ID   MATRX_SENDE             Reviewed;         348 AA.
AC   Q88428;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   29-SEP-2021, entry version 74.
DE   RecName: Full=Matrix protein;
DE            Short=M protein;
GN   Name=M;
OS   Sendai virus (strain Enders) (SeV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Respirovirus.
OX   NCBI_TaxID=11194;
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=7494321; DOI=10.1128/jvi.69.12.8057-8060.1995;
RA   Cole G.A., Tao T., Hogg T.L., Ryan K.W., Woodland D.L.;
RT   "Binding motifs predict major histocompatibility complex class II-
RT   restricted epitopes in the Sendai virus M protein.";
RL   J. Virol. 69:8057-8060(1995).
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 (By similarity). {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:0000250}. Host cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=During bud
CC       formation, associates at the inner side of the plasma membrane of
CC       infected cells. {ECO:0000250}.
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; U31956; AAB60595.1; -; Genomic_RNA.
DR   SMR; Q88428; -.
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   3: Inferred from homology;
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_0000142772"
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"
SQ   SEQUENCE   348 AA;  38472 MW;  B9BA09AA67677F4D CRC64;
     MADIYRFPKF SYEDNGTVEP LPLRTGPDKK AIPHIRIIKV GVPPKHGVRY LDLLLLGFFE
     TPKQTTNLGS VSDLTEPTSY SICGSGSLPI GVAKYYGTDQ ELLKACTDLR ITVRRTVRAG
     EMIVYMVGSI GAPLLPWSGR LRQGMIFNAN KVALAPQCLP VDKDIRLRVV FVNGTSLGAI
     TIAKIPKTLA DLALPNSISV NLLVTLKTGI STEQKGVLPV LDDQGEKKLN FMVHLGLIRR
     KVGKIYSVEY CKSKIERMRL IFSLGLTGGI SFHVQVTGTL SKTFMSQLAW KRAVCFPLMD
     VNPHMNMVIW AASVEITGVD AVFQPAIPRD FRYYPNVVAK NIGRIRKL