MATRX_SENDZ
ID MATRX_SENDZ Reviewed; 348 AA.
AC P06446; P27567; Q91UL5; Q9YIJ5; Q9YIM6; Q9YNG5; Q9YNG6; Q9YNG7; Q9YNG8;
AC Q9YNG9; Q9YNH0; Q9YZ78;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 29-SEP-2021, entry version 91.
DE RecName: Full=Matrix protein;
DE Short=M protein;
GN Name=M;
OS Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Respirovirus.
OX NCBI_TaxID=11198;
OH NCBI_TaxID=10144; Cavia cutleri (Guinea pig).
OH NCBI_TaxID=36483; Cricetidae sp. (Hamster).
OH NCBI_TaxID=10090; Mus musculus (Mouse).
OH NCBI_TaxID=10116; Rattus norvegicus (Rat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6095182; DOI=10.1093/nar/12.21.7965;
RA Hidaka Y., Kanda T., Iwasaki K., Nomoto A., Shioda T., Shibuta H.;
RT "Nucleotide sequence of a Sendai virus genome region covering the entire M
RT gene and the 3' proximal 1013 nucleotides of the F gene.";
RL Nucleic Acids Res. 12:7965-7973(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Mutant F1-R, and Mutant ts-f1;
RX PubMed=2161155; DOI=10.1016/0042-6822(90)90040-x;
RA Middleton Y., Tashiro M., Thai T., Oh J., Seymour J., Pritzer E.,
RA Klenk H.-D., Rott R., Seto J.T.;
RT "Nucleotide sequence analyses of the genes encoding the HN, M, NP, P, and L
RT proteins of two host range mutants of Sendai virus.";
RL Virology 176:656-657(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Mutant F1-R / T-5 revertant;
RX PubMed=1651590; DOI=10.1016/0042-6822(91)90839-4;
RA Tashiro M., James I., Karri S., Wahn K., Tobita K., Klenk H.-D., Rott R.,
RA Seto J.T.;
RT "Pneumotropic revertants derived from a pantropic mutant, F1-R, of Sendai
RT virus.";
RL Virology 184:227-234(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Mutant KD-11M, Mutant KD-22M, Mutant KD-32M, Mutant KD-51M, and
RC Mutant KD-52M;
RX PubMed=1312267; DOI=10.1016/0042-6822(92)90443-s;
RA Tashiro M., Seto J.T., Choosakul S., Yamakawa M., Klenk H.-D., Rott R.;
RT "Budding site of Sendai virus in polarized epithelial cells is one of the
RT determinants for tropism and pathogenicity in mice.";
RL Virology 187:413-422(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Mutant BF-13, Mutant BF-132, Mutant BF-53, Mutant BF-82,
RC Mutant BY-4, Mutant BY-41, Mutant BY-5, and Mutant BY-8;
RX PubMed=9930191; DOI=10.1007/s007050050465;
RA Okada H., Seto J.T., McQueen N.L., Klenk H.-D., Rott R., Tashiro M.;
RT "Determinants of pantropism of the F1-R mutant of Sendai virus: specific
RT mutations involved are in the F and M genes.";
RL Arch. Virol. 143:2343-2352(1998).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=6285608; DOI=10.1016/0042-6822(82)90036-8;
RA Buechi M., Baechi T.;
RT "Microscopy of internal structures of Sendai virus associated with the
RT cytoplasmic surface of host membranes.";
RL Virology 120:349-359(1982).
RN [7]
RP PHOSPHORYLATION AT SER-70, AND MUTAGENESIS OF SER-70.
RX PubMed=9281516; DOI=10.1006/viro.1997.8701;
RA Sakaguchi T., Kiyotani K., Kato A., Asakawa M., Fujii Y., Nagai Y.,
RA Yoshida T.;
RT "Phosphorylation of the Sendai virus M protein is not essential for virus
RT replication either in vitro or in vivo.";
RL Virology 235:360-366(1997).
RN [8]
RP INTERACTION WITH F AND HN PROTEINS.
RX PubMed=11040121; DOI=10.1006/viro.2000.0556;
RA Ali A., Nayak D.P.;
RT "Assembly of Sendai virus: M protein interacts with F and HN proteins and
RT with the cytoplasmic tail and transmembrane domain of F protein.";
RL Virology 276:289-303(2000).
RN [9]
RP MUTAGENESIS OF CYS-83; CYS-106; CYS-158; CYS-251 AND CYS-295.
RX PubMed=11799163; DOI=10.1128/jvi.76.4.1682-1690.2002;
RA Sakaguchi T., Uchiyama T., Huang C., Fukuhara N., Kiyotani K., Nagai Y.,
RA Yoshida T.;
RT "Alteration of Sendai virus morphogenesis and nucleocapsid incorporation
RT due to mutation of cysteine residues of the matrix protein.";
RL J. Virol. 76:1682-1690(2002).
RN [10]
RP INTERACTION WITH HUMAN ALPHA/BETA TUBULINS.
RX PubMed=14592411; DOI=10.1016/j.bbrc.2003.09.205;
RA Ogino T., Iwama M., Ohsawa Y., Mizumoto K.;
RT "Interaction of cellular tubulin with Sendai virus M protein regulates
RT transcription of viral genome.";
RL Biochem. Biophys. Res. Commun. 311:283-293(2003).
RN [11]
RP INTERACTION WITH HOST ANP32B.
RX PubMed=31793855; DOI=10.1099/jgv.0.001362;
RA Guenther M., Bauer A., Mueller M., Zaeck L., Finke S.;
RT "Interaction of host cellular factor ANP32B with matrix proteins of
RT different paramyxoviruses.";
RL J. Gen. Virol. 101:44-58(2020).
CC -!- FUNCTION: Plays a crucial role in virion assembly and budding. Forms a
CC shell at the inner face of the plasma membrane and concentrates the HN
CC and F glycoproteins. Acts as a negative regulator for transcription and
CC replication by sticking to the nucleocapsid. This effect might be
CC regulated by the cytoplasmic interaction with tubulin that dissociates
CC the M protein from the nucleocapsid.
CC -!- SUBUNIT: Homomultimer. Binds to the cytoplasmic regions of F and HN
CC proteins. Interacts with nucleocapsid. Interacts with human alpha-
CC tubulin and beta-tubulin. Interacts with host ANP32B.
CC {ECO:0000269|PubMed:11040121, ECO:0000269|PubMed:14592411,
CC ECO:0000269|PubMed:31793855}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm
CC {ECO:0000269|PubMed:6285608}. Host cell membrane
CC {ECO:0000269|PubMed:6285608}; Peripheral membrane protein
CC {ECO:0000269|PubMed:6285608}; Cytoplasmic side
CC {ECO:0000269|PubMed:6285608}. Note=During bud formation, associates at
CC the inner side of the plasma membrane of infected cells.
CC -!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
CC essential for viral particle budding. They recruit proteins of the host
CC ESCRT machinery (Endosomal Sorting Complex Required for Transport) or
CC ESCRT-associated proteins. The matrix protein contains one L domain: a
CC YLDL motif (By similarity). {ECO:0000250}.
CC -!- PTM: A large portion is phosphorylated in the cytoplasm, but not in
CC virion. However, this phosphorylation is not essential for virus
CC replication. {ECO:0000269|PubMed:9281516}.
CC -!- SIMILARITY: Belongs to the morbillivirus/respirovirus/rubulavirus M
CC protein family. {ECO:0000305}.
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DR EMBL; X00087; CAA24949.1; -; Genomic_RNA.
DR EMBL; M30202; AAB06280.1; -; Genomic_RNA.
DR EMBL; M30203; AAB06286.1; -; Genomic_RNA.
DR EMBL; M30204; AAB06198.1; -; Genomic_RNA.
DR EMBL; M69046; AAB06292.1; -; Genomic_RNA.
DR EMBL; AF001284; AAC82321.1; -; Genomic_RNA.
DR EMBL; U86424; AAC82304.1; -; Genomic_DNA.
DR EMBL; U86425; AAC82305.1; -; Genomic_DNA.
DR EMBL; U86426; AAC82306.1; -; Genomic_DNA.
DR EMBL; U86427; AAC82307.1; -; Genomic_DNA.
DR EMBL; U86428; AAC82308.1; -; Genomic_DNA.
DR EMBL; U86429; AAC82309.1; -; Genomic_DNA.
DR EMBL; U86430; AAC82310.1; -; Genomic_DNA.
DR EMBL; U86431; AAC82311.1; -; Genomic_DNA.
DR EMBL; U86432; AAC82312.1; -; Genomic_DNA.
DR EMBL; U86433; AAC82313.1; -; Genomic_DNA.
DR EMBL; U86434; AAC82314.1; -; Genomic_DNA.
DR EMBL; U86435; AAC82315.1; -; Genomic_DNA.
DR EMBL; U86436; AAC82316.1; -; Genomic_DNA.
DR PIR; A04043; MFNZSV.
DR SMR; P06446; -.
DR iPTMnet; P06446; -.
DR Proteomes; UP000006560; Genome.
DR Proteomes; UP000110830; Genome.
DR Proteomes; UP000163956; Genome.
DR Proteomes; UP000169749; Genome.
DR Proteomes; UP000181310; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
DR Gene3D; 2.70.20.50; -; 1.
DR Gene3D; 2.70.20.60; -; 1.
DR InterPro; IPR000982; Matrix.
DR InterPro; IPR042539; Matrix_C.
DR InterPro; IPR042540; Matrix_N.
DR Pfam; PF00661; Matrix; 1.
PE 1: Evidence at protein level;
KW Host cell membrane; Host cytoplasm; Host membrane; Host-virus interaction;
KW Membrane; Phosphoprotein; Reference proteome; Viral budding;
KW Viral budding via the host ESCRT complexes; Viral matrix protein;
KW Viral release from host cell; Virion.
FT CHAIN 1..348
FT /note="Matrix protein"
FT /id="PRO_0000142776"
FT MOTIF 50..53
FT /note="YLDL motif"
FT /evidence="ECO:0000250"
FT MOD_RES 70
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000305|PubMed:9281516"
FT VARIANT 42
FT /note="D -> V (in wild-type, Mutant F1-R, Mutant F1-R / T-5
FT revertant, Mutant ts-f1, Mutant KD-11M, Mutant KD-22M,
FT Mutant KD-32M, Mutant 51M and Mutant 52M)"
FT VARIANT 128
FT /note="D -> G (in Mutant F1-R and Mutant F1-R / T-5
FT revertant)"
FT VARIANT 128
FT /note="D -> V (in strain: Mutant BY-5)"
FT VARIANT 161
FT /note="V -> M (in strain: Mutant KD-32M)"
FT VARIANT 182
FT /note="I -> V (in strain: Mutant KD-22M)"
FT VARIANT 191
FT /note="D -> Y (in strain: Mutant KD-32M)"
FT VARIANT 197
FT /note="S -> C (in strain: Mutant KD-22M)"
FT VARIANT 210
FT /note="I -> T (in strain: Mutant F1-R and Mutant F1-R / T-5
FT revertant)"
FT VARIANT 211
FT /note="S -> F (in strain: Mutant KD-51M)"
FT VARIANT 212
FT /note="T -> A (in strain: Mutant KD-22M and Mutant KD-51M)"
FT VARIANT 217
FT /note="V -> A (in strain: Mutant KD-52M)"
FT VARIANT 232..233
FT /note="MV -> IL (in strain: Mutant BY-4)"
FT VARIANT 237
FT /note="L -> F (in strain: Mutant BY-4, Mutant BF-13 and
FT Mutant BY-41)"
FT VARIANT 237
FT /note="L -> M (in strain: Mutant KD-11M)"
FT VARIANT 240..241
FT /note="RK -> SL (in strain: Mutant KD-11M)"
FT VARIANT 253
FT /note="S -> C (in strain: Mutant KD-11M)"
FT VARIANT 264..267
FT /note="LGLI -> VGFV (in strain: Mutant BY-5)"
FT VARIANT 277
FT /note="N -> I (in strain: wild-type, Mutant F1-R, Mutant
FT F1-R / T-5 revertant, Mutant ts-f1, Mutant BY-4, Mutant BY-
FT 8, Mutant BY-13, Mutant BF-41, Mutant BF-53, Mutant BF-82,
FT Mutant BF-132, Mutant KD-22M, Mutant KD-32M, Mutant KD-51
FT and Mutant KD-52M)"
FT VARIANT 277
FT /note="N -> L (in strain: Mutant BY-5)"
FT VARIANT 279
FT /note="T -> R (in strain: Mutant BY-5)"
FT VARIANT 294
FT /note="V -> L (in strain: Mutant KD-52M)"
FT MUTAGEN 70
FT /note="S->A: Complete loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:9281516"
FT MUTAGEN 83
FT /note="C->S: Smaller viral particles."
FT /evidence="ECO:0000269|PubMed:11799163"
FT MUTAGEN 106
FT /note="C->S: Smaller viral particles."
FT /evidence="ECO:0000269|PubMed:11799163"
FT MUTAGEN 158
FT /note="C->S: Complete loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:11799163"
FT MUTAGEN 251
FT /note="C->S: Complete loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:11799163"
FT MUTAGEN 295
FT /note="C->A,G,S: Larger viral particles."
FT /evidence="ECO:0000269|PubMed:11799163"
SQ 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
