GGAG_FSVHZ
ID GGAG_FSVHZ Reviewed; 414 AA.
AC P0DP83;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2017, sequence version 1.
DT 02-JUN-2021, entry version 10.
DE RecName: Full=Glyco-Gag protein;
DE AltName: Full=Gross cell surface antigen;
DE AltName: Full=glycosylated Pr80 gag;
DE Short=gPr80 Gag;
DE Short=gag-gPr80;
OS Feline sarcoma virus (strain Hardy-Zuckerman 4).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX NCBI_TaxID=11777;
OH NCBI_TaxID=9681; Felidae (cat family).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3007997; DOI=10.1038/320415a0;
RA Besmer P., Murphy J.E., George P.C., Qiu F., Bergold P.J., Lederman L.,
RA Snyder H.W. Jr., Brodeur D., Zuckerman E.E., Hardy W.D.;
RT "A new acute transforming feline retrovirus and relationship of its
RT oncogene v-kit with the protein kinase gene family.";
RL Nature 320:415-421(1986).
CC -!- FUNCTION: Plays a role in viral particle release. Presumably acts by
CC facilitating the fission of the virion bud at the cell surface.
CC {ECO:0000250|UniProtKB:P0DOG8}.
CC -!- SUBCELLULAR LOCATION: Host cell membrane {ECO:0000250|UniProtKB:P0DOG8,
CC ECO:0000255}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P0DOG8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Glyco-Gag protein;
CC IsoId=P0DP83-1; Sequence=Displayed;
CC Name=Gag polyprotein;
CC IsoId=P04322-1; Sequence=External;
CC -!- PTM: Glycosylated by host. {ECO:0000250|UniProtKB:P0DOG8}.
CC -!- PTM: Cleaved by host near the middle of the molecule, releasing the c-
CC terminal half containing capsid and nucleoprotein domains op GAG.
CC {ECO:0000250|UniProtKB:P0DOG8}.
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DR EMBL; X03711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; P0DP83; -.
DR Proteomes; UP000242259; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019068; P:virion assembly; IEA:InterPro.
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; IPR002079; Gag_p12.
DR InterPro; IPR003036; Gag_P30.
DR InterPro; IPR008919; Retrov_capsid_N.
DR InterPro; IPR010999; Retrovr_matrix.
DR Pfam; PF01140; Gag_MA; 1.
DR Pfam; PF01141; Gag_p12; 1.
DR Pfam; PF02093; Gag_p30; 1.
DR SUPFAM; SSF47836; SSF47836; 1.
DR SUPFAM; SSF47943; SSF47943; 1.
PE 3: Inferred from homology;
KW Alternative initiation; Glycoprotein; Host cell membrane; Host membrane;
KW Membrane; Transmembrane; Transmembrane helix.
FT CHAIN 1..414
FT /note="Glyco-Gag protein"
FT /id="PRO_0000441133"
FT TOPO_DOM 1..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..414
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 171..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..192
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..247
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 414 AA; 45732 MW; 8B17A571FB5885F7 CRC64;
MSGASSGTAI GAHLFGVSPE CRVLIGDEGA GPSKSLSEVS FSVWYQSRAA RLVIFCLVAS
FLVPCLTFLI AETVMGQTIA TPLSLTLDHW SEVRARAHNQ GVEVRKKKWV TLCEAEWVMM
NVGWPREGTF SLDNISQVEK KIFAPGPYGH PDQVPYITTW RSLATDPPSW VRPFLPPPKP
PTPLPQPLSP QPSAPLTSSL YPVLPKTDPP KPPVLPPDPS SPLIDLLTEE PPPYPGGHGP
LPSGPRTPTA SPIASRLRER RENPAEESQA LPLREGPNNR PQYWPFSASD LYNWKSHNPP
FSQDPVALTN LIESILVTHQ PTWDDCQQLL QALLTGEERQ RVLLEARKQV PGEDGRPTQL
PNVIDETFPL TRPNWDFATP AGREHLRLYR QLLLAGLRGA ARRPTNLAQV KQVV