VGLG_TRTV
ID VGLG_TRTV Reviewed; 391 AA.
AC P33495;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 23-FEB-2022, entry version 64.
DE RecName: Full=Major surface glycoprotein G;
DE AltName: Full=Attachment glycoprotein G;
GN Name=G;
OS Turkey rhinotracheitis virus (TRTV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Metapneumovirus.
OX NCBI_TaxID=11264;
OH NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1629697; DOI=10.1099/0022-1317-73-7-1709;
RA Ling R., Easton A.J., Pringle C.R.;
RT "Sequence analysis of the 22K, SH and G genes of turkey rhinotracheitis
RT virus and their intergenic regions reveals a gene order different from that
RT of other pneumoviruses.";
RL J. Gen. Virol. 73:1709-1715(1992).
CC -!- FUNCTION: It is likely to be the virus attachment protein.
CC -!- SUBCELLULAR LOCATION: Host cell surface. Virion membrane.
CC Note=Expressed on the surface of the infected cells and incorporated in
CC the membrane of the virions.
CC -!- PTM: May carry a lot of separate O-linked carbohydrate chains
CC distributed among serine and threonine residues. {ECO:0000250}.
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; S40185; AAB22547.1; -; mRNA.
DR PIR; JQ1626; JQ1626.
DR PRIDE; P33495; -.
DR GO; GO:0044228; C:host cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
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.
DR InterPro; IPR008781; Pneumo_att_G.
DR Pfam; PF05539; Pneumo_att_G; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Host-virus interaction; Membrane; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell; Virion;
KW Virus entry into host cell.
FT CHAIN 1..391
FT /note="Major surface glycoprotein G"
FT /id="PRO_0000142864"
FT TOPO_DOM 1..28
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..391
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT REGION 171..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 391 AA; 42981 MW; A2F82EAED76ABCC1 CRC64;
MGSKLYMVQG TSAYQTAVGF WLDIGRRYIL AIVLSAFGLT CTVTIALTVS VIVEQSVLEE
CRNYNGGDRD WWSTTQEQPT TAPSATPAGN YGGLQTARTR KSESCLHVQI SYGDMYSRSD
TVLGGFDCMG LLVLCKSGPI CQRDNQVDPT ALCHCRVDLS SVDCCKVNKI STNSSTTSEP
QKTNPAWPSQ DNTDSDPNPQ GITTSTATLL STSLGLMLTS KTGTHKSGPP QALPGSNTNG
KTTTDREPGP TNQPNSTTNG QHNKHTQRMT PPPSHDNTRT ILQHTTPWEK TFSTYKPTHS
PTNESDQSLP TTQNSINCEH FDPQGKEKIC YRVGSYNSNI TKQCRIDVPL CSTYSTVCMK
TYYTEPFNCW RRIWRCLCDD GVGLVEWCCT S
