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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}.
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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
 
 
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