MATRX_NIPAV
ID MATRX_NIPAV Reviewed; 352 AA.
AC Q9IK90; Q5K4E0;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 29-SEP-2021, entry version 69.
DE RecName: Full=Matrix protein;
DE Short=Protein M;
GN Name=M;
OS Nipah virus.
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Henipavirus.
OX NCBI_TaxID=121791;
OH NCBI_TaxID=58060; Cynopterus brachyotis (Lesser short-nosed fruit bat) (Pachysoma brachyotis).
OH NCBI_TaxID=58065; Eonycteris spelaea (Lesser dawn bat) (Macroglossus spelaeus).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9405; Pteropus hypomelanus (Island flying fox) (Variable flying fox).
OH NCBI_TaxID=132908; Pteropus vampyrus (Large flying fox).
OH NCBI_TaxID=153297; Scotophilus kuhlii (Lesser asiatic yellow bat).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10827955; DOI=10.1126/science.288.5470.1432;
RA Chua K.B., Bellini W.J., Rota P.A., Harcourt B.H., Tamin A., Lam S.K.,
RA Ksiazek T.G., Rollin P.E., Zaki S.R., Shieh W., Goldsmith C.S.,
RA Gubler D.J., Roehrig J.T., Eaton B., Gould A.R., Olson J., Field H.,
RA Daniels P., Ling A.E., Peters C.J., Anderson L.J., Mahy B.W.;
RT "Nipah virus: a recently emergent deadly paramyxovirus.";
RL Science 288:1432-1435(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11504554; DOI=10.1006/viro.2001.1026;
RA Harcourt B.H., Tamin A., Halpin K., Ksiazek T.G., Rollin P.E.,
RA Bellini W.J., Rota P.A.;
RT "Molecular characterization of the polymerase gene and genomic termini of
RT Nipah virus.";
RL Virology 287:192-201(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate UMMC1, and Isolate UMMC2;
RX PubMed=11514724; DOI=10.1099/0022-1317-82-9-2151;
RA Chan Y.P., Chua K.B., Koh C.L., Lim M.E., Lam S.K.;
RT "Complete nucleotide sequences of Nipah virus isolates from Malaysia.";
RL J. Gen. Virol. 82:2151-2155(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11880045; DOI=10.1016/s1286-4579(01)01522-2;
RA Chua K.B., Koh C.L., Hooi P.S., Wee K.F., Khong J.H., Chua B.H., Chan Y.P.,
RA Lim M.E., Lam S.K.;
RT "Isolation of Nipah virus from Malaysian island flying-foxes.";
RL Microbes Infect. 4:145-151(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate NiV/MY/99/UM-0128, Isolate NiV/MY/99/VRI-1413, and
RC Isolate NiV/MY/99/VRI-2794;
RX PubMed=15663869; DOI=10.3201/eid1012.040452;
RA Abubakar S., Chang L.Y., Mohdali A.R., Sharifah S.H., Yusoff K., Zamrod Z.;
RT "Isolation and molecular identification of Nipah virus from pigs.";
RL Emerg. Infect. Dis. 10:2228-2230(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate NiV/MY/99/VRI-0626;
RA Abubakar S., Li-Yen C., Mohdali A.R., Sharifah S.H.;
RT "Identification of a new Nipah virus strain from pigs.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF TYR-62.
RX PubMed=17005661; DOI=10.1128/jvi.01743-06;
RA Ciancanelli M.J., Basler C.F.;
RT "Mutation of YMYL in the Nipah virus matrix protein abrogates budding and
RT alters subcellular localization.";
RL J. Virol. 80:12070-12078(2006).
RN [8]
RP FUNCTION.
RX PubMed=17204159; DOI=10.1186/1743-422x-4-1;
RA Patch J.R., Crameri G., Wang L.F., Eaton B.T., Broder C.C.;
RT "Quantitative analysis of Nipah virus proteins released as virus-like
RT particles reveals central role for the matrix protein.";
RL Virol. J. 4:1-1(2007).
RN [9]
RP FUNCTION, MUTAGENESIS OF TYR-92; PRO-93 AND LEU-94, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19000317; DOI=10.1186/1743-422x-5-137;
RA Patch J.R., Han Z., McCarthy S.E., Yan L., Wang L.F., Harty R.N.,
RA Broder C.C.;
RT "The YPLGVG sequence of the Nipah virus matrix protein is required for
RT budding.";
RL Virol. J. 5:137-137(2008).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION, MUTAGENESIS OF LYS-258, AND
RP MOTIF.
RX PubMed=21085610; DOI=10.1371/journal.ppat.1001186;
RA Wang Y.E., Park A., Lake M., Pentecost M., Torres B., Yun T.E., Wolf M.C.,
RA Holbrook M.R., Freiberg A.N., Lee B.;
RT "Ubiquitin-regulated nuclear-cytoplasmic trafficking of the Nipah virus
RT matrix protein is important for viral budding.";
RL PLoS Pathog. 6:e1001186-e1001186(2010).
RN [11]
RP INTERACTION WITH HOST TRIM6, AND FUNCTION.
RX PubMed=27622505; DOI=10.1371/journal.ppat.1005880;
RA Bharaj P., Wang Y.E., Dawes B.E., Yun T.E., Park A., Yen B., Basler C.F.,
RA Freiberg A.N., Lee B., Rajsbaum R.;
RT "The Matrix Protein of Nipah Virus Targets the E3-Ubiquitin Ligase TRIM6 to
RT Inhibit the IKKepsilon Kinase-Mediated Type-I IFN Antiviral Response.";
RL PLoS Pathog. 12:e1005880-e1005880(2016).
RN [12]
RP FUNCTION.
RX PubMed=28250132; DOI=10.1128/jvi.02150-16;
RA Johnston G.P., Contreras E.M., Dabundo J., Henderson B.A., Matz K.M.,
RA Ortega V., Ramirez A., Park A., Aguilar H.C.;
RT "Cytoplasmic Motifs in the Nipah Virus Fusion Protein Modulate Virus
RT Particle Assembly and Egress.";
RL J. Virol. 91:0-0(2017).
CC -!- FUNCTION: Plays a crucial role in virion assembly and budding. Forms a
CC shell at the inner face of the plasma membrane (PubMed:17005661,
CC PubMed:17204159, PubMed:19000317). Transits through the host nucleus
CC before gaining the functional ability to localize and bud from the
CC plasma membrane (PubMed:21085610). Mediates together with fusion
CC protein the incorporation of the glycoprotein to the viral particles
CC (PubMed:28250132). Participates also in the inhibition of the host
CC interferon type I antiviral response by interacting with and thereby
CC inhibiting host TRIM6 (PubMed:27622505). {ECO:0000250,
CC ECO:0000269|PubMed:17005661, ECO:0000269|PubMed:17204159,
CC ECO:0000269|PubMed:19000317, ECO:0000269|PubMed:21085610,
CC ECO:0000269|PubMed:27622505, ECO:0000269|PubMed:28250132}.
CC -!- SUBUNIT: Homomultimer (PubMed:17005661). Interacts with host TRIM6;
CC this interaction inhibits the IKBKE-dependent activation of the type I
CC interferon signaling pathway (PubMed:27622505). Interacts with host
CC ANP32B; this interaction promotes M nuclear localization (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:17005661,
CC ECO:0000269|PubMed:27622505}.
CC -!- INTERACTION:
CC Q9IK90; Q9UPY3: DICER1; Xeno; NbExp=3; IntAct=EBI-25747115, EBI-395506;
CC -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm. Host cell membrane
CC {ECO:0000269|PubMed:17005661, ECO:0000269|PubMed:19000317,
CC ECO:0000269|PubMed:21085610}. Host nucleus
CC {ECO:0000269|PubMed:21085610}. Note=During bud formation, associates at
CC the inner side of the plasma membrane of infected cells. Nuclear-
CC cytoplasmic trafficking is essential for budding and requires matrix
CC ubiquitination. {ECO:0000269|PubMed:21085610}.
CC -!- PTM: Ubiquitinated; regulates matrix nuclear export.
CC {ECO:0000269|PubMed:21085610}.
CC -!- SIMILARITY: Belongs to the morbillivirus/respirovirus/rubulavirus M
CC protein family. {ECO:0000305}.
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DR EMBL; AF212302; AAF73379.1; -; Genomic_RNA.
DR EMBL; AY029767; AAK50543.1; -; Genomic_RNA.
DR EMBL; AY029768; AAK50552.1; -; Genomic_RNA.
DR EMBL; AF376747; AAM13404.1; -; Genomic_RNA.
DR EMBL; AJ564621; CAD92349.1; -; Genomic_RNA.
DR EMBL; AJ564622; CAD92355.1; -; Genomic_RNA.
DR EMBL; AJ564623; CAD92361.1; -; Genomic_RNA.
DR EMBL; AJ627196; CAF25495.1; -; Genomic_RNA.
DR RefSeq; NP_112025.1; NC_002728.1.
DR SMR; Q9IK90; -.
DR IntAct; Q9IK90; 20.
DR MINT; Q9IK90; -.
DR GeneID; 920953; -.
DR KEGG; vg:920953; -.
DR Proteomes; UP000002330; Genome.
DR Proteomes; UP000007527; Genome.
DR Proteomes; UP000008676; Genome.
DR Proteomes; UP000100567; Genome.
DR Proteomes; UP000110983; Genome.
DR Proteomes; UP000130871; Genome.
DR Proteomes; UP000170143; 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:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
DR GO; GO:0019068; P:virion assembly; IEA:InterPro.
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 nucleus;
KW Host-virus interaction; Membrane; Reference proteome; Ubl conjugation;
KW Viral matrix protein; Virion.
FT CHAIN 1..352
FT /note="Matrix protein"
FT /id="PRO_0000236001"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 106..115
FT /note="Nuclear export signal 1"
FT /evidence="ECO:0000269|PubMed:21085610"
FT MOTIF 244..258
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:21085610"
FT MOTIF 268..276
FT /note="Nuclear export signal 2"
FT /evidence="ECO:0000269|PubMed:21085610"
FT VARIANT 147
FT /note="S -> G (in strain: Isolate NiV/MY/99/VRI-0626)"
FT MUTAGEN 62
FT /note="Y->A: Complete loss of budding."
FT /evidence="ECO:0000269|PubMed:17005661"
FT MUTAGEN 92
FT /note="Y->A: Complete loss of budding."
FT /evidence="ECO:0000269|PubMed:17005661"
FT MUTAGEN 93
FT /note="P->A: Complete loss of budding."
FT /evidence="ECO:0000269|PubMed:17005661"
FT MUTAGEN 94
FT /note="L->A: Complete loss of budding."
FT /evidence="ECO:0000269|PubMed:17005661"
FT MUTAGEN 258
FT /note="K->A: Complete loss of membrane association and
FT budding."
FT /evidence="ECO:0000269|PubMed:21085610"
FT MUTAGEN 258
FT /note="K->R: Complete loss of membrane association and
FT budding."
FT /evidence="ECO:0000269|PubMed:21085610"
SQ SEQUENCE 352 AA; 39928 MW; 08F7B3906A07B605 CRC64;
MEPDIKSISS ESMEGVSDFS PSSWEHGGYL DKVEPEIDEN GSMIPKYKIY TPGANERKYN
NYMYLICYGF VEDVERTPET GKRKKIRTIA AYPLGVGKSA SHPQDLLEEL CSLKVTVRRT
AGSTEKIVFG SSGPLNHLVP WKKVLTSGSI FNAVKVCRNV DQIQLDKHQA LRIFFLSITK
LNDSGIYMIP RTMLEFRRNN AIAFNLLVYL KIDADLSKMG IQGSLDKDGF KVASFMLHLG
NFVRRAGKYY SVDYCRRKID RMKLQFSLGS IGGLSLHIKI NGVISKRLFA QMGFQKNLCF
SLMDINPWLN RLTWNNSCEI SRVAAVLQPS IPREFMIYDD VFIDNTGRIL KG
