DR Pfam; PF00607; Gag_p24; 1.
DR Pfam; PF19317; Gag_p24_C; 1.
DR SUPFAM; SSF47836; SSF47836; 1.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
PE 1: Evidence at protein level;
KW Capsid protein; Direct protein sequencing; Host-virus interaction;
KW Lipoprotein; Myristate; Phosphoprotein; Repeat; Ribosomal frameshifting;
KW 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:0000255"
FT CHAIN 2..740
FT /note="Gag polyprotein"
FT /id="PRO_0000443125"
FT CHAIN 2..163
FT /note="Matrix protein p19"
FT /id="PRO_0000040956"
FT CHAIN 164..318
FT /note="Core protein p16"
FT /id="PRO_0000040957"
FT CHAIN 319..648
FT /note="Capsid protein p35"
FT /id="PRO_0000040958"
FT CHAIN 649..740
FT /note="Probable nucleocapsid protein p10"
FT /id="PRO_0000040959"
FT REGION 115..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 396..399
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000255"
FT COMPBIAS 119..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..366
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 163..164
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000305|PubMed:3201749"
FT SITE 318..319
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000305|PubMed:3201749"
FT SITE 648..649
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000305|PubMed:3201749"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 740 AA; 80543 MW; CC2503C2661221F5 CRC64;
MGQASSHSEN DLFISHLKES LKVRRIRVRK KDLVSFFSFI FKTCPWFPQE GSIDSRVWGR
VGDCLNDYYR VFGPETIPIT TFNYYNLIRD VLTNQSDSPD IQRLCKEGHK ILISHSRPPS
RQAPVTITTS EKASSRPPSR APSTCPSVAI DIGSHDTGQS SLYPNLATLT DPPIQSPHSR
AHTPPQHLPL LANSKTLHNS GSQDDQLNPA DQADLEEAAA QYNNPDWPQL TNTPALPPFR
PPSYVSTAVP PVAVAAPVLH APTSGVPGSP TAPNLPGVAL AKPSGPIDET VSLLDGVKTL
VTKLSDLALL PPAGVMAFPV TRSQGQVSSN TTGRASPHPD THTIPEEEEA DSGESDSEDD
EEESSEPTEP TYTHSYKRLN LKTIEKIKTA VANYGPTAPF TVALVESLSE RWLTPSDWFF
LSRAALSGGD NILWKSEYED ISKQFAERTR VRPPPKDGPL KIPGASPYQN NDKQAQFPPG
LLTQIQSAGL KAWKRLPQKG AATTSLAKIR QGPDESYSDF VSRLQETADR LFGSGESESS
FVKHLAYENA NPACQSAIRP FRQKELSTMS PLLWYCSAHA VGLAIGAALQ NLAPAQLLEP
RPAFAIIVTN PAIFQETAPK KIQPPTQLPT QPNAPQASLI KNLGPTTKCP RCKKGFHWAS
ECRSRLDING QPIIKQGNLN RGQPQGPTTG MNSGASQFTP QYRQPTPALP VINHAATSQT
SGEQQRAVQD WTSVPPPTQY
