NSP_CALCV
ID NSP_CALCV Reviewed; 256 AA.
AC Q96706;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Nuclear shuttle protein;
DE Short=NSP;
DE AltName: Full=Protein BR1;
DE AltName: Full=Protein BV1;
GN ORFNames=BR1, BV1;
OS Cabbage leaf curl virus (isolate Jamaica) (CaLCuV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Begomovirus.
OX NCBI_TaxID=345184;
OH NCBI_TaxID=3712; Brassica oleracea (Wild cabbage).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Abouzid A.M., Hiebert E., Strandberg J.O.;
RT "Cloning, identification and partial sequencing of a new geminivirus
RT infecting Brassicaceae.";
RL Phytopathology 82:1070-1070(1992).
RN [2]
RP INTERACTION WITH ARABIDOPSIS THALIANA NSI.
RX PubMed=12837950; DOI=10.1105/tpc.012120;
RA McGarry R.C., Barron Y.D., Carvalho M.F., Hill J.E., Gold D., Cheung E.,
RA Kraus W.L., Lazarowitz S.G.;
RT "A novel Arabidopsis acetyltransferase interacts with the geminivirus
RT movement protein NSP.";
RL Plant Cell 15:1605-1618(2003).
RN [3]
RP INTERACTION WITH ARABIDOPSIS THALIANA NSI, AND MUTAGENESIS OF GLU-150;
RP ILE-164 AND ASP-187.
RX PubMed=15452236; DOI=10.1128/jvi.78.20.11161-11171.2004;
RA Carvalho M.F., Lazarowitz S.G.;
RT "Interaction of the movement protein NSP and the Arabidopsis
RT acetyltransferase AtNSI is necessary for Cabbage leaf curl geminivirus
RT infection and pathogenicity.";
RL J. Virol. 78:11161-11171(2004).
RN [4]
RP INTERACTION WITH ARABIDOPSIS THALIANA NSI.
RX PubMed=16461385; DOI=10.1104/pp.105.075556;
RA Carvalho M.F., Turgeon R., Lazarowitz S.G.;
RT "The geminivirus nuclear shuttle protein NSP inhibits the activity of
RT AtNSI, a vascular-expressed Arabidopsis acetyltransferase regulated with
RT the sink-to-source transition.";
RL Plant Physiol. 140:1317-1330(2006).
CC -!- FUNCTION: Binds to the genomic viral ssDNA, shuttles it into and out of
CC the cell nucleus. Begomoviruses use 2 proteins to transport their DNA
CC from cell to cell. The nuclear shuttle protein (NSP) shuttles it
CC between nucleus and cytoplasm and the movement protein (MP) probably
CC transports the DNA-NSP complex to the cell periphery and facilitates
CC movement across the cell wall (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds to single-stranded and double-stranded viral DNA.
CC Interacts with the host nuclear shuttle interacting (NSI) protein. This
CC interaction may allow NSP to recruit NSI monomers to the viral genome
CC and thus regulate nuclear export of viral genome by NSP.
CC {ECO:0000269|PubMed:12837950, ECO:0000269|PubMed:15452236,
CC ECO:0000269|PubMed:16461385}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250}. Host cytoplasm
CC {ECO:0000250}. Host cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC Note=Translocated to the plasma membrane by the movement protein BC1.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the begomovirus nuclear shuttle protein family.
CC {ECO:0000305}.
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DR EMBL; U65530; AAB17965.1; -; Genomic_DNA.
DR Proteomes; UP000007622; 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:0019028; C:viral capsid; IEA:InterPro.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0051027; P:DNA transport; IEA:InterPro.
DR GO; GO:0046740; P:transport of virus in host, cell to cell; IEA:UniProtKB-KW.
DR InterPro; IPR001530; Gemini_BR1.
DR InterPro; IPR000263; GV_A/BR1_coat.
DR Pfam; PF00844; Gemini_coat; 1.
DR PRINTS; PR00223; GEMCOATARBR1.
DR PRINTS; PR00225; GEMCOATBR1.
PE 1: Evidence at protein level;
KW DNA-binding; Host cell membrane; Host cytoplasm; Host membrane;
KW Host nucleus; Host-virus interaction; Membrane; Reference proteome;
KW Transport; Viral movement protein.
FT CHAIN 1..256
FT /note="Nuclear shuttle protein"
FT /id="PRO_0000323698"
FT REGION 18..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..187
FT /note="Interaction with Arabidopsis thaliana NSI protein"
FT MOTIF 21..42
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 81..96
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 27..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 150
FT /note="E->G: Complete loss of interaction with Arabidopsis
FT thaliana NSI protein. Reduced level of infectivity."
FT /evidence="ECO:0000269|PubMed:15452236"
FT MUTAGEN 164
FT /note="I->T: Complete loss of interaction with Arabidopsis
FT thaliana NSI protein. Reduced level of infectivity."
FT /evidence="ECO:0000269|PubMed:15452236"
FT MUTAGEN 187
FT /note="D->G: Complete loss of interaction with Arabidopsis
FT thaliana NSI protein. Reduced level of infectivity."
FT /evidence="ECO:0000269|PubMed:15452236"
SQ SEQUENCE 256 AA; 29278 MW; 0C2E8E0DB4D2B748 CRC64;
MYPTKFRRGV SYSQRRFVSR NQSSKRGTFV RRTDGKRRKG PSSKAHDEPK MKLQRIHENQ
YGPEFVMTHN SALSTFINFP VLGKIEPNRS RSYIKLNRLS FKGTVKIERV HADVNMDGVI
SKIEGVFSLV IVVDRKPHLS STGGLHTFDE IFGARIHSHG NLAITPGLKD RYYVLHVLKR
VLSVEKDTLM VDLEGSTTIS NRRYNCWASF NDLEHDLCNG VYANISKNAI LVYYCWMSDA
MSKASTFVSY DLDYLG
