ID   MATRX_ISFV              Reviewed;         226 AA.
AC   Q5K2K5;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Matrix protein;
GN   Name=M;
OS   Isfahan virus (ISFV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Vesiculovirus.
OX   NCBI_TaxID=290008;
OH   NCBI_TaxID=10045; Gerbillinae (gerbils).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=29031; Phlebotomus papatasi (Sandfly).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=15614433; DOI=10.1007/s00705-004-0452-2;
RA   Marriott A.C.;
RT   "Complete genome sequences of Chandipura and Isfahan vesiculoviruses.";
RL   Arch. Virol. 150:671-680(2005).
CC   -!- FUNCTION: Plays a major role in assembly and budding of virion.
CC       Condensates the ribonucleocapsid core during virus assembly. Shut off
CC       cellular transcription by inhibiting mRNA nuclear export through direct
CC       interaction with host RAE1-NUP98 complex. This shutoff presumably
CC       inhibit interferon signaling and thus establishment of antiviral state
CC       in virus infected cells. Induces cell-rounding, cytoskeleton
CC       disorganization and apoptosis in infected cell (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homomultimer. Interacts with viral nucleocapsid (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane; Peripheral membrane protein.
CC       Host endomembrane system {ECO:0000250}; Peripheral membrane protein
CC       {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. M contains two overlapping L domains: a PPXY
CC       motif which interacts with the WW domain 3 of NEDD4 and a PTAP/PSAP
CC       motif, which interacts with the UEV domain of TSG101 (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylated by host. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Most abundant protein in the virion. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the vesiculoviruses matrix protein family.
CC       {ECO:0000305}.
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DR   EMBL; AJ810084; CAH17546.1; -; Genomic_RNA.
DR   RefSeq; YP_007641384.1; NC_020806.1.
DR   SMR; Q5K2K5; -.
DR   GeneID; 14857917; -.
DR   KEGG; vg:14857917; -.
DR   Proteomes; UP000204017; Genome.
DR   GO; GO:0033645; C:host cell endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:InterPro.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
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; 3.10.460.10; -; 1.
DR   InterPro; IPR009397; Vesiculo_matrix.
DR   InterPro; IPR036711; VSV_matrix_sf.
DR   Pfam; PF06326; Vesiculo_matrix; 1.
DR   SUPFAM; SSF75404; SSF75404; 1.
PE   3: Inferred from homology;
KW   Apoptosis; Host membrane; Host-virus interaction; Membrane; Phosphoprotein;
KW   Viral budding; Viral budding via the host ESCRT complexes;
KW   Viral matrix protein; Viral release from host cell; Virion.
FT   CHAIN           1..226
FT                   /note="Matrix protein"
FT                   /id="PRO_0000287255"
FT   MOTIF           28..31
FT                   /note="PPXY motif"
FT   MOTIF           40..43
FT                   /note="PTAP/PSAP motif"
SQ   SEQUENCE   226 AA;  25865 MW;  9C52FCEDDA785A95 CRC64;
     MKSLKRLIKS NKKKGDKKNV SFMDWDEPPS YSDSRYGCYP SAPLFGVDEM METLPTLGIQ
     SLKIQYKCSL QVRAETPFTS FNDAARCISL WETDYRGYAG KKPFYRLLML IATKKLRAAP
     MSLMDGNRPE YSSMIQGQSI VHHSLGVIPP MMHVPETFTR EWNLLTNKGM ITAQIWLGIT
     DVVDDLNPLI NPALFSDEKE MTLTSQMFGL ELKKRNDNTW LISKSY