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MATRX_TIBVC
ID   MATRX_TIBVC             Reviewed;         253 AA.
AC   D8V072;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   29-SEP-2021, entry version 28.
DE   RecName: Full=Matrix protein;
GN   Name=M;
OS   Tibrogargan virus (strain CS132) (TIBV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Tibrovirus.
OX   NCBI_TaxID=1559361;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
OH   NCBI_TaxID=469753; Culicoides brevitarsis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=CS132;
RX   PubMed=21593274; DOI=10.1099/vir.0.026120-0;
RA   Gubala A., Davis S., Weir R., Melville L., Cowled C., Boyle D.;
RT   "Tibrogargan and Coastal Plains rhabdoviruses: genomic characterization,
RT   evolution of novel genes and seroprevalence in Australian livestock.";
RL   J. Gen. Virol. 92:2160-2170(2011).
CC   -!- FUNCTION: Plays a major role in assembly and budding of virion, by
CC       recruiting cellular partners of the ESCRT complexes that play a key
CC       role in releasing the budding particle from the host membrane.
CC       Condensates the ribonucleocapsid core during virus assembly.
CC       {ECO:0000250|UniProtKB:P03519}.
CC   -!- SUBUNIT: Homomultimer. Interacts with viral nucleocapsid. Interacts
CC       with host TSG101. {ECO:0000250|UniProtKB:P03519}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250|UniProtKB:P03519};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host
CC       endomembrane system {ECO:0000250|UniProtKB:P03519}; Peripheral membrane
CC       protein {ECO:0000250|UniProtKB:P03519}. Host nucleus membrane
CC       {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P03519}.
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 a PTAP/PSAP motif, which
CC       interacts with the UEV domain of TSG101.
CC       {ECO:0000250|UniProtKB:P03519}.
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DR   EMBL; GQ294472; ADG86349.1; -; Viral_cRNA.
DR   RefSeq; YP_007641370.1; NC_020804.1.
DR   GeneID; 14857900; -.
DR   KEGG; vg:14857900; -.
DR   Proteomes; UP000029770; Genome.
DR   GO; GO:0044200; C:host cell nuclear 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: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   InterPro; IPR009397; Vesiculo_matrix.
DR   Pfam; PF06326; Vesiculo_matrix; 1.
PE   3: Inferred from homology;
KW   Host membrane; Host nucleus; Host-virus interaction; Membrane;
KW   Reference proteome; Viral budding;
KW   Viral budding via the host ESCRT complexes; Viral matrix protein;
KW   Viral release from host cell; Virion.
FT   CHAIN           1..253
FT                   /note="Matrix protein"
FT                   /id="PRO_0000432063"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           55..58
FT                   /note="PTAP/PSAP motif"
FT   COMPBIAS        8..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   253 AA;  28910 MW;  E892F74C511E15F1 CRC64;
     MLSRIKQGIK TKRSSSSSSS RSKTGDEDSS LMLRWVYDND PPLKQTDTFQ YLMAPTAPTD
     KASSSYIATT YKVDCKVEII SRASIRNFDE LINIASCLID SYDGQLLIKP WIITVYLTII
     THLVKEPDTH GVRSSVNRYH NGFNEILTLY INKNFAPENK KYSFKKNLST THKGNQCNII
     ISIDLLPTDR KGKSIKDVYE VKMPDNREIP NFQQMLKPYN LKVKEKNGKY LISHKMSSSD
     DSIDVSDSDE NEF
 
 
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