SH_BRSVA
ID SH_BRSVA Reviewed; 73 AA.
AC P24616; Q77KZ9; Q8V690;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 23-FEB-2022, entry version 80.
DE RecName: Full=Small hydrophobic protein;
DE AltName: Full=Small protein 1A;
GN Name=SH; Synonyms=1A;
OS Bovine respiratory syncytial virus (strain A51908) (BRS).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX NCBI_TaxID=11247;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1856698; DOI=10.1099/0022-1317-72-7-1715;
RA Samal S.K., Zamora M.;
RT "Nucleotide sequence analysis of a matrix and small hydrophobic protein
RT dicistronic mRNA of bovine respiratory syncytial virus demonstrates
RT extensive sequence divergence of the small hydrophobic protein from that of
RT human respiratory syncytial virus.";
RL J. Gen. Virol. 72:1715-1720(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=A51908, and ATCC 51908;
RX PubMed=11724268; DOI=10.1023/a:1011888019966;
RA Yunus A.S., Khattar S.K., Collins P.L., Samal S.K.;
RT "Rescue of bovine respiratory syncytial virus from cloned cDNA: entire
RT genome sequence of BRSV strain A51908.";
RL Virus Genes 23:157-164(2001).
CC -!- FUNCTION: Viroporin that forms a homopentameric ion channel displaying
CC low ion selectivity. May play a role in virus morphogenesis and
CC pathogenicity at various stages of the viral life cycle. Accumulates at
CC the membrane of the Golgi apparatus in infected cells and may
CC facilitate virus release by modifying the secretory pathway. May
CC enhance host membrane permeability and disrupt cellular ion
CC homeostasis, which can be sensed as damage-associated molecular
CC patterns/danger signals, triggering NLRP3 inflammasome activation and
CC inflammatory immune response. Also inhibits host TNFA-mediated
CC signaling pathway and may delay apoptosis, allowing time for the virus
CC to replicate. {ECO:0000250|UniProtKB:P0DOE5}.
CC -!- ACTIVITY REGULATION: Channel activity is inhibited by copper. Also
CC inhibited by small-molecule pyronin B. {ECO:0000250|UniProtKB:P0DOE5}.
CC -!- SUBUNIT: Homopentamer forming a funnel-like pore. Interacts with
CC glycoprotein G; this interaction occurs on the surface of virion
CC particles and infected cells. Interacts with host BCAP31 (via C-
CC terminus); this interaction is direct. {ECO:0000250|UniProtKB:P0DOE5}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250|UniProtKB:P0DOE5};
CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:P0DOE5}.
CC Host cell membrane {ECO:0000250|UniProtKB:P0DOE5}; Single-pass type II
CC membrane protein {ECO:0000250|UniProtKB:P0DOE5}. Host Golgi apparatus
CC membrane {ECO:0000250|UniProtKB:P0DOE5}; Single-pass type II membrane
CC protein {ECO:0000250|UniProtKB:P0DOE5}. Host endoplasmic reticulum
CC membrane {ECO:0000250|UniProtKB:P0DOE5}; Single-pass type II membrane
CC protein {ECO:0000250|UniProtKB:P0DOE5}. Note=Present in very small
CC amount in the virion. Detected in lipid rafts of host Golgi apparatus
CC membrane. {ECO:0000250|UniProtKB:P0DOE5}.
CC -!- PTM: Four species of SH have been detected in infected cell cytoplasm:
CC a 7.5 kDa non-glycosylated form (SH0), a 13-15 kDa form that contains
CC one or two N-linked carbohydrate side chains of the high-mannose type
CC (SHg), a 21-30 kDa polylactosaminoglycan-modified form of the protein
CC (SHp), and the isoform generated by alternative translational
CC initiation. Of these different forms, SH0 is by far the most abundant
CC protein detected during virus infection.
CC {ECO:0000250|UniProtKB:P0DOE5}.
CC -!- PTM: Tyrosine phosphorylated. {ECO:0000250|UniProtKB:P0DOE5}.
CC -!- SIMILARITY: Belongs to the orthopneumovirus small hydrophobic protein
CC family. {ECO:0000305}.
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DR EMBL; D01012; BAA00813.1; -; mRNA.
DR EMBL; AF295543; AAL49397.1; -; Genomic_RNA.
DR EMBL; AF295544; AAL49408.1; -; Genomic_RNA.
DR PIR; JQ1179; P1NZBR.
DR SMR; P24616; -.
DR Proteomes; UP000007616; Genome.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
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.
DR InterPro; IPR005327; SHP.
DR Pfam; PF03579; SHP; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Host cell membrane; Host endoplasmic reticulum;
KW Host Golgi apparatus; Host membrane; Hydrogen ion transport; Ion transport;
KW Membrane; Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix; Transport; Virion.
FT CHAIN 1..73
FT /note="Small hydrophobic protein"
FT /id="PRO_0000142866"
FT TOPO_DOM 1..19
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..73
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT VARIANT 7
FT /note="M -> I (in strain: ATCC 51908)"
FT VARIANT 13
FT /note="K -> E (in strain: ATCC 51908)"
FT VARIANT 21
FT /note="V -> A (in strain: ATCC 51908)"
FT VARIANT 26
FT /note="I -> T (in strain: ATCC 51908)"
FT VARIANT 32..33
FT /note="VI -> IV (in strain: ATCC 51908)"
FT VARIANT 32
FT /note="V -> A"
FT VARIANT 47
FT /note="L -> F (in strain: ATCC 51908)"
FT VARIANT 60
FT /note="G -> R (in strain: ATCC 51908)"
FT VARIANT 67
FT /note="S -> L (in strain: ATCC 51908)"
FT VARIANT 73
FT /note="V -> E (in strain: ATCC 51908)"
SQ SEQUENCE 73 AA; 8402 MW; 6A617D33CCFB9F93 CRC64;
MNNTSTMIEF TGKFWTYFTL VFMMLIIGFF FVITSLVAAI LNKLCDLNDH HTNSLDIRTG
LRNDTQSITR AHV
