VGLG_AMPV1
ID VGLG_AMPV1 Reviewed; 585 AA.
AC Q2Y2L9;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 02-JUN-2021, entry version 42.
DE RecName: Full=Major surface glycoprotein G;
DE AltName: Full=Attachment glycoprotein G;
DE AltName: Full=Membrane-bound glycoprotein;
DE Short=mG;
GN Name=G;
OS Avian metapneumovirus (isolate Canada goose/Minnesota/15a/2001) (AMPV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Metapneumovirus.
OX NCBI_TaxID=652954;
OH NCBI_TaxID=8847; Anser sp. (goose).
OH NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15666873; DOI=10.1637/7208-051804r;
RA Bennett R.S., Nezworski J., Velayudhan B.T., Nagaraja K.V., Zeman D.H.,
RA Dyer N., Graham T., Lauer D.C., Njenga M.K., Halvorson D.A.;
RT "Evidence of avian pneumovirus spread beyond Minnesota among wild and
RT domestic birds in central North America.";
RL Avian Dis. 48:902-908(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16282483; DOI=10.1128/jvi.79.23.14834-14842.2005;
RA Bennett R.S., LaRue R., Shaw D., Yu Q., Nagaraja K.V., Halvorson D.A.,
RA Njenga M.K.;
RT "A wild goose metapneumovirus containing a large attachment glycoprotein is
RT avirulent but immunoprotective in domestic turkeys.";
RL J. Virol. 79:14834-14842(2005).
CC -!- FUNCTION: Attaches the virion to the host cell membrane initiating the
CC infection. Unlike the other paramyxovirus attachment proteins, lacks
CC both neuraminidase and hemagglutinating activities (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer. Interacts (via N-terminus) with protein M.
CC Interacts with protein F; this interaction occurs on the surface of
CC infected cells. Interacts with protein SH (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion membrane. Host cell surface {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the metapneumoviruses glycoprotein G family.
CC {ECO:0000305}.
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DR EMBL; DQ009484; AAY81661.1; -; Viral_cRNA.
DR RefSeq; YP_443844.1; NC_007652.1.
DR Proteomes; UP000002471; Genome.
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.
PE 3: Inferred from homology;
KW Glycoprotein; Host-virus interaction; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Viral attachment to host cell; Virion;
KW Virus entry into host cell.
FT CHAIN 1..585
FT /note="Major surface glycoprotein G"
FT /id="PRO_0000390372"
FT TOPO_DOM 1..31
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..299
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT REGION 67..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 570
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 585 AA; 64514 MW; CE01B50B8E0DD76B CRC64;
MEVKVENVGK SQELKVKVKN FIKRSDCKKK LFALILGLVS FELTMNIMLS VMYVESNEAL
SLCRIQGTPA PRDNKTNTEN TKKETTFHTT TTTRDPEVRE TKTTKPKTNE GATSPSRNLT
TKGDIHQTTR ATTEAELEKQ SKQTIEPDTS TKKHTPTRPS SESPTTTQAT AQLTTPTAPK
ASIAPKNRQA TTKKTETGTT TTSRAKKTNN PTETATTTLK ATTETGKGKE GPTQHTIKEQ
PETTAGETTT PQSRRTTSRP APTTKTEEEA ETTKTRTTKS TQTSTGPPGP TRSTPSKTAT
ENNKRTTTIK RPNTANTDSR QQTRTTAEQD RQIQTKAKPT TNGAHAQTTT TPEHNTDTTN
STKESSKEDK TTRDPSSKTP TDQEDASKGT TAANPRKNTE ANTRTPPTTT PTRHTTESAT
STTGDKTKAK TTRWKSTADR QPIRNSTTAE TKTAQSKQPT PKQLSNNTTP ENTTPPNNKS
SSQTDAAPTE EIEIRSSLWR RRYVYGPCRE NVLEHPMNPC FKDNTTWIYS DNGRNLPAGY
YDSKTDKIIC YGIYRGNSYC YGRIECTCKN GTGLLSYCCN SYNWS
