MAT_INCAA
ID MAT_INCAA Reviewed; 374 AA.
AC Q6I7B9; Q6I7B8;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 02-JUN-2021, entry version 66.
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/Ann Arbor/1/1950).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Gammainfluenzavirus.
OX NCBI_TaxID=11553;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15218173; DOI=10.1099/vir.0.79937-0;
RA Muraki Y., Washioka H., Sugawara K., Matsuzaki Y., Takashita E., Hongo S.;
RT "Identification of an amino acid residue on influenza C virus M1 protein
RT responsible for formation of the cord-like structures of the virus.";
RL J. Gen. Virol. 85:1885-1893(2004).
RN [2]
RP CHARACTERIZATION, SUBCELLULAR LOCATION, GLYCOSYLATION, MUTAGENESIS OF
RP THR-272, AND TOPOLOGY OF CM2.
RX PubMed=9356355; DOI=10.1006/viro.1997.8788;
RA Pekosz A., Lamb R.A.;
RT "The CM2 protein of influenza C virus is an oligomeric integral membrane
RT glycoprotein structurally analogous to influenza A virus M2 and influenza B
RT virus NB proteins.";
RL Virology 237:439-451(1997).
RN [3]
RP CLEAVAGE BY HOST SIGNAL PEPTIDASE.
RX PubMed=9847305; DOI=10.1128/jvi.73.1.46-50.1999;
RA Hongo S., Sugawara K., Muraki Y., Matsuzaki Y., Takashita E., Kitame F.,
RA Nakamura K.;
RT "Influenza C virus CM2 protein is produced from a 374-amino-acid protein
RT (P42) by signal peptidase cleavage.";
RL J. Virol. 73:46-50(1999).
RN [4]
RP SUBUNIT, PALMITOYLATION AT CYS-324, PHOSPHORYLATION AT SER-337 AND SER-362,
RP AND MUTAGENESIS OF CYS-260; CYS-265; CYS-279; SER-337 AND SER-367.
RX PubMed=11297683; DOI=10.1099/0022-1317-82-5-1085;
RA Li Z.N., Hongo S., Sugawara K., Sugahara K., Tsuchiya E., Matsuzaki Y.,
RA Nakamura K.;
RT "The sites for fatty acylation, phosphorylation and intermolecular
RT disulphide bond formation of influenza C virus CM2 protein.";
RL J. Gen. Virol. 82:1085-1093(2001).
RN [5]
RP FUNCTION.
RX PubMed=21106743; DOI=10.1128/jvi.01367-10;
RA Furukawa T., Muraki Y., Noda T., Takashita E., Sho R., Sugawara K.,
RA Matsuzaki Y., Shimotai Y., Hongo S.;
RT "Role of the CM2 protein in the influenza C virus replication cycle.";
RL J. Virol. 85:1322-1329(2011).
CC -!- FUNCTION: Ion channel, which might have a role in genome packaging and
CC uncoating processes. {ECO:0000269|PubMed:21106743}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Homotetramer; disulfide-linked.
CC {ECO:0000305|PubMed:11297683}.
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=Q6I7B9-1; Sequence=Displayed;
CC Name=M1; Synonyms=CM1;
CC IsoId=Q6I7B9-2; Sequence=VSP_022111;
CC -!- PTM: Palmitoylated. {ECO:0000269|PubMed:11297683}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:9356355}.
CC -!- PTM: Ser-337 is the major site of phosphorylation, Ser-362 being a
CC minor one. {ECO:0000269|PubMed:11297683}.
CC -!- MISCELLANEOUS: [Isoform p42]: Produced by unspliced mRNA.
CC -!- SIMILARITY: Belongs to the influenza C protein M1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD24942.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD24943.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB126196; BAD24942.1; ALT_TERM; Viral_cRNA.
DR EMBL; AB126196; BAD24943.1; ALT_INIT; Viral_cRNA.
DR RefSeq; YP_089657.1; NC_006312.1. [Q6I7B9-2]
DR RefSeq; YP_089658.1; NC_006312.1.
DR PDB; 5M1M; X-ray; 1.50 A; A=1-155.
DR PDBsum; 5M1M; -.
DR SMR; Q6I7B9; -.
DR iPTMnet; Q6I7B9; -.
DR DNASU; 3077361; -.
DR GeneID; 3077361; -.
DR GeneID; 3077362; -.
DR KEGG; vg:3077361; -.
DR KEGG; vg:3077362; -.
DR Proteomes; UP000008286; Genome.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disulfide bond; Glycoprotein;
KW Host cell membrane; Host endoplasmic reticulum; Host membrane; Ion channel;
KW Ion transport; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Transport; Viral ion channel; Viral matrix protein; Virion.
FT CHAIN 1..374
FT /note="Polyprotein p42"
FT /id="PRO_0000408875"
FT CHAIN 1..259
FT /note="Protein M1'"
FT /id="PRO_0000269455"
FT CHAIN 260..374
FT /note="Protein CM2"
FT /id="PRO_0000269903"
FT TOPO_DOM 1..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9356355"
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:0000305|PubMed:9356355"
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:0000269|PubMed:11297683"
FT MOD_RES 362
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:11297683"
FT LIPID 324
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000269|PubMed:11297683"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000305|PubMed:9356355"
FT VAR_SEQ 243..374
FT /note="Missing (in isoform M1)"
FT /evidence="ECO:0000305"
FT /id="VSP_022111"
FT MUTAGEN 260
FT /note="C->A: Complete loss of oligomerization; when
FT associated with A-265 and A279."
FT /evidence="ECO:0000269|PubMed:11297683"
FT MUTAGEN 265
FT /note="C->A: Complete loss of oligomerization; when
FT associated with A-260 and A279."
FT /evidence="ECO:0000269|PubMed:11297683"
FT MUTAGEN 272
FT /note="T->A: Loss of carbohydrate modification."
FT /evidence="ECO:0000269|PubMed:9356355"
FT MUTAGEN 279
FT /note="C->A: Complete loss of oligomerization; when
FT associated with A-260 and A265."
FT /evidence="ECO:0000269|PubMed:11297683"
FT MUTAGEN 324
FT /note="C->A: Complete loss of palmitoylation."
FT MUTAGEN 337
FT /note="S->A: 93% loss of phosphorylation. Complete loss of
FT phosphorylation; when associated with A-362."
FT /evidence="ECO:0000269|PubMed:11297683"
FT MUTAGEN 362
FT /note="S->A: Complete loss of phosphorylation; when
FT associated with A-337."
FT MUTAGEN 367
FT /note="S->A: No effet on phosphorylation."
FT /evidence="ECO:0000269|PubMed:11297683"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:5M1M"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:5M1M"
FT HELIX 19..29
FT /evidence="ECO:0007829|PDB:5M1M"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:5M1M"
FT HELIX 52..65
FT /evidence="ECO:0007829|PDB:5M1M"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:5M1M"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:5M1M"
FT HELIX 88..101
FT /evidence="ECO:0007829|PDB:5M1M"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:5M1M"
FT HELIX 118..130
FT /evidence="ECO:0007829|PDB:5M1M"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:5M1M"
FT HELIX 137..152
FT /evidence="ECO:0007829|PDB:5M1M"
SQ SEQUENCE 374 AA; 41740 MW; D6BD65E9CB55B739 CRC64;
MAHEILIAET EAFLKNVAPE TRTAIISAIT GGKSACKSAA KLIKNEHLPL MSGEATTMHI
VMRCLYPEIK PWKKASDMLN KATSSLKKSE GRDIRKQMKA AGDFLGVESM MKMRAFRDDQ
IMEMVEEVYD HPDDYTPDIR IGTITAWLRC KNKKSERYRS NVSESGRTAL KIHEVRKAST
AMNEIAGITG LGEEALSLQR QTESLAILCN HTFGSNIMRP HLEKAIKGVE GRVGEMGRMA
MKWLVVIICF SITSQPASAC NLKTCLKLFN NTDAVTVHCF NENQGYMLTL ASLGLGIITM
LYLLVKIIIE LVNGFVLGRW ERWCGDIKTT IMPEIDSMEK DIALSRERLD LGEDAPDETD
NSPIPFSNDG IFEI
