MATRX_SENDH
ID MATRX_SENDH Reviewed; 348 AA.
AC P03426;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 29-SEP-2021, entry version 85.
DE RecName: Full=Matrix protein;
DE Short=M protein;
GN Name=M;
OS Sendai virus (strain Harris) (SeV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Respirovirus.
OX NCBI_TaxID=11196;
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=6092688; DOI=10.1128/jvi.52.2.656-663.1984;
RA Blumberg B.M., Rose K., Simona M.G., Roux L., Giorgi C., Kolakofsky D.;
RT "Analysis of the Sendai virus M gene and protein.";
RL J. Virol. 52:656-663(1984).
RN [2]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 112-THR-VAL-113.
RX PubMed=8661424; DOI=10.1006/viro.1996.0362;
RA Mottet G., Muehlemann A., Tapparel C., Hoffmann F., Roux L.;
RT "A Sendai virus vector leading to the efficient expression of mutant M
RT proteins interfering with virus particle budding.";
RL Virology 221:159-171(1996).
RN [3]
RP INTERACTION WITH MEMBRANE, AND MUTAGENESIS OF THR-112; VAL-113 AND
RP 112-THR-VAL-113.
RX PubMed=10580060; DOI=10.1099/0022-1317-80-11-2977;
RA Mottet G., Mueller V., Roux L.;
RT "Characterization of Sendai virus M protein mutants that can partially
RT interfere with virus particle production.";
RL J. Gen. Virol. 80:2977-2986(1999).
CC -!- FUNCTION: 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 (By similarity). Plays a crucial
CC role in virion assembly and budding. Forms a shell at the inner face of
CC the plasma membrane and concentrates the HN and F glycoproteins.
CC {ECO:0000250}.
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:0000250|UniProtKB:P06446}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm
CC {ECO:0000269|PubMed:8661424}. Host cell membrane
CC {ECO:0000269|PubMed:8661424}; Peripheral membrane protein
CC {ECO:0000269|PubMed:8661424}; Cytoplasmic side
CC {ECO:0000269|PubMed:8661424}. 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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the morbillivirus/respirovirus/rubulavirus M
CC protein family. {ECO:0000305}.
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DR EMBL; K02742; AAA47811.1; -; Genomic_RNA.
DR PIR; A04042; MFNZS.
DR SMR; P03426; -.
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; 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_0000142774"
FT MOTIF 50..53
FT /note="YLDL motif"
FT /evidence="ECO:0000250"
FT MOD_RES 70
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT MUTAGEN 112..113
FT /note="TV->EE,KE: Not incorporated in virions. No effect on
FT in vitro membrane association."
FT /evidence="ECO:0000269|PubMed:10580060"
FT MUTAGEN 112..113
FT /note="TV->KR,ME: Not incorporated in virions. Loss of
FT efficient in vivo transport to the plasma membrane. 60%
FT loss of in vitro membrane association. Reduces
FT nucleocapsid-membrane association. Loss of interaction with
FT itself."
FT /evidence="ECO:0000269|PubMed:10580060"
FT MUTAGEN 112..113
FT /note="TV->RE: Not incorporated in virions."
FT /evidence="ECO:0000269|PubMed:10580060,
FT ECO:0000269|PubMed:8661424"
FT MUTAGEN 112
FT /note="T->E,M: No effect."
FT /evidence="ECO:0000269|PubMed:10580060"
FT MUTAGEN 112
FT /note="T->K,R: 20% increase of in vitro membrane
FT association."
FT /evidence="ECO:0000269|PubMed:10580060"
FT MUTAGEN 113
FT /note="V->A: Not incorporated in virions."
FT /evidence="ECO:0000269|PubMed:10580060"
FT MUTAGEN 113
FT /note="V->C: No effect."
FT /evidence="ECO:0000269|PubMed:10580060"
FT MUTAGEN 113
FT /note="V->E: Not incorporated in virions. 50% loss of in
FT vitro membrane association."
FT /evidence="ECO:0000269|PubMed:10580060"
FT MUTAGEN 113
FT /note="V->F,K,L,R: Not incorporated in virions."
FT /evidence="ECO:0000269|PubMed:10580060"
SQ SEQUENCE 348 AA; 38590 MW; C1C0133694F16F88 CRC64;
MADIYRFPKF SYEDNGTVEP LPLRTGSDKK AIPYIRIIKV GDPPKHGVRY LDLLLLGFFE
TPKQTTNLGS VSDLTEPTSY SICGSGSLPI GVAKYYGTDQ ELLKACTDLR ITVRRTVRAG
EMIVYMVDSI GAPLLPWSGR LRQGMIFNAN KVALAPQCLP VDKDIRFRVV FVNGTSLGAI
TIAKIPKTLA DLALPNSISV NLLVTLKTGI STEQKGVLPV LDDQGEKKLN FMVHLGLIRR
KVGKIYSVEY CKSKIERMRL IFSLGLIGGI SFHVQVTGTL SKTFMSQLAW KRAVCFPLMD
VNPHMNLVIW AASVEITGVD AVFQPAIPRD FRYYPNVVAK NIGRIRKL
