ID   GC_GAHVM                Reviewed;         501 AA.
AC   P22651; Q6LAR3; Q77MR8;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   29-SEP-2021, entry version 107.
DE   RecName: Full=Envelope glycoprotein C homolog;
DE   AltName: Full=A antigen;
DE   AltName: Full=Glycoprotein A;
DE            Short=GA;
DE   AltName: Full=Secretory glycoprotein GP57-65;
DE   Flags: Precursor;
GN   Name=gC; ORFNames=GA;
OS   Gallid herpesvirus 2 (strain Chicken/Md5/ATCC VR-987) (GaHV-2) (Marek's
OS   disease herpesvirus type 1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX   NCBI_TaxID=10389;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2559540; DOI=10.1007/bf00125125;
RA   Ihara T., Kato A., Ueda S., Ishihama A., Hirai K.;
RT   "Comparison of the sequence of the secretory glycoprotein A (gA) gene in
RT   Md5 and BC-1 strains of Marek's disease virus type 1.";
RL   Virus Genes 3:127-140(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10933706; DOI=10.1128/jvi.74.17.7980-7988.2000;
RA   Tulman E.R., Afonso C.L., Lu Z., Zsak L., Rock D.L., Kutish G.F.;
RT   "The genome of a very virulent Marek's disease virus.";
RL   J. Virol. 74:7980-7988(2000).
CC   -!- FUNCTION: May play an immunoevasive role in the pathogenesis of Marek's
CC       disease. It is a candidate for causing the early-stage
CC       immunosuppression that occurs after MDHV infection.
CC   -!- SUBCELLULAR LOCATION: Secreted. Host cell membrane; Single-pass
CC       membrane protein. Note=Predominantly secreted. Secreted, but a small
CC       amount of mature GP57-65 is anchored in the plasma membrane or held by
CC       other interactions.
CC   -!- SIMILARITY: Belongs to the herpesviridae glycoprotein C family.
CC       {ECO:0000305}.
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DR   EMBL; D90001; BAA14052.1; -; Genomic_DNA.
DR   EMBL; AF243438; AAG14237.1; -; Genomic_DNA.
DR   RefSeq; YP_001033973.1; NC_002229.3.
DR   PRIDE; P22651; -.
DR   GeneID; 4811518; -.
DR   KEGG; vg:4811518; -.
DR   Proteomes; UP000008072; Genome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   InterPro; IPR001038; GA_GC.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR001654; Marek_A.
DR   Pfam; PF02124; Marek_A; 1.
DR   PRINTS; PR00675; MAREKSGPA.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Host cell membrane; Host membrane; Host-virus interaction;
KW   Immunoglobulin domain; Membrane; Reference proteome; Secreted; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..501
FT                   /note="Envelope glycoprotein C homolog"
FT                   /id="PRO_0000038209"
FT   TOPO_DOM        28..465
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        466..492
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        493..501
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          258..356
FT                   /note="Ig-like"
FT   REGION          53..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..86
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        120
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        212
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        354
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        400
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        429
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   501 AA;  56089 MW;  4393C56AA779340A CRC64;
     MLTPRVLRAL GWTGLFFLLL SPSNVLGASL SRDLETPPFL SFDPSNISIN GAPLTEVPHA
     PSTESVSTNS ESTNEHTITE TTGKNAYIHN NASTDKQNAN DTHKTPNILC DTEEVFVFLN
     ETGRFVCTLK VDPPSDSEWS NFVLDLIFNP IEYHANEKNV EAARIAGLYG VPGSDYAYPR
     QSELISSIRR DPQGTFWTSP SPHGNKYFIW INKTTNTMGV EIRNVDYADN GYMQVIMRDH
     FNRPLIDKHI YIRVCQRPAS VDVLAPPVLS GENYKASCIV RHFYPPGSVY VSWRQNGNIA
     TPRKDRDGSF WWFESGRGAT LVSTITLGNS GIDFPPKISC LVAWKQGDMI STTNATAIPT
     VYHHPRLSLA FKDGYAICTI ECVPSEITVR WLVHDEAQPN TTYNTVVTGL CRTIDRHRNL
     LSRIPVWDNW TKTKYTCRLI GYPFDEDKFQ DSEYYDATPA ARGTPMVITV TAVLGLAVIL
     GMGIIMTALC LYNSTRKNIR L