ID   SH_BRSV3                Reviewed;          81 AA.
AC   P32554;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   23-FEB-2022, entry version 63.
DE   RecName: Full=Small hydrophobic protein;
DE   AltName: Full=Small protein 1A;
GN   Name=SH; Synonyms=1A;
OS   Bovine respiratory syncytial virus (strain 391-2) (BRS).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX   NCBI_TaxID=31611;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1413513; DOI=10.1016/0042-6822(92)90203-2;
RA   Anderson K., King A.M.Q., Lerch R.A., Wertz G.W.;
RT   "Polylactosaminoglycan modification of the respiratory syncytial virus
RT   small hydrophobic (SH) protein: a conserved feature among human and bovine
RT   respiratory syncytial viruses.";
RL   Virology 191:417-430(1992).
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; M86652; AAA42811.1; -; mRNA.
DR   PIR; A44049; P1NZB2.
DR   SMR; P32554; -.
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; Signal-anchor; Transmembrane;
KW   Transmembrane helix; Transport; Virion.
FT   CHAIN           1..81
FT                   /note="Small hydrophobic protein"
FT                   /id="PRO_0000142865"
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..81
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   81 AA;  9306 MW;  02FEFA89D6625A32 CRC64;
     MNSTSTIIEF TGEFWTYFTL VFMMLTIGFF FIVTSLVAAI LNKLCDLNDH HTNSLDIRTK
     LRSDTQLITR AHEESINQSS N