ID   SH_AMPV1                Reviewed;         175 AA.
AC   Q2Y2M0;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   23-FEB-2022, entry version 42.
DE   RecName: Full=Small hydrophobic protein;
GN   Name=SH;
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: Viroporin that forms a ion channel probably displaying low
CC       ion selectivity. Plays a role in counteracting host innate immunity by
CC       inhibiting TLR7/MyD88/TRAF6 signaling and STAT1 phosphorylation,
CC       leading to down-regulation of type-I IFN.
CC       {ECO:0000250|UniProtKB:Q6WB95}.
CC   -!- SUBUNIT: Homooligomer (By similarity). Interacts with glycoprotein G
CC       (By similarity). {ECO:0000250|UniProtKB:P0DOE5,
CC       ECO:0000250|UniProtKB:Q6WB95}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250|UniProtKB:Q6WB95};
CC       Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6WB95}.
CC       Host cell membrane {ECO:0000250|UniProtKB:Q6WB95}; Single-pass type II
CC       membrane protein {ECO:0000250|UniProtKB:Q6WB95}.
CC   -!- PTM: Tyrosine phosphorylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the metapneumovirus small hydrophobic protein
CC       family. {ECO:0000305}.
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DR   EMBL; DQ009484; AAY81660.1; -; Viral_cRNA.
DR   RefSeq; YP_443843.1; NC_007652.1.
DR   Proteomes; UP000002471; Genome.
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   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Glycoprotein; Host cell membrane; Host membrane; Hydrogen ion transport;
KW   Ion transport; Membrane; Phosphoprotein; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix; Transport; Virion.
FT   CHAIN           1..175
FT                   /note="Small hydrophobic protein"
FT                   /id="PRO_0000390374"
FT   TOPO_DOM        1..28
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        29..49
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        50..175
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   REGION          73..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        120
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        138
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        152
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   175 AA;  19544 MW;  A67FBD5A1C677FCA CRC64;
     MEPLKVSGSG GIPMKTRLNI ILEKSINKIL IILGLLLIAS TVITITLTVE YIRVENELQL
     CKMGAEVAKT TLEPPAQPTK TTPTLTSTRS TTATFKTRPV SRTNHHTNPS CWREEEKCQN
     ITAKWSNCFG TFLPVRVNCT VLRELCDEQL GNHTTVQVSK RCTCIYALNW DCSYA