GG_SUHVR
ID GG_SUHVR Reviewed; 498 AA.
AC P07562;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Envelope glycoprotein G;
DE Short=gG;
DE Flags: Precursor;
GN Name=gG; OrderedLocusNames=70;
OS Suid herpesvirus 1 (strain Rice) (SuHV-1) (Pseudorabies virus (strain
OS Rice)).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10350;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2983115; DOI=10.1128/jvi.54.1.21-29.1985;
RA Rea T.J., Timmins J.G., Long G.W., Post L.E.;
RT "Mapping and sequence of the gene for the pseudorabies virus glycoprotein
RT which accumulates in the medium of infected cells.";
RL J. Virol. 54:21-29(1985).
CC -!- FUNCTION: Chemokine-binding protein that inhibits neutrophils'
CC chemotaxis. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the alphaherpesvirinae glycoprotein G family.
CC {ECO:0000305}.
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DR EMBL; M10986; AAC35206.1; -; Genomic_DNA.
DR PIR; A21879; VGBEGX.
DR RefSeq; YP_068386.1; NC_006151.1.
DR GeneID; 2952520; -.
DR KEGG; vg:2952520; -.
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:0039553; P:suppression by virus of host chemokine activity; IEA:UniProtKB-KW.
DR InterPro; IPR002896; Herpes_glycop_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR Pfam; PF01537; Herpes_glycop_D; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Host-virus interaction;
KW Inhibition of host chemokines by virus; Membrane; Repeat; Signal;
KW Transmembrane; Transmembrane helix; Viral envelope protein;
KW Viral immunoevasion; Virion.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..498
FT /note="Envelope glycoprotein G"
FT /id="PRO_0000115788"
FT TRANSMEM 463..483
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 271..292
FT /note="1"
FT REPEAT 308..329
FT /note="2"
FT REGION 271..329
FT /note="2 X 22 AA repeats of E-E-[DE]-[AE]-E-L-T-S-S-D-L-D-
FT N-I-E-I-E-V-V-G-S-P"
FT REGION 290..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..318
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 498 AA; 53722 MW; 17DEA180672A62DD CRC64;
MKWATWILAL GLLVVRTVVA REAPRELCYG HPVHDDRRPV GPATDAQPVN PLAPANATGT
DYSRGCEMRL LDPPLDVSSR SSDPVNVTVA WFFDGGHCKV PLVHREYYGC PGDAMPSVET
CTGGYSYTRT RIDTLMEYAL VNASLVLQPG LYDAGLYIVV LVFGDDAYLG TVSLSVEANL
DYPCGMKHGL TITRPGATLP PIAPTAGDHQ RWRGCFPSTD EGAWENVTAA EKGLSDDYAD
YYDVHIFRSE SDDEVVHGDA PEAPEGEEVT EEEAELTSSD LDNIEIEVVG SPAAPAEGPA
TEEGRGAEED EELTSSDLDN IEIEVVGSPR PPASSPPPPP PRPHPRGRDH DHDHGHHRAD
DRGPQRHHRL PPEPTFVSPS DIFVTPTGSP ALLLGFLGSA LASRPLHLTA GETAQHVREA
QQKSRHIRSL GGLQLSVETE TTNTTTTQTG LSGDIRTSIY ICVALAGLVV VGIVIMCLHM
AIIRARARND GYRHVASA