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C_SENDF
ID   C_SENDF                 Reviewed;         215 AA.
AC   P14254; P14257; P14258; Q88446; Q88447;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   23-FEB-2022, entry version 68.
DE   RecName: Full=Protein C';
GN   Name=P/V/C;
OS   Sendai virus (strain Fushimi) (SeV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Respirovirus.
OX   NCBI_TaxID=11195;
OH   NCBI_TaxID=10144; Cavia cutleri (Guinea pig).
OH   NCBI_TaxID=36483; Cricetidae sp. (Hamster).
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
OH   NCBI_TaxID=10116; Rattus norvegicus (Rat).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2557576; DOI=10.1093/nar/17.23.10101;
RA   Neubert W.J.;
RT   "Cloning and sequencing of the polymerase gene (P) of Sendai virus (strain
RT   Fushimi).";
RL   Nucleic Acids Res. 17:10101-10101(1989).
CC   -!- FUNCTION: The different products prevent the establishment of cellular
CC       antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta)
CC       and IFN-gamma signaling pathways. They inhibit IFN-alpha/beta induced
CC       tyrosine phosphorylation of STAT1 and STAT2. Blocking the IFN-
CC       alpha/beta pathway requires binding to STAT1 in the cytoplasm. They
CC       inhibit IFN-gamma induced serine phosphorylation of STAT1. Block the
CC       IFN-gamma pathway by binding to and stabilizing the parallel form of
CC       the STAT1 dimer, further inducing high-molecular-weight complex
CC       formation and inhibition of transcription by IFN-gamma. May also have a
CC       role in preventing the cell to enter apoptosis. Modulate regulation of
CC       viral transcription and replication. Overexpression inhibits the viral
CC       RNA polymerase. The absence of all C', C, Y1 and Y2 proteins leads to
CC       viral delayed growth. Plays an important role in virion particles
CC       release. Modulates virion shape. {ECO:0000250|UniProtKB:P04862}.
CC   -!- SUBUNIT: The different isoforms interact (via C-terminus) with
CC       unphosphorylated and phosphorylated human STAT1 (via N-terminus),
CC       favoring the formation of parallel STAT1 homodimers. The different
CC       isoforms do not interact with host STAT2. C protein interacts with L
CC       protein; this interaction has an inhibitory effect on viral
CC       transcription and replication. {ECO:0000250|UniProtKB:P04862}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250|UniProtKB:P04862}.
CC       Note=Protein C' seems to localize around the Golgi.
CC       {ECO:0000250|UniProtKB:P04862}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=4;
CC       Name=C';
CC         IsoId=P14254-1; Sequence=Displayed;
CC       Name=C;
CC         IsoId=P14254-2; Sequence=VSP_018936;
CC       Name=Y1;
CC         IsoId=P14254-3; Sequence=VSP_018937;
CC       Name=Y2;
CC         IsoId=P14254-4; Sequence=VSP_018938;
CC   -!- DOMAIN: The disordered region at the N-terminus is involved in C
CC       protein self-degradation in trans. This self-degradation of C protein
CC       may play a role in the regulation of viral RNA synthesis. The
CC       disordered region at the N-terminus is also involved in the host STAT1
CC       degradation in order to counteract the host innate antiviral response.
CC       {ECO:0000250|UniProtKB:P04861}.
CC   -!- PTM: Y1 and Y2 proteins are produced not only by alternative
CC       initiation, but also by proteolytic cleavage of C'. Only alternative
CC       initiation is detected in vitro, whereas in vivo cleavage seems to be
CC       predominant. {ECO:0000250|UniProtKB:P04861}.
CC   -!- MISCELLANEOUS: The C protein is found in virion at a ratio of
CC       approximately 40 molecules per virion, presumably associated with the
CC       nucleocapsid. {ECO:0000250|UniProtKB:P04862}.
CC   -!- MISCELLANEOUS: The P/V/C gene has two overlapping open reading frames.
CC       One encodes the P/V/W proteins and the other the C/Y proteins.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform C']: The initiator methionine is coded by an
CC       unusual start codon ACG.
CC   -!- MISCELLANEOUS: [Isoform C]: Most abundant isoform in infected cells.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the respirovirus protein C family.
CC       {ECO:0000305}.
CC   -!- CAUTION: The C' protein uses an unusual ACG start codon. {ECO:0000305}.
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DR   EMBL; X17008; CAA34872.1; -; Genomic_RNA.
DR   EMBL; X17008; CAA34873.1; -; Genomic_RNA.
DR   EMBL; X17008; CAA34874.1; -; Genomic_RNA.
DR   SMR; P14254; -.
DR   IntAct; P14254; 2.
DR   Proteomes; UP000006825; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0039563; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT1 activity; ISS:UniProtKB.
DR   GO; GO:0039564; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT2 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR002608; Paramyxo_C.
DR   Pfam; PF01692; Paramyxo_C; 1.
PE   3: Inferred from homology;
KW   Alternative initiation; Host cytoplasm; Host-virus interaction;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host interferon signaling pathway by virus;
KW   Inhibition of host STAT1 by virus; Inhibition of host STAT2 by virus;
KW   Interferon antiviral system evasion; Viral immunoevasion.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..215
FT                   /note="Protein C'"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000039400"
FT   REGION          12..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000250|UniProtKB:P04861"
FT   REGION          15..22
FT                   /note="Involved in self-degradation and in host STAT1
FT                   degradation"
FT                   /evidence="ECO:0000250|UniProtKB:P04861"
FT   REGION          51..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..66
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..40
FT                   /note="Missing (in isoform Y2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018938"
FT   VAR_SEQ         1..34
FT                   /note="Missing (in isoform Y1)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018937"
FT   VAR_SEQ         1..11
FT                   /note="Missing (in isoform C)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018936"
SQ   SEQUENCE   215 AA;  25171 MW;  59AE39A81E480A3C CRC64;
     MASATLTAWI KMPSFLKKIL KLRGRRQEEE SRSRMLSDSS MLSCRVNQLT SEGTEAGSTT
     PSTLPKDQAL PIEPKVRAKE KSQHRRPKII DQVRRVESLG EQASQRQKHM LETLINKIYT
     GPLGEELVQT LYLRIWAMEE TPESLKIPQM REDIRDQVLK MKTERWLRTL IRGEKTKLKD
     FQKRYEEVHP YLMKEKVEQV IMEEAWSLAA HIVQE
 
 
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