MTRX_AMPV1
ID MTRX_AMPV1 Reviewed; 254 AA.
AC Q2Y2M4;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 23-FEB-2022, entry version 41.
DE RecName: Full=Matrix protein;
GN Name=M;
OS Avian metapneumovirus (isolate Canada goose/Minnesota/15a/2001) (AMPV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Metapneumovirus.
OX NCBI_TaxID=652954;
OH NCBI_TaxID=8847; Anser sp. (goose).
OH NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15666873; DOI=10.1637/7208-051804r;
RA Bennett R.S., Nezworski J., Velayudhan B.T., Nagaraja K.V., Zeman D.H.,
RA Dyer N., Graham T., Lauer D.C., Njenga M.K., Halvorson D.A.;
RT "Evidence of avian pneumovirus spread beyond Minnesota among wild and
RT domestic birds in central North America.";
RL Avian Dis. 48:902-908(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16282483; DOI=10.1128/jvi.79.23.14834-14842.2005;
RA Bennett R.S., LaRue R., Shaw D., Yu Q., Nagaraja K.V., Halvorson D.A.,
RA Njenga M.K.;
RT "A wild goose metapneumovirus containing a large attachment glycoprotein is
RT avirulent but immunoprotective in domestic turkeys.";
RL J. Virol. 79:14834-14842(2005).
CC -!- FUNCTION: Has a crucial role in virus assembly and budding. The matrix
CC interacts with the RNP complex and this association serves two
CC functions: facilitate virion assembly and inhibit the viral
CC transcriptase activity. Early in infection, M is localized to the
CC nucleus and may inhibit host cell transcription. Later on, M can
CC associate with lipid rafts supposely by interacting with the
CC cytoskeleton and with the cytoplasmic tail of glycoprotein G. The
CC binding of M to host membrane is stabilized by the surface expression
CC of the viral glycoproteins. These interactions may allow virus
CC formation by mediating association of the nucleocapsid with the nascent
CC envelope (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with glycoprotein G (via N-terminus), and protein N.
CC Interacts with protein M2-1; this interaction mediates the association
CC between proteins M and N (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}. Host cytoplasm
CC {ECO:0000250}. Host nucleus {ECO:0000250}. Host cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Note=During bud formation, associates at the inner
CC side of the plasma membrane of infected cells. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the paramyxoviruses M protein family.
CC {ECO:0000305}.
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DR EMBL; DQ009484; AAY81656.1; -; Viral_cRNA.
DR RefSeq; YP_443839.1; NC_007652.1.
DR SMR; Q2Y2M4; -.
DR PRIDE; Q2Y2M4; -.
DR Proteomes; UP000002471; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; 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:0019031; C:viral envelope; IEA:InterPro.
DR GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
DR GO; GO:0019068; P:virion assembly; IEA:InterPro.
DR Gene3D; 2.70.20.30; -; 1.
DR InterPro; IPR005056; Pneu_matrix.
DR InterPro; IPR043062; Pneu_matrix_N.
DR Pfam; PF03393; Pneumo_matrix; 1.
PE 3: Inferred from homology;
KW Host cell membrane; Host cytoplasm; Host membrane; Host nucleus;
KW Host-virus interaction; Membrane; Reference proteome; Viral matrix protein;
KW Virion.
FT CHAIN 1..254
FT /note="Matrix protein"
FT /id="PRO_0000390369"
SQ SEQUENCE 254 AA; 27622 MW; 73DACAB5E03304A4 CRC64;
MESYLVDTYQ GVPYTAAVQT DLVEKDQLPA RLTVWFPLFQ TNTPPTVLLE QLKTLTITTL
YTASQNGPIL KVNASAQGAA MSALPKSFDV SASVALDDYS KLEFDKLTVC ELKAVYLTTM
KPYGMVSKFV NSAKAVGKKT HDLIALCDFL DLEKGVPVTI PAYIKSVSIK ESESATVEAA
IGGEADQAIT QARIAPYAGL IMIMTMNNPK GIFKKLGAGV QVIVELGAYV QAESISRICR
NWSHQGTRYV LKSR