MATRX_HENDH
ID MATRX_HENDH Reviewed; 352 AA.
AC O89341; Q66760;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 2.
DT 29-SEP-2021, entry version 67.
DE RecName: Full=Matrix protein;
DE Short=Protein M;
GN Name=M;
OS Hendra virus (isolate Horse/Autralia/Hendra/1994).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Henipavirus.
OX NCBI_TaxID=928303;
OH NCBI_TaxID=9796; Equus caballus (Horse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9402; Pteropus alecto (Black flying fox).
OH NCBI_TaxID=9403; Pteropus poliocephalus (Grey-headed flying fox).
OH NCBI_TaxID=94117; Pteropus scapulatus (Little red flying fox).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8822631; DOI=10.1016/0168-1702(96)01308-1;
RA Gould A.R.;
RT "Comparison of the deduced matrix and fusion protein sequences of equine
RT morbillivirus with cognate genes of the Paramyxoviridae.";
RL Virus Res. 43:17-31(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11024125; DOI=10.1128/jvi.74.21.9972-9979.2000;
RA Wang L.-F., Yu M., Hansson E., Pritchard L.I., Shiell B., Michalski W.P.,
RA Eaton B.T.;
RT "The exceptionally large genome of Hendra virus: support for creation of a
RT new genus within the family Paramyxoviridae.";
RL J. Virol. 74:9972-9979(2000).
RN [3]
RP INTERACTION WITH HOST ANP32B, AND SUBCELLULAR LOCATION.
RX PubMed=24823948; DOI=10.1371/journal.pone.0097233;
RA Bauer A., Neumann S., Karger A., Henning A.K., Maisner A., Lamp B.,
RA Dietzel E., Kwasnitschka L., Balkema-Buschmann A., Keil G.M., Finke S.;
RT "ANP32B is a nuclear target of henipavirus M proteins.";
RL PLoS ONE 9:e97233-e97233(2014).
CC -!- FUNCTION: Plays a crucial role in virion assembly and budding. Forms a
CC shell at the inner face of the plasma membrane (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homomultimer. Interacts with host ANP32B; this interaction
CC promotes M nuclear localization. {ECO:0000269|PubMed:24823948}.
CC -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm. Host nucleus
CC {ECO:0000269|PubMed:24823948}. Note=During bud formation, associates at
CC the inner side of the plasma membrane of infected cells. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the morbillivirus/respirovirus/rubulavirus M
CC protein family. {ECO:0000305}.
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DR EMBL; U49404; AAB39504.1; -; Genomic_RNA.
DR EMBL; AF017149; AAC83191.2; -; Genomic_RNA.
DR PIR; T08209; T08209.
DR RefSeq; NP_047110.2; NC_001906.3.
DR PDB; 6BK6; X-ray; 2.50 A; A=1-352.
DR PDBsum; 6BK6; -.
DR SMR; O89341; -.
DR PRIDE; O89341; -.
DR GeneID; 1446472; -.
DR KEGG; vg:1446472; -.
DR Proteomes; UP000008771; 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: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 3D-structure; Host cytoplasm; Host nucleus; Host-virus interaction;
KW Reference proteome; Viral matrix protein; Virion.
FT CHAIN 1..352
FT /note="Matrix protein"
FT /id="PRO_0000236000"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 84
FT /note="K -> N (in Ref. 1; AAB39504)"
FT /evidence="ECO:0000305"
FT CONFLICT 103..112
FT /note="PQDLLEELCS -> RCEDPFRRAMF (in Ref. 1; AAB39504)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="E -> Y (in Ref. 1; AAB39504)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="N -> K (in Ref. 1; AAB39504)"
FT /evidence="ECO:0000305"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:6BK6"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:6BK6"
FT STRAND 62..73
FT /evidence="ECO:0007829|PDB:6BK6"
FT STRAND 86..98
FT /evidence="ECO:0007829|PDB:6BK6"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:6BK6"
FT STRAND 113..133
FT /evidence="ECO:0007829|PDB:6BK6"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:6BK6"
FT HELIX 142..146
FT /evidence="ECO:0007829|PDB:6BK6"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:6BK6"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:6BK6"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:6BK6"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:6BK6"
FT STRAND 169..184
FT /evidence="ECO:0007829|PDB:6BK6"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:6BK6"
FT STRAND 201..211
FT /evidence="ECO:0007829|PDB:6BK6"
FT STRAND 232..243
FT /evidence="ECO:0007829|PDB:6BK6"
FT HELIX 252..260
FT /evidence="ECO:0007829|PDB:6BK6"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:6BK6"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:6BK6"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:6BK6"
FT HELIX 286..291
FT /evidence="ECO:0007829|PDB:6BK6"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:6BK6"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:6BK6"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:6BK6"
FT HELIX 307..311
FT /evidence="ECO:0007829|PDB:6BK6"
FT TURN 312..315
FT /evidence="ECO:0007829|PDB:6BK6"
FT STRAND 319..332
FT /evidence="ECO:0007829|PDB:6BK6"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:6BK6"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:6BK6"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:6BK6"
SQ SEQUENCE 352 AA; 39827 MW; 79E232D4496222D5 CRC64;
MDFSVSDNLD DPIEGVSDFS PTSWENGGYL DKVEPEIDKH GSMIPKYKIY TPGANERKFN
NYMYMICYGF VEDVERSPES GKRKKIRTIA AYPLGVGKST SHPQDLLEEL CSLKVTVRRT
AGATEKIVFG SSGPLHHLLP WKKILTGGSI FNAVKVCRNV DQIQLENQQS LRIFFLSITK
LNDSGIYMIP RTMLEFRRNN AIAFNLLVYL KIDADLAKAG IQGSFDKDGT KVASFMLHLG
NFVRRAGKYY SVEYCKRKID RMKLQFSLGS IGGLSLHIKI NGVISKRLFA QMGFQKNLCF
SLMDINPWLN RLTWNNSCEI SRVAAVLQPS VPREFMIYDD VFIDNTGKIL KG
