ID   GLYC_GOGV               Reviewed;         427 AA.
AC   J7HBH4;
DT   31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Glycoprotein;
GN   Name=GPC; Synonyms=GP-C; OrderedLocusNames=Segment S;
OS   Alethinophid 1 reptarenavirus (isolate AlRrV1/Boa/USA/BC/2009) (Golden Gate
OS   virus).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Ellioviricetes; Bunyavirales; Arenaviridae; Reptarenavirus.
OX   NCBI_TaxID=1223562;
OH   NCBI_TaxID=8574; Boa constrictor (Boa).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22893382; DOI=10.1128/mbio.00180-12;
RA   Stenglein M.D., Sanders C., Kistler A.L., Ruby J.G., Franco J.Y.,
RA   Reavill D.R., Dunker F., Derisi J.L.;
RT   "Identification, characterization, and in vitro culture of highly divergent
RT   arenaviruses from bosysa constrictors and annulated tree boas: candidate
RT   etiological agents for snake inclusion body disease.";
RL   MBio 3:1-12(2012).
CC   -!- FUNCTION: mediates virus attachment to host receptor and fusion of
CC       viral and host membrane. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Glycoprotein]: Virion membrane {ECO:0000305}.
CC       Host cell membrane {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the reptarenavirus GPC protein family.
CC       {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; JQ717264; AFP93555.1; -; Genomic_RNA.
DR   RefSeq; YP_006590090.1; NC_018483.1.
DR   SMR; J7HBH4; -.
DR   GeneID; 13466439; -.
DR   KEGG; vg:13466439; -.
DR   Proteomes; UP000134698; 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:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Fusion of virus membrane with host endosomal membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein;
KW   Host cell membrane; Host membrane; Host-virus interaction; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix;
KW   Viral attachment to host cell; Viral envelope protein;
KW   Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT   CHAIN           1..427
FT                   /note="Glycoprotein"
FT                   /id="PRO_0000443034"
FT   TOPO_DOM        2..50
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        72..88
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        110..400
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        401..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        422..427
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        153
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        186
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        223
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        311
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        367
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   427 AA;  47176 MW;  C66D75F58463EFE7 CRC64;
     MMSHIRLVLC SALLSMMSCP TSGTIGEMLS LAASSNSSIC HGMQFTEPTE SFMGILPNET
     LPMFIFSIMH SEAVPKVGKT LRISHDMKLF GGEAVNYMIF VNKILYEPIS YYNYTGSCRQ
     QGLSSCVRVY SDLVNGSKGN PSVKLGFTAI ELNKTKNTDF HNLGFKICFS CRDHNGIRLV
     VYNKNNRTAQ LMMCPSELIF SQDFTINSTS VNPSEEAAVP LLNVTGYTCI ALHNKNMLTH
     HSPALSSGSK VDNTLEPGCD SNVGLFGHST GTDYGWGLAN FFSAGITNSL QISQLEHVTD
     AIACKIAKTS NYTTTALFLL NKEEGEIRDH VIEHEVALNY LLAHQGGLCS VVKGPMCCSD
     IDDFRRNVSD MIDKVHEEMK KFYHEPDPFG GLGTWGFYGT IFGHVLQWIP IIIMVVVVCF
     VCSWVRK