SH_HRSVB
ID SH_HRSVB Reviewed; 65 AA.
AC O36632;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 23-FEB-2022, entry version 65.
DE RecName: Full=Small hydrophobic protein {ECO:0000250|UniProtKB:P0DOE5};
DE AltName: Full=Small protein 1A;
GN Name=SH {ECO:0000250|UniProtKB:P0DOE5};
GN Synonyms=1A {ECO:0000250|UniProtKB:P0DOE5};
OS Human respiratory syncytial virus B (strain B1).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX NCBI_TaxID=79692;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=9391135; DOI=10.1073/pnas.94.25.13961;
RA Karron R.A., Buonagurio D.A., Georgiu A.F., Whitehead S.S., Adamus J.E.,
RA Clements-Mann M.L., Harris D.O., Randolph V.B., Udem S.A., Murphy B.R.,
RA Sidhu M.S.;
RT "Respiratory syncytial virus (RSV) SH and G proteins are not essential for
RT viral replication in vitro: clinical evaluation and molecular
RT characterization of a cold-passaged, attenuated RSV subgroup B mutant.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:13961-13966(1997).
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; AF013254; AAB82434.1; -; Genomic_RNA.
DR RefSeq; NP_056861.1; NC_001781.1.
DR SMR; O36632; -.
DR TCDB; 1.A.68.1.3; the viral small hydrophobic viroporin (v-sh) family.
DR PRIDE; O36632; -.
DR GeneID; 1489823; -.
DR KEGG; vg:1489823; -.
DR Proteomes; UP000002472; 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: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:0039651; P:induction by virus of host cysteine-type endopeptidase activity involved in apoptotic process; 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; IPR005327; SHP.
DR Pfam; PF03579; SHP; 1.
PE 3: Inferred from homology;
KW Activation of host caspases by virus; Glycoprotein; Host cell membrane;
KW Host endoplasmic reticulum; Host Golgi apparatus; Host membrane;
KW Host-virus interaction; Ion channel; Ion transport; Membrane;
KW Modulation of host cell apoptosis by virus; Phosphoprotein;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Transport; Viral ion channel; Virion.
FT CHAIN 1..65
FT /note="Small hydrophobic protein"
FT /id="PRO_0000365796"
FT TOPO_DOM 1..20
FT /note="Intravirion"
FT /evidence="ECO:0000250|UniProtKB:P0DOE5"
FT TRANSMEM 21..44
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000250|UniProtKB:P0DOE5"
FT TOPO_DOM 45..65
FT /note="Virion surface"
FT /evidence="ECO:0000250|UniProtKB:P0DOE5"
FT REGION 6..15
FT /note="Interaction with host BCAP31"
FT /evidence="ECO:0000250|UniProtKB:P0DOE5"
FT REGION 38..43
FT /note="Interaction with small-molecule inhibitor"
FT /evidence="ECO:0000250|UniProtKB:P0DOE5"
FT SITE 22
FT /note="Involved in opening and closing mechanism of the
FT pentameric structure"
FT /evidence="ECO:0000250|UniProtKB:P0DOE5"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 65 AA; 7511 MW; 249F12DF2BFF69EB CRC64;
MGNTSITIEF TSKFWPYFTL IHMILTLISL LIIITIMIAI LNKLSEHKTF CNNTLELGQM
HQINT
