ID   MATRX_SENDO             Reviewed;         348 AA.
AC   O57299;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   29-SEP-2021, entry version 80.
DE   RecName: Full=Matrix protein;
DE            Short=M protein;
GN   Name=M;
OS   Sendai virus (strain Ohita) (SeV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Respirovirus.
OX   NCBI_TaxID=302272;
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].
RC   STRAIN=Isolate MVC11;
RX   PubMed=9400971; DOI=10.1099/0022-1317-78-12-3207;
RA   Itoh M., Isegawa Y., Hotta H., Homma M.;
RT   "Isolation of an avirulent mutant of Sendai virus with two amino acid
RT   mutations from a highly virulent field strain through adaptation to LLC-MK2
RT   cells.";
RL   J. Gen. Virol. 78:3207-3215(1997).
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; AB005795; BAA24389.1; -; Genomic_RNA.
DR   EMBL; AB005796; BAA24398.1; -; Genomic_RNA.
DR   RefSeq; NP_056876.1; NC_001552.1.
DR   SMR; O57299; -.
DR   GeneID; 1489778; -.
DR   KEGG; vg:1489778; -.
DR   Proteomes; UP000006563; Genome.
DR   Proteomes; UP000007311; 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:0046761; P:viral budding from plasma membrane; IDA:UniProtKB.
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; 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_0000142775"
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;  38501 MW;  419402309450F9F3 CRC64;
     MADIYRFPKF SYEDNGTVEP LPLRTGPDKK AIPHIRIVKV GDPPKHGVRY LDLLLLGFFE
     TPKQTASLGS VSDLTEHTGY SICGSGSLPI GVAKYHGSDQ ELLKACTDLR ITVRRTVRAG
     EMIVYMVDSI GAPLLPWSGR LRQGMIFNAN KVALAPQCLP VDKDIRFRVV FVNGTSLGAI
     TIAKIPKTLA DLALPNSISV NLLVTLKTGI STEQKGVLPV LDDQGEKKLN FMVHLGLIRR
     KVGKIYSVEY CKSKIERMRL IFSLGLIGGI SFHVQVTGTL SKTFMGQLAW KRAVCFPLMD
     VNPHMNLVIW AASVEITDVD AVFQPAIPRD FRYYPNVVAK NIGRIRKL