MAT_INCJJ
ID MAT_INCJJ Reviewed; 374 AA.
AC P12446;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 02-DEC-2020, entry version 64.
DE RecName: Full=Polyprotein p42;
DE Contains:
DE RecName: Full=Protein M1';
DE AltName: Full=CM1';
DE AltName: Full=p31;
DE Contains:
DE RecName: Full=Protein CM2;
GN Name=M;
OS Influenza C virus (strain C/JJ/1950).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Gammainfluenzavirus.
OX NCBI_TaxID=11560;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3404579; DOI=10.1128/jvi.62.9.3348-3355.1988;
RA Yamashita M., Krystal M., Palese P.;
RT "Evidence that the matrix protein of influenza C virus is coded for by a
RT spliced mRNA.";
RL J. Virol. 62:3348-3355(1988).
CC -!- FUNCTION: Ion channel, which might have a role in genome packaging and
CC uncoating processes. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Homotetramer; disulfide-linked.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Polyprotein p42]: Host endoplasmic reticulum
CC membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protein M1']: Virion membrane {ECO:0000305};
CC Single-pass type II membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protein CM2]: Virion membrane {ECO:0000305};
CC Single-pass type I membrane protein {ECO:0000305}. Host cell membrane
CC {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=p42;
CC IsoId=P12446-1; Sequence=Displayed;
CC Name=M1; Synonyms=CM1;
CC IsoId=P12446-2; Sequence=VSP_022114;
CC -!- PTM: Palmitoylated. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: Ser-337 is the major site of phosphorylation, Ser-362 being a
CC minor one. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform p42]: Produced by unspliced mRNA.
CC -!- SIMILARITY: Belongs to the influenza C protein M1 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M22038; AAA43781.1; ALT_TERM; Genomic_RNA.
DR PIR; A28878; MFIVCJ.
DR SMR; P12446; -.
DR GO; GO:0044167; C:host cell endoplasmic reticulum 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:0019028; C:viral capsid; IEA:InterPro.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0039660; F:structural constituent of virion; 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; IPR004271; CM1.
DR InterPro; IPR004267; CM2.
DR Pfam; PF03026; CM1; 1.
DR Pfam; PF03021; CM2; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Disulfide bond; Glycoprotein; Host cell membrane;
KW Host endoplasmic reticulum; Host membrane; Ion channel; Ion transport;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Signal-anchor;
KW Transmembrane; Transmembrane helix; Transport; Viral ion channel;
KW Viral matrix protein; Virion.
FT CHAIN 1..374
FT /note="Polyprotein p42"
FT /id="PRO_0000408878"
FT CHAIN 1..259
FT /note="Protein M1'"
FT /id="PRO_0000078876"
FT CHAIN 260..374
FT /note="Protein CM2"
FT /id="PRO_0000269906"
FT TOPO_DOM 1..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..288
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT SITE 259..260
FT /note="Cleavage; by host signal peptidase"
FT MOD_RES 337
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT MOD_RES 362
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT LIPID 324
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT VAR_SEQ 243..374
FT /note="Missing (in isoform M1)"
FT /evidence="ECO:0000305"
FT /id="VSP_022114"
SQ SEQUENCE 374 AA; 41709 MW; 75C44623669A0D85 CRC64;
MAHEILIAET EAFLKNVAPE TRTAIISAIT GGKSACKSAA KLIKNEHLPL MSGEATTMHI
VMRCLYPEIK PWKKASDMLN KATSSLKKSE GRDIRKQMKA AGDFLGVESM MKMRAFRDDQ
IMEMVEEVYD HPDDYTPDIR IGTITAWLRC KNKKSERYRS NVSESGRTAL KIHEVRKAST
AINEIAGITG LGEEALSLQR QTESLAILCN HTFGSNIMRP HLEKAIKGVE GRVGEMGRMA
MKWLVVIICF SITSQPASAC NLKTCLKLFN NTDAVTVHCF NETQGYMLTL ASLGLGIITM
LYLLVKIIIE LVNGFVLGRW ERWCGDIKTT IMPEIDSMEK DIALSRERLD LGEDAPDETD
ISPIPFSNDG IFEI
