MVP_ABMVW
ID MVP_ABMVW Reviewed; 293 AA.
AC P21946;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 23-FEB-2022, entry version 88.
DE RecName: Full=Movement protein BC1;
DE AltName: Full=Movement protein BL1;
GN ORFNames=BC1, BL1;
OS Abutilon mosaic virus (isolate West India) (AbMV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Begomovirus.
OX NCBI_TaxID=10816;
OH NCBI_TaxID=3630; Abutilon.
OH NCBI_TaxID=3635; Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OH NCBI_TaxID=47605; Hibiscus.
OH NCBI_TaxID=96479; Malva.
OH NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
OH NCBI_TaxID=108335; Sida.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2219703; DOI=10.1016/0042-6822(90)90343-p;
RA Frischmuth T., Zimmat G., Jeske H.;
RT "The nucleotide sequence of abutilon mosaic virus reveals prokaryotic as
RT well as eukaryotic features.";
RL Virology 178:461-468(1990).
RN [2]
RP SEQUENCE REVISION.
RA Jeske H.;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=11883189; DOI=10.1006/viro.2001.1185;
RA Zhang S.C., Wege C., Jeske H.;
RT "Movement proteins (BC1 and BV1) of Abutilon mosaic geminivirus are
RT cotransported in and between cells of sink but not of source leaves as
RT detected by green fluorescent protein tagging.";
RL Virology 290:249-260(2001).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=12491102; DOI=10.1007/s00705-002-0880-9;
RA Zhang S.C., Ghosh R., Jeske H.;
RT "Subcellular targeting domains of Abutilon mosaic geminivirus movement
RT protein BC1.";
RL Arch. Virol. 147:2349-2363(2002).
RN [5]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=15220444; DOI=10.1128/jvi.78.14.7698-7706.2004;
RA Hehnle S., Wege C., Jeske H.;
RT "Interaction of DNA with the movement proteins of geminiviruses
RT revisited.";
RL J. Virol. 78:7698-7706(2004).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17351736; DOI=10.1007/s00709-006-0223-x;
RA Frischmuth S., Wege C., Huelsefr D., Jeske H.;
RT "The movement protein BC1 promotes redirection of the nuclear shuttle
RT protein BV1 of Abutilon mosaic geminivirus to the plasma membrane in
RT fission yeast.";
RL Protoplasma 230:117-123(2007).
RN [7]
RP PHOSPHORYLATION.
RX PubMed=17919761; DOI=10.1016/j.virusres.2007.08.011;
RA Kleinow T., Holeiter G., Nischang M., Stein M., Karayavuz M., Wege C.,
RA Jeske H.;
RT "Post-translational modifications of Abutilon mosaic virus movement protein
RT (BC1) in fission yeast.";
RL Virus Res. 131:86-94(2008).
RN [8]
RP PHOSPHORYLATION AT THR-221; SER-223 AND SER-250, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19464722; DOI=10.1016/j.virol.2009.04.018;
RA Kleinow T., Nischang M., Beck A., Kratzer U., Tanwir F., Preiss W.,
RA Kepp G., Jeske H.;
RT "Three C-terminal phosphorylation sites in the Abutilon mosaic virus
RT movement protein affect symptom development and viral DNA accumulation.";
RL Virology 390:89-101(2009).
CC -!- FUNCTION: Transports viral genome to neighboring plant cells directly
CC through plasmosdesmata, without any budding. The movement protein
CC allows efficient cell to cell propagation, by bypassing the host cell
CC wall barrier. Begomovirus genome is shuttled out of nucleus by Nuclear
CC shuttle protein (NSP) and the movement protein transports the DNA-NSP
CC complex to cell plasmodesmata and facilitates further movement across
CC the cell wall. {ECO:0000269|PubMed:15220444,
CC ECO:0000269|PubMed:17351736}.
CC -!- SUBUNIT: Binds to dimeric supercoiled plasmid DNA.
CC -!- SUBCELLULAR LOCATION: Host cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Host microsome membrane; Peripheral membrane protein;
CC Cytoplasmic side. Host endoplasmic reticulum membrane; Peripheral
CC membrane protein; Cytoplasmic side. Note=Found on ER-derived vesicles.
CC -!- PTM: Phosphorylated in yeast. {ECO:0000269|PubMed:17919761,
CC ECO:0000269|PubMed:19464722}.
CC -!- SIMILARITY: Belongs to the begomovirus movement protein BC1 family.
CC {ECO:0000305}.
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DR EMBL; X15984; CAA34115.2; -; Genomic_DNA.
DR PIR; F36214; QQCVW6.
DR RefSeq; NP_047220.2; NC_001929.2.
DR iPTMnet; P21946; -.
DR GeneID; 956375; -.
DR KEGG; vg:956375; -.
DR Proteomes; UP000006885; Genome.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; 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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046740; P:transport of virus in host, cell to cell; IEA:UniProtKB-KW.
DR InterPro; IPR000211; Gemini_BL.
DR Pfam; PF00845; Gemini_BL1; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Host cell membrane; Host endoplasmic reticulum; Host membrane;
KW Host microsome; Membrane; Phosphoprotein; Transport;
KW Viral movement protein.
FT CHAIN 1..293
FT /note="Movement protein BC1"
FT /id="PRO_0000222251"
FT MOD_RES 221
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000305|PubMed:19464722"
FT MOD_RES 223
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000305|PubMed:19464722"
FT MOD_RES 250
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000305|PubMed:19464722"
SQ SEQUENCE 293 AA; 33342 MW; 780275D489258045 CRC64;
MDSQLVNPPN AFNYIESHRD EYQLSHDLTE IILQFPSTAA QLTARLSRSC MKIDHCVIEY
RQQVPINATG SVIVEIHDKR MTDNESLQAS WTFPIRCNID LHYFSASFFS LKDPIPWKLY
YKVCDTNVHQ RTHFAKFKGK LKLSTAKHSV DIPFRAPTVR ILSKQFSEKD VDFSHVDYGK
WERKPIRCAS MSRIGLRGPI EIRPGESWAS RSTIGTAQPD TDSEMENELH PYRHLNRLGT
SLLDPGESAS IVGDQRAEPN ITMSMGQLNE LVRTAVQECV NSNCQASQAK SLK
