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Polyprotein p42 [Cleaved into: Protein M1' (CM1') (p31); Protein CM2]

 MAT_INCAA               Reviewed;         374 AA.
Q6I7B9; Q6I7B8;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
09-JAN-2007, sequence version 2.
10-MAY-2017, entry version 53.
RecName: Full=Polyprotein p42;
Contains:
RecName: Full=Protein M1';
AltName: Full=CM1';
AltName: Full=p31;
Contains:
RecName: Full=Protein CM2;
Name=M;
Influenza C virus (strain C/Ann Arbor/1/1950).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Influenzavirus C.
NCBI_TaxID=11553;
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=15218173; DOI=10.1099/vir.0.79937-0;
Muraki Y., Washioka H., Sugawara K., Matsuzaki Y., Takashita E.,
Hongo S.;
"Identification of an amino acid residue on influenza C virus M1
protein responsible for formation of the cord-like structures of the
virus.";
J. Gen. Virol. 85:1885-1893(2004).
[2]
CHARACTERIZATION, SUBCELLULAR LOCATION, GLYCOSYLATION, MUTAGENESIS OF
THR-272, AND TOPOLOGY OF CM2.
PubMed=9356355; DOI=10.1006/viro.1997.8788;
Pekosz A., Lamb R.A.;
"The CM2 protein of influenza C virus is an oligomeric integral
membrane glycoprotein structurally analogous to influenza A virus M2
and influenza B virus NB proteins.";
Virology 237:439-451(1997).
[3]
CLEAVAGE BY HOST SIGNAL PEPTIDASE.
PubMed=9847305;
Hongo S., Sugawara K., Muraki Y., Matsuzaki Y., Takashita E.,
Kitame F., Nakamura K.;
"Influenza C virus CM2 protein is produced from a 374-amino-acid
protein (P42) by signal peptidase cleavage.";
J. Virol. 73:46-50(1999).
[4]
SUBUNIT, PALMITOYLATION AT CYS-324, PHOSPHORYLATION AT SER-337 AND
SER-362, AND MUTAGENESIS OF CYS-260; CYS-265; CYS-279; SER-337 AND
SER-367.
PubMed=11297683;
Li Z.N., Hongo S., Sugawara K., Sugahara K., Tsuchiya E.,
Matsuzaki Y., Nakamura K.;
"The sites for fatty acylation, phosphorylation and intermolecular
disulphide bond formation of influenza C virus CM2 protein.";
J. Gen. Virol. 82:1085-1093(2001).
[5]
FUNCTION.
PubMed=21106743; DOI=10.1128/JVI.01367-10;
Furukawa T., Muraki Y., Noda T., Takashita E., Sho R., Sugawara K.,
Matsuzaki Y., Shimotai Y., Hongo S.;
"Role of the CM2 protein in the influenza C virus replication cycle.";
J. Virol. 85:1322-1329(2011).
-!- FUNCTION: Ion channel, which might have a role in genome packaging
and uncoating processes. {ECO:0000269|PubMed:21106743}.
-!- SUBUNIT: Homodimer; disulfide-linked. Homotetramer; disulfide-
linked. {ECO:0000305|PubMed:11297683}.
-!- SUBCELLULAR LOCATION: Polyprotein p42: Host endoplasmic reticulum
membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein M1': Virion membrane {ECO:0000305};
Single-pass type II membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein CM2: Virion membrane {ECO:0000305};
Single-pass type I membrane protein {ECO:0000305}. Host cell
membrane {ECO:0000305}; Single-pass type I membrane protein
{ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=p42;
IsoId=Q6I7B9-1; Sequence=Displayed;
Note=Produced by unspliced mRNA.;
Name=M1; Synonyms=CM1;
IsoId=Q6I7B9-2; Sequence=VSP_022111;
-!- PTM: Palmitoylated. {ECO:0000269|PubMed:11297683}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:9356355}.
-!- PTM: Ser-337 is the major site of phosphorylation, Ser-362 being a
minor one. {ECO:0000269|PubMed:11297683}.
-!- SIMILARITY: Belongs to the influenza C protein M1 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD24942.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=BAD24943.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AB126196; BAD24942.1; ALT_TERM; Viral_cRNA.
EMBL; AB126196; BAD24943.1; ALT_INIT; Viral_cRNA.
RefSeq; YP_089657.1; NC_006312.1. [Q6I7B9-2]
RefSeq; YP_089658.1; NC_006312.1.
PDB; 5M1M; X-ray; 1.50 A; A=1-155.
PDBsum; 5M1M; -.
SMR; Q6I7B9; -.
iPTMnet; Q6I7B9; -.
GeneID; 3077361; -.
GeneID; 3077362; -.
KEGG; vg:3077361; -.
KEGG; vg:3077362; -.
Proteomes; UP000008286; Genome.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0019028; C:viral capsid; IEA:InterPro.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW.
InterPro; IPR004271; CM1.
InterPro; IPR004267; CM2.
Pfam; PF03026; CM1; 1.
Pfam; PF03021; CM2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Disulfide bond;
Glycoprotein; Host cell membrane; Host endoplasmic reticulum;
Host membrane; Ion channel; Ion transport; Lipoprotein; Membrane;
Palmitate; Phosphoprotein; Reference proteome; Signal-anchor;
Transmembrane; Transmembrane helix; Transport; Viral ion channel;
Viral matrix protein; Virion.
CHAIN 1 374 Polyprotein p42.
/FTId=PRO_0000408875.
CHAIN 1 259 Protein M1'.
/FTId=PRO_0000269455.
CHAIN 260 374 Protein CM2.
/FTId=PRO_0000269903.
TOPO_DOM 1 238 Cytoplasmic.
{ECO:0000305|PubMed:9356355}.
TRANSMEM 239 259 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 260 288 Extracellular.
{ECO:0000305|PubMed:9356355}.
TRANSMEM 289 309 Helical. {ECO:0000255}.
TOPO_DOM 310 374 Cytoplasmic. {ECO:0000255}.
SITE 259 260 Cleavage; by host signal peptidase.
MOD_RES 337 337 Phosphoserine; by host.
{ECO:0000269|PubMed:11297683}.
MOD_RES 362 362 Phosphoserine; by host.
{ECO:0000269|PubMed:11297683}.
LIPID 324 324 S-palmitoyl cysteine; by host.
{ECO:0000269|PubMed:11297683}.
CARBOHYD 270 270 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000305|PubMed:9356355}.
VAR_SEQ 243 374 Missing (in isoform M1). {ECO:0000305}.
/FTId=VSP_022111.
MUTAGEN 260 260 C->A: Complete loss of oligomerization;
when associated with A-265 and A279.
{ECO:0000269|PubMed:11297683}.
MUTAGEN 265 265 C->A: Complete loss of oligomerization;
when associated with A-260 and A279.
{ECO:0000269|PubMed:11297683}.
MUTAGEN 272 272 T->A: Loss of carbohydrate modification.
{ECO:0000269|PubMed:9356355}.
MUTAGEN 279 279 C->A: Complete loss of oligomerization;
when associated with A-260 and A265.
{ECO:0000269|PubMed:11297683}.
MUTAGEN 324 324 C->A: Complete loss of palmitoylation.
MUTAGEN 337 337 S->A: 93% loss of phosphorylation.
Complete loss of phosphorylation; when
associated with A-362.
{ECO:0000269|PubMed:11297683}.
MUTAGEN 362 362 S->A: Complete loss of phosphorylation;
when associated with A-337.
MUTAGEN 367 367 S->A: No effet on phosphorylation.
{ECO:0000269|PubMed:11297683}.
HELIX 3 13 {ECO:0000244|PDB:5M1M}.
TURN 14 16 {ECO:0000244|PDB:5M1M}.
HELIX 19 29 {ECO:0000244|PDB:5M1M}.
HELIX 33 44 {ECO:0000244|PDB:5M1M}.
HELIX 52 65 {ECO:0000244|PDB:5M1M}.
HELIX 73 82 {ECO:0000244|PDB:5M1M}.
TURN 83 85 {ECO:0000244|PDB:5M1M}.
HELIX 88 101 {ECO:0000244|PDB:5M1M}.
HELIX 104 113 {ECO:0000244|PDB:5M1M}.
HELIX 118 130 {ECO:0000244|PDB:5M1M}.
HELIX 132 134 {ECO:0000244|PDB:5M1M}.
HELIX 137 152 {ECO:0000244|PDB:5M1M}.
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


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