MATRX_NDVA
ID MATRX_NDVA Reviewed; 364 AA.
AC P11206;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 02-JUN-2021, entry version 69.
DE RecName: Full=Matrix protein;
GN Name=M;
OS Newcastle disease virus (strain Chicken/Australia-Victoria/32) (NDV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Avulavirinae;
OC Orthoavulavirus; Avian orthoavulavirus 1.
OX NCBI_TaxID=11177;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3027973; DOI=10.1016/0042-6822(87)90401-6;
RA McGinnes L.W., Morrison T.G.;
RT "The nucleotide sequence of the gene encoding the Newcastle disease virus
RT membrane protein and comparisons of membrane protein sequences.";
RL Virology 156:221-228(1987).
CC -!- FUNCTION: The M protein has a crucial role in virus assembly and
CC interacts with the RNP complex as well as with the viral membrane.
CC -!- INTERACTION:
CC P11206; P11206: M; NbExp=3; IntAct=EBI-25764833, EBI-25764833;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
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 FPIV motif (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the morbillivirus/respirovirus/rubulavirus M
CC protein family. {ECO:0000305}.
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DR EMBL; M16622; AAA46673.1; -; mRNA.
DR PIR; A27530; MFNZNV.
DR PDB; 4G1G; X-ray; 2.20 A; A/B=1-364.
DR PDB; 4G1L; X-ray; 2.21 A; A/B=1-364.
DR PDB; 4G1O; X-ray; 2.20 A; A/B=1-364.
DR PDBsum; 4G1G; -.
DR PDBsum; 4G1L; -.
DR PDBsum; 4G1O; -.
DR SASBDB; P11206; -.
DR SMR; P11206; -.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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 1: Evidence at protein level;
KW 3D-structure; Host-virus interaction; Viral budding;
KW Viral budding via the host ESCRT complexes; Viral envelope protein;
KW Viral matrix protein; Viral release from host cell; Virion.
FT CHAIN 1..364
FT /note="Matrix protein"
FT /id="PRO_0000142759"
FT MOTIF 23..26
FT /note="FPIV motif"
FT /evidence="ECO:0000250"
FT HELIX 17..22
FT /evidence="ECO:0007829|PDB:4G1G"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:4G1L"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:4G1G"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:4G1G"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:4G1O"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:4G1G"
FT STRAND 55..67
FT /evidence="ECO:0007829|PDB:4G1G"
FT STRAND 85..99
FT /evidence="ECO:0007829|PDB:4G1G"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:4G1G"
FT STRAND 114..133
FT /evidence="ECO:0007829|PDB:4G1G"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:4G1G"
FT HELIX 142..146
FT /evidence="ECO:0007829|PDB:4G1G"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:4G1G"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:4G1G"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:4G1G"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:4G1G"
FT STRAND 169..182
FT /evidence="ECO:0007829|PDB:4G1G"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:4G1G"
FT HELIX 191..195
FT /evidence="ECO:0007829|PDB:4G1G"
FT STRAND 201..212
FT /evidence="ECO:0007829|PDB:4G1G"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:4G1G"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:4G1G"
FT STRAND 228..246
FT /evidence="ECO:0007829|PDB:4G1G"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:4G1G"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:4G1G"
FT HELIX 257..264
FT /evidence="ECO:0007829|PDB:4G1G"
FT STRAND 266..282
FT /evidence="ECO:0007829|PDB:4G1G"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:4G1G"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:4G1G"
FT STRAND 298..303
FT /evidence="ECO:0007829|PDB:4G1G"
FT HELIX 304..307
FT /evidence="ECO:0007829|PDB:4G1G"
FT HELIX 309..317
FT /evidence="ECO:0007829|PDB:4G1G"
FT STRAND 320..333
FT /evidence="ECO:0007829|PDB:4G1G"
FT HELIX 334..339
FT /evidence="ECO:0007829|PDB:4G1G"
FT STRAND 343..347
FT /evidence="ECO:0007829|PDB:4G1O"
SQ SEQUENCE 364 AA; 39746 MW; AADEFB6D46DC05D8 CRC64;
MDSSRTIGLY FDSALPSSNL LAFPIVLQDI GDGKKQIAPQ YRIQRLDSWT DSKEDSVFIT
TYGFIFQVGN EEVTVGMISD NPKHELLSAA MLCLGSVPNV GDLVELARAC LTMVVTCKKS
ATDTERMVFS VVQAPQVLQS CRVVANKYSS VNAVKHVKAP EKIPGSGTLE YKVNFVSLTV
VPRKDVYKIP TAALKVSGSS LYNLALNVTI DVEVDPKSPL VKSLSKSDSG YYANLFLHIG
LMSTVDKKGK KVTFDKLERK IRRLDLSVGL SDVLGPSVLV KARGARTRLL APFFSSSGTA
CYPISNASPQ VAKILWSQTA RLRSVKVIIQ AGTQRAVAVT ADHEVTSTKI EKRHTIAKYN
PFKK
