ID   VNB_INBLE               Reviewed;         100 AA.
AC   P06817;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   23-FEB-2022, entry version 88.
DE   RecName: Full=Glycoprotein NB;
GN   Name=NB;
OS   Influenza B virus (strain B/Lee/1940).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Betainfluenzavirus.
OX   NCBI_TaxID=518987;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6294654; DOI=10.1073/pnas.79.22.6817;
RA   Shaw M.W., Lamb R.A., Erickson B.W., Briedis D.J., Choppin P.W.;
RT   "Complete nucleotide sequence of the neuraminidase gene of influenza B
RT   virus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 79:6817-6821(1982).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6308656; DOI=10.1073/pnas.80.16.4879;
RA   Shaw M.W., Choppin P.W., Lamb R.A.;
RT   "A previously unrecognized influenza B virus glycoprotein from a
RT   bicistronic mRNA that also encodes the viral neuraminidase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:4879-4883(1983).
RN   [3]
RP   TOPOLOGY.
RX   PubMed=3025652; DOI=10.1128/mcb.6.12.4317-4328.1986;
RA   William M.A., Lamb R.A.;
RT   "Determination of the orientation of an integral membrane protein and sites
RT   of glycosylation by oligonucleotide-directed mutagenesis: influenza B virus
RT   NB glycoprotein lacks a cleavable signal sequence and has an extracellular
RT   NH2-terminal region.";
RL   Mol. Cell. Biol. 6:4317-4328(1986).
RN   [4]
RP   FUNCTION, AND MUTAGENESIS OF SER-20; THR-24; CYS-26 AND SER-28.
RX   PubMed=15042345; DOI=10.1007/s00232-004-0648-0;
RA   Premkumar A., Ewart G.D., Cox G.B., Gage P.W.;
RT   "An amino-acid substitution in the influenza-B NB protein affects ion-
RT   channel gating.";
RL   J. Membr. Biol. 197:135-143(2004).
RN   [5]
RP   TOPOLOGY.
RX   PubMed=8922461; DOI=10.1099/0022-1317-77-11-2689;
RA   Betakova T., Nermut M.V., Hay A.J.;
RT   "The NB protein is an integral component of the membrane of influenza B
RT   virus.";
RL   J. Gen. Virol. 77:2689-2694(1996).
CC   -!- FUNCTION: Putative viral proton channel. May play a role in virus
CC       entry. {ECO:0000269|PubMed:15042345}.
CC   -!- SUBUNIT: Dimer.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type
CC       III membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the influenza viruses type B glycoprotein NB
CC       family. {ECO:0000305}.
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DR   EMBL; J02095; AAA43748.1; -; Genomic_RNA.
DR   PIR; A26026; VGIVL4.
DR   RefSeq; NP_056662.1; NC_002209.1.
DR   SMR; P06817; -.
DR   DNASU; 26824003; -.
DR   GeneID; 26824003; -.
DR   KEGG; vg:26824003; -.
DR   Proteomes; UP000008158; Genome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
DR   GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR   InterPro; IPR007288; InfluenzaB_glycoprotein_NB.
DR   Pfam; PF04159; NB; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Hydrogen ion transport; Ion channel; Ion transport; Membrane;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW   Transport; Viral ion channel; Virion.
FT   CHAIN           1..100
FT                   /note="Glycoprotein NB"
FT                   /id="PRO_0000078906"
FT   TOPO_DOM        1..18
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        19..40
FT                   /note="Helical; Signal-anchor for type III membrane
FT                   protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        41..100
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        3
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        7
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         20
FT                   /note="S->A: Loss of gating and proton permeability."
FT                   /evidence="ECO:0000269|PubMed:15042345"
FT   MUTAGEN         24
FT                   /note="T->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:15042345"
FT   MUTAGEN         26
FT                   /note="C->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:15042345"
FT   MUTAGEN         28
FT                   /note="S->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:15042345"
SQ   SEQUENCE   100 AA;  11024 MW;  D32A55CCCABC7F54 CRC64;
     MNNATFNCTN INPITHIRGS IIITICVSLI VILIVFGCIA KIFINKNNCT NNVIRVHKRI
     KCPDCEPFCN KRDDISTPRA GVDIPSFILP GLNLSEGTPN