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Matrix protein (M protein)

 MATRX_SENDZ             Reviewed;         348 AA.
P06446; P27567; Q91UL5; Q9YIJ5; Q9YIM6; Q9YNG5; Q9YNG6; Q9YNG7;
Q9YNG8; Q9YNG9; Q9YNH0; Q9YZ78;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
25-APR-2018, entry version 80.
RecName: Full=Matrix protein;
Short=M protein;
Name=M;
Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ)).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Paramyxoviridae; Respirovirus.
NCBI_TaxID=11198;
NCBI_TaxID=10144; Cavia cutleri (Guinea pig).
NCBI_TaxID=36483; Cricetidae sp. (Hamster).
NCBI_TaxID=10090; Mus musculus (Mouse).
NCBI_TaxID=10116; Rattus norvegicus (Rat).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=6095182; DOI=10.1093/nar/12.21.7965;
Hidaka Y., Kanda T., Iwasaki K., Nomoto A., Shioda T., Shibuta H.;
"Nucleotide sequence of a Sendai virus genome region covering the
entire M gene and the 3' proximal 1013 nucleotides of the F gene.";
Nucleic Acids Res. 12:7965-7973(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Mutant F1-R, and Mutant ts-f1;
PubMed=2161155; DOI=10.1016/0042-6822(90)90040-X;
Middleton Y., Tashiro M., Thai T., Oh J., Seymour J., Pritzer E.,
Klenk H.-D., Rott R., Seto J.T.;
"Nucleotide sequence analyses of the genes encoding the HN, M, NP, P,
and L proteins of two host range mutants of Sendai virus.";
Virology 176:656-657(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Mutant F1-R / T-5 revertant;
PubMed=1651590; DOI=10.1016/0042-6822(91)90839-4;
Tashiro M., James I., Karri S., Wahn K., Tobita K., Klenk H.-D.,
Rott R., Seto J.T.;
"Pneumotropic revertants derived from a pantropic mutant, F1-R, of
Sendai virus.";
Virology 184:227-234(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Mutant KD-11M, Mutant KD-22M, Mutant KD-32M, Mutant KD-51M, and
Mutant KD-52M;
PubMed=1312267; DOI=10.1016/0042-6822(92)90443-S;
Tashiro M., Seto J.T., Choosakul S., Yamakawa M., Klenk H.-D.,
Rott R.;
"Budding site of Sendai virus in polarized epithelial cells is one of
the determinants for tropism and pathogenicity in mice.";
Virology 187:413-422(1992).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Mutant BF-13, Mutant BF-132, Mutant BF-53, Mutant BF-82,
Mutant BY-4, Mutant BY-41, Mutant BY-5, and Mutant BY-8;
PubMed=9930191; DOI=10.1007/s007050050465;
Okada H., Seto J.T., McQueen N.L., Klenk H.-D., Rott R., Tashiro M.;
"Determinants of pantropism of the F1-R mutant of Sendai virus:
specific mutations involved are in the F and M genes.";
Arch. Virol. 143:2343-2352(1998).
[6]
SUBCELLULAR LOCATION.
PubMed=6285608; DOI=10.1016/0042-6822(82)90036-8;
Buechi M., Baechi T.;
"Microscopy of internal structures of Sendai virus associated with the
cytoplasmic surface of host membranes.";
Virology 120:349-359(1982).
[7]
PHOSPHORYLATION AT SER-70, AND MUTAGENESIS OF SER-70.
PubMed=9281516; DOI=10.1006/viro.1997.8701;
Sakaguchi T., Kiyotani K., Kato A., Asakawa M., Fujii Y., Nagai Y.,
Yoshida T.;
"Phosphorylation of the Sendai virus M protein is not essential for
virus replication either in vitro or in vivo.";
Virology 235:360-366(1997).
[8]
INTERACTION WITH F AND HN PROTEINS.
PubMed=11040121; DOI=10.1006/viro.2000.0556;
Ali A., Nayak D.P.;
"Assembly of Sendai virus: M protein interacts with F and HN proteins
and with the cytoplasmic tail and transmembrane domain of F protein.";
Virology 276:289-303(2000).
[9]
MUTAGENESIS OF CYS-83; CYS-106; CYS-158; CYS-251 AND CYS-295.
PubMed=11799163; DOI=10.1128/JVI.76.4.1682-1690.2002;
Sakaguchi T., Uchiyama T., Huang C., Fukuhara N., Kiyotani K.,
Nagai Y., Yoshida T.;
"Alteration of Sendai virus morphogenesis and nucleocapsid
incorporation due to mutation of cysteine residues of the matrix
protein.";
J. Virol. 76:1682-1690(2002).
[10]
INTERACTION WITH HUMAN ALPHA/BETA TUBULINS.
PubMed=14592411; DOI=10.1016/j.bbrc.2003.09.205;
Ogino T., Iwama M., Ohsawa Y., Mizumoto K.;
"Interaction of cellular tubulin with Sendai virus M protein regulates
transcription of viral genome.";
Biochem. Biophys. Res. Commun. 311:283-293(2003).
-!- FUNCTION: Plays a crucial role in virion assembly and budding.
Forms a shell at the inner face of the plasma membrane and
concentrates the HN and F glycoproteins. Acts as a negative
regulator for transcription and replication by sticking to the
nucleocapsid. This effect might be regulated by the cytoplasmic
interaction with tubulin that dissociates the M protein from the
nucleocapsid.
-!- SUBUNIT: Homomultimer. Binds to the cytoplasmic regions of F and
HN proteins. Interacts with nucleocapsid. Interacts with human
alpha-tubulin and beta-tubulin. {ECO:0000269|PubMed:11040121,
ECO:0000269|PubMed:14592411}.
-!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm
{ECO:0000269|PubMed:6285608}. Host cell membrane
{ECO:0000269|PubMed:6285608}; Peripheral membrane protein
{ECO:0000269|PubMed:6285608}; Cytoplasmic side
{ECO:0000269|PubMed:6285608}. Note=During bud formation,
associates at the inner side of the plasma membrane of infected
cells.
-!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
essential for viral particle budding. They recruit proteins of the
host ESCRT machinery (Endosomal Sorting Complex Required for
Transport) or ESCRT-associated proteins. The matrix protein
contains one L domain: a YLDL motif (By similarity).
{ECO:0000250}.
-!- PTM: A large portion is phosphorylated in the cytoplasm, but not
in virion. However, this phosphorylation is not essential for
virus replication. {ECO:0000269|PubMed:9281516}.
-!- SIMILARITY: Belongs to the morbillivirus/respirovirus/rubulavirus
M protein family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X00087; CAA24949.1; -; Genomic_RNA.
EMBL; M30202; AAB06280.1; -; Genomic_RNA.
EMBL; M30203; AAB06286.1; -; Genomic_RNA.
EMBL; M30204; AAB06198.1; -; Genomic_RNA.
EMBL; M69046; AAB06292.1; -; Genomic_RNA.
EMBL; AF001284; AAC82321.1; -; Genomic_RNA.
EMBL; U86424; AAC82304.1; -; Genomic_DNA.
EMBL; U86425; AAC82305.1; -; Genomic_DNA.
EMBL; U86426; AAC82306.1; -; Genomic_DNA.
EMBL; U86427; AAC82307.1; -; Genomic_DNA.
EMBL; U86428; AAC82308.1; -; Genomic_DNA.
EMBL; U86429; AAC82309.1; -; Genomic_DNA.
EMBL; U86430; AAC82310.1; -; Genomic_DNA.
EMBL; U86431; AAC82311.1; -; Genomic_DNA.
EMBL; U86432; AAC82312.1; -; Genomic_DNA.
EMBL; U86433; AAC82313.1; -; Genomic_DNA.
EMBL; U86434; AAC82314.1; -; Genomic_DNA.
EMBL; U86435; AAC82315.1; -; Genomic_DNA.
EMBL; U86436; AAC82316.1; -; Genomic_DNA.
PIR; A04043; MFNZSV.
iPTMnet; P06446; -.
OrthoDB; VOG090000HS; -.
Proteomes; UP000006560; Genome.
Proteomes; UP000110830; Genome.
Proteomes; UP000163956; Genome.
Proteomes; UP000169749; Genome.
Proteomes; UP000181310; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
InterPro; IPR000982; Matrix.
Pfam; PF00661; Matrix; 1.
ProDom; PD000741; Matrix; 1.
1: Evidence at protein level;
Complete proteome; Host cell membrane; Host cytoplasm; Host membrane;
Host-virus interaction; Membrane; Phosphoprotein; Reference proteome;
Viral budding; Viral budding via the host ESCRT complexes;
Viral matrix protein; Viral release from host cell; Virion.
CHAIN 1 348 Matrix protein.
/FTId=PRO_0000142776.
MOTIF 50 53 YLDL motif. {ECO:0000250}.
MOD_RES 70 70 Phosphoserine; by host.
{ECO:0000305|PubMed:9281516}.
VARIANT 42 42 D -> V (in wild-type, Mutant F1-R, Mutant
F1-R / T-5 revertant, Mutant ts-f1,
Mutant KD-11M, Mutant KD-22M, Mutant KD-
32M, Mutant 51M and Mutant 52M).
VARIANT 128 128 D -> G (in Mutant F1-R and Mutant F1-R /
T-5 revertant).
VARIANT 128 128 D -> V (in strain: Mutant BY-5).
VARIANT 161 161 V -> M (in strain: Mutant KD-32M).
VARIANT 182 182 I -> V (in strain: Mutant KD-22M).
VARIANT 191 191 D -> Y (in strain: Mutant KD-32M).
VARIANT 197 197 S -> C (in strain: Mutant KD-22M).
VARIANT 210 210 I -> T (in strain: Mutant F1-R and Mutant
F1-R / T-5 revertant).
VARIANT 211 211 S -> F (in strain: Mutant KD-51M).
VARIANT 212 212 T -> A (in strain: Mutant KD-22M and
Mutant KD-51M).
VARIANT 217 217 V -> A (in strain: Mutant KD-52M).
VARIANT 232 233 MV -> IL (in strain: Mutant BY-4).
VARIANT 237 237 L -> F (in strain: Mutant BY-4, Mutant
BF-13 and Mutant BY-41).
VARIANT 237 237 L -> M (in strain: Mutant KD-11M).
VARIANT 240 241 RK -> SL (in strain: Mutant KD-11M).
VARIANT 253 253 S -> C (in strain: Mutant KD-11M).
VARIANT 264 267 LGLI -> VGFV (in strain: Mutant BY-5).
VARIANT 277 277 N -> I (in strain: wild-type, Mutant F1-
R, Mutant F1-R / T-5 revertant, Mutant
ts-f1, Mutant BY-4, Mutant BY-8, Mutant
BY-13, Mutant BF-41, Mutant BF-53, Mutant
BF-82, Mutant BF-132, Mutant KD-22M,
Mutant KD-32M, Mutant KD-51 and Mutant
KD-52M).
VARIANT 277 277 N -> L (in strain: Mutant BY-5).
VARIANT 279 279 T -> R (in strain: Mutant BY-5).
VARIANT 294 294 V -> L (in strain: Mutant KD-52M).
MUTAGEN 70 70 S->A: Complete loss of phosphorylation.
{ECO:0000269|PubMed:9281516}.
MUTAGEN 83 83 C->S: Smaller viral particles.
{ECO:0000269|PubMed:11799163}.
MUTAGEN 106 106 C->S: Smaller viral particles.
{ECO:0000269|PubMed:11799163}.
MUTAGEN 158 158 C->S: Complete loss of viral infectivity.
{ECO:0000269|PubMed:11799163}.
MUTAGEN 251 251 C->S: Complete loss of viral infectivity.
{ECO:0000269|PubMed:11799163}.
MUTAGEN 295 295 C->A,G,S: Larger viral particles.
{ECO:0000269|PubMed:11799163}.
SEQUENCE 348 AA; 38557 MW; 367C3CAA6C4365CF CRC64;
MADIYRFPKF SYEDNGTVEP LPLRTGPDKK AIPHIRIVKV GDPPKHGVRY LDLLLLGFFE
TPKQTTNLGS VSDLTEPTSY SICGSGSLPI GVAKYYGTDQ ELLKACTDLR ITVRRTVRAG
EMIVYMVDSI GAPLLPWSGR LRQGMIFNAN KVALAPQCLP VDKDIRLRVV FVNGTSLGAI
TIAKIPKTLA DLALPNSISV NLLVTLKTGI STEQKGVLPV LDDQGEKKLN FMVHLGLIRR
KVGKIYSVEY CKSKIERMRL IFSLGLIGGI SFHVQVNGTL SKTFMSQLAW KRAVCFPLMD
VNPHMNMVIW AASVEITGVD AVFQPAIPRD FRYYPNVVAK NIGRIRKL


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