C_SEND6
ID C_SEND6 Reviewed; 215 AA.
AC P14253; P14256; Q88436;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 23-FEB-2022, entry version 63.
DE RecName: Full=Protein C';
GN Name=P/V/C;
OS Sendai virus (strain 6/94) (SeV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Respirovirus.
OX NCBI_TaxID=11193;
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=2557577; DOI=10.1093/nar/17.23.10102;
RA Homann H.E., Neubert W.J.;
RT "Cloning and sequencing of the polymerase gene (P) of Sendai virus (strain
RT 6/94).";
RL Nucleic Acids Res. 17:10102-10102(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 and Y2 proteins leads to viral
CC delayed growth. Plays an important role in virion particles release.
CC 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=3;
CC Name=C';
CC IsoId=P14253-1; Sequence=Displayed;
CC Name=C;
CC IsoId=P14253-2; Sequence=VSP_018929;
CC Name=Y2;
CC IsoId=P14253-3; Sequence=VSP_018930;
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: Protein Y2 is produced not only by alternative initiation, but
CC also by proteolytic cleavage of C'. Only alternative initiation is
CC detected in vitro, whereas in vivo cleavage seems to be predominant.
CC {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; X17007; CAA34868.1; -; Genomic_RNA.
DR EMBL; X17007; CAA34869.1; -; Genomic_RNA.
DR SMR; P14253; -.
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_0000039390"
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 VAR_SEQ 1..40
FT /note="Missing (in isoform Y2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018930"
FT VAR_SEQ 1..11
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_018929"
SQ SEQUENCE 215 AA; 25159 MW; 2E46011104240290 CRC64;
MASATLTAWI KMPSFLKKIL KLRGRRQEDE SRSRTLSDSS MLSCRVNQLT SEGTEAGSTT
PSTLPKDQAL LIEPKVRAKE KSQHRRPKII DQVRRVESLG EQASQRQKHM LETLINKIYT
GPLGEELVQT LYLRIWAMEE TPESLKILQM REDIRDQVLK MKTERWLRTL IRGEKTKLKD
FQKRYEEVHP YLMKEKVEQV IMEEAWSLAA HIVQE
