ID   SH_MUMPE                Reviewed;          57 AA.
AC   P22109;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   23-FEB-2022, entry version 69.
DE   RecName: Full=Small hydrophobic protein;
GN   Name=SH;
OS   Mumps virus (strain Enders) (MuV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC   Orthorubulavirus; Mumps orthorubulavirus.
OX   NCBI_TaxID=11167;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Takeuchi K.;
RL   Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8435047; DOI=10.1007/bf01309447;
RA   Yeo R.P., Afzal M.A., Forsey T., Rima B.K.;
RT   "Identification of a new mumps virus lineage by nucleotide sequence
RT   analysis of the SH gene of ten different strains.";
RL   Arch. Virol. 128:371-377(1993).
RN   [3]
RP   SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=8918542; DOI=10.1006/viro.1996.0583;
RA   Takeuchi K., Tanabayashi K., Hishiyama M., Yamada A.;
RT   "The mumps virus SH protein is a membrane protein and not essential for
RT   virus growth.";
RL   Virology 225:156-162(1996).
RN   [4]
RP   FUNCTION.
RX   PubMed=16439527; DOI=10.1128/jvi.80.4.1700-1709.2006;
RA   Wilson R.L., Fuentes S.M., Wang P., Taddeo E.C., Klatt A., Henderson A.J.,
RA   He B.;
RT   "Function of small hydrophobic proteins of paramyxovirus.";
RL   J. Virol. 80:1700-1709(2006).
CC   -!- FUNCTION: Plays a role in the inhibition of the host NF-kappa-B
CC       pathway. This inhibition occurs at the receptor level, by preventing
CC       the signaling of TNFR1 as well as IL-1R and TLR3.
CC       {ECO:0000250|UniProtKB:P22112}.
CC   -!- SUBUNIT: Interacts with host TNFRSF1A, RIPK1 AND IRAK1; these
CC       interactions interfere with host NF-kappa-B activation at the level of
CC       receptor complexes (By similarity). Interacts with host protein UBQLN4
CC       (By similarity). {ECO:0000250|UniProtKB:P22110,
CC       ECO:0000250|UniProtKB:P22112}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250|UniProtKB:P22112};
CC       Single-pass membrane protein {ECO:0000250|UniProtKB:P22112}. Host cell
CC       membrane {ECO:0000250|UniProtKB:P22112}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:P22112}.
CC   -!- SIMILARITY: Belongs to the rubulavirus small hydrophobic protein
CC       family. {ECO:0000305}.
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DR   EMBL; D90231; BAA14279.1; -; Genomic_RNA.
DR   EMBL; X63705; CAA45235.1; -; Genomic_RNA.
DR   PIR; JU0305; SHNZME.
DR   SMR; P22109; -.
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:0039644; P:suppression by virus of host NF-kappaB cascade; IEA:UniProtKB-KW.
DR   InterPro; IPR001477; SH.
DR   Pfam; PF01445; SH; 1.
DR   PIRSF; PIRSF003923; SH; 1.
PE   1: Evidence at protein level;
KW   Host cell membrane; Host membrane; Host-virus interaction;
KW   Inhibition of host NF-kappa-B by virus; Membrane; Transmembrane;
KW   Transmembrane helix; Virion.
FT   CHAIN           1..57
FT                   /note="Small hydrophobic protein"
FT                   /id="PRO_0000142877"
FT   TOPO_DOM        1..8
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..57
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000269|PubMed:8918542"
SQ   SEQUENCE   57 AA;  6717 MW;  D443CB495BBBF323 CRC64;
     MPAIQPPLYL TFLLLILLYL IITLYVWTIL TINHKTAVRY AALYQRSCSR WGFDQSL