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NSP_SLCV
ID   NSP_SLCV                Reviewed;         256 AA.
AC   P21935;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Nuclear shuttle protein;
DE            Short=NSP;
DE   AltName: Full=Protein BR1;
DE   AltName: Full=Protein BV1;
GN   ORFNames=BR1, BV1;
OS   Squash leaf curl virus (SLCV).
OC   Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC   Geplafuvirales; Geminiviridae; Begomovirus.
OX   NCBI_TaxID=10829;
OH   NCBI_TaxID=3662; Cucurbita moschata (Winter crookneck squash) (Cucurbita pepo var. moschata).
OH   NCBI_TaxID=3663; Cucurbita pepo (Vegetable marrow) (Summer squash).
OH   NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1984668; DOI=10.1016/0042-6822(91)90009-z;
RA   Lazarowitz S.G., Lazdins I.B.;
RT   "Infectivity and complete nucleotide sequence of the cloned genomic
RT   components of a bipartite squash leaf curl geminivirus with a broad host
RT   range phenotype.";
RL   Virology 180:58-69(1991).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12242403; DOI=10.2307/3870094;
RA   Sanderfoot A.A., Lazarowitz S.G.;
RT   "Cooperation in viral movement: the geminivirus BL1 movement protein
RT   interacts with BR1 and redirects it from the nucleus to the eell
RT   periphery.";
RL   Plant Cell 7:1185-1194(1995).
RN   [3]
RP   FUNCTION, NUCLEAR LOCALIZATION SIGNAL, AND MUTAGENESIS OF 25-LYS-ARG-26;
RP   36-ARG--ARG-38; 89-ARG--ARG-91; 97-LYS--ARG-100; 148-PHE-ASP-149;
RP   170-ASP-ARG-171; 201-ASN--ARG-203; ASP-212; 215-ARG-ASP-216; ASN-224 AND
RP   227-LYS-ASN-228.
RX   PubMed=8587985; DOI=10.1104/pp.110.1.23;
RA   Sanderfoot A.A., Ingham D.J., Lazarowitz S.G.;
RT   "A viral movement protein as a nuclear shuttle. The geminivirus BR1
RT   movement protein contains domains essential for interaction with BL1 and
RT   nuclear localization.";
RL   Plant Physiol. 110:23-33(1996).
RN   [4]
RP   NUCLEAR EXPORT SIGNAL, AND MUTAGENESIS OF 189-LEU--LEU-193.
RX   PubMed=10402428; DOI=10.2307/3870748;
RA   Ward B.M., Lazarowitz S.G.;
RT   "Nuclear export in plants. Use of geminivirus movement proteins for a cell-
RT   based export assay.";
RL   Plant Cell 11:1267-1276(1999).
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. {ECO:0000269|PubMed:8587985}.
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:12242403}. Host
CC       cytoplasm {ECO:0000269|PubMed:12242403}. Host cell membrane
CC       {ECO:0000269|PubMed:12242403}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:12242403}; Cytoplasmic side
CC       {ECO:0000269|PubMed:12242403}. Note=Translocated to the plasma membrane
CC       by the movement protein BC1.
CC   -!- SIMILARITY: Belongs to the begomovirus nuclear shuttle protein family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC32408.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; M38182; AAC32408.1; ALT_INIT; Genomic_DNA.
DR   PIR; A36785; QQCVSV.
DR   RefSeq; NP_047247.2; NC_001937.1.
DR   GeneID; 956398; -.
DR   KEGG; vg:956398; -.
DR   Proteomes; UP000009151; 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_0000222267"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          150..187
FT                   /note="Interaction with Arabidopsis thaliana NSI protein"
FT                   /evidence="ECO:0000250"
FT   MOTIF           21..42
FT                   /note="Bipartite nuclear localization signal"
FT   MOTIF           81..96
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000269|PubMed:8587985"
FT   MOTIF           177..198
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        27..43
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         25..26
FT                   /note="KR->AA: Delayed nuclear targeting. No effect on
FT                   infectivity."
FT                   /evidence="ECO:0000269|PubMed:8587985"
FT   MUTAGEN         36..38
FT                   /note="RRR->AAA: No effect on subcellular location."
FT                   /evidence="ECO:0000269|PubMed:8587985"
FT   MUTAGEN         89..91
FT                   /note="RTR->ATA: Mislocalizes to the cytoplasm. Complete
FT                   loss of infectivity."
FT                   /evidence="ECO:0000269|PubMed:8587985"
FT   MUTAGEN         97..100
FT                   /note="KRVR->AAVA: No effect on subcellular location."
FT                   /evidence="ECO:0000269|PubMed:8587985"
FT   MUTAGEN         148..149
FT                   /note="FD->AA: No effect on subcellular location."
FT                   /evidence="ECO:0000269|PubMed:8587985"
FT   MUTAGEN         170..171
FT                   /note="DR->AA: No effect on subcellular location."
FT                   /evidence="ECO:0000269|PubMed:8587985"
FT   MUTAGEN         189..193
FT                   /note="LLIDL->AAIDA: Complete loss of infectivity."
FT                   /evidence="ECO:0000269|PubMed:10402428"
FT   MUTAGEN         201..203
FT                   /note="NKR->AAA: Delayed nuclear targeting. No effect on
FT                   infectivity."
FT                   /evidence="ECO:0000269|PubMed:8587985"
FT   MUTAGEN         212
FT                   /note="D->A: Delayed nuclear targeting."
FT                   /evidence="ECO:0000269|PubMed:8587985"
FT   MUTAGEN         215..216
FT                   /note="RD->AA: Delayed nuclear targeting."
FT                   /evidence="ECO:0000269|PubMed:8587985"
FT   MUTAGEN         224
FT                   /note="N->A: Mislocalizes to the cytoplasm. Complete loss
FT                   of infectivity."
FT                   /evidence="ECO:0000269|PubMed:8587985"
FT   MUTAGEN         227..228
FT                   /note="KN->AA: Mislocalizes to the cytoplasm. Complete loss
FT                   of infectivity."
FT                   /evidence="ECO:0000269|PubMed:8587985"
SQ   SEQUENCE   256 AA;  29228 MW;  0EC879D1983DEFAF CRC64;
     MYSTSNRRGR SQTQRGSHVR RTGVKRSYGA ARGDDRRRPN VVSKTQVEPR MTIQRVQENQ
     FGPEFVLSQN SALSTFVTYP SYVKTVPNRT RTYIKLKRVR FKGTLKIERG QGDTIMDGPS
     SNIEGVFSMV IVVDRKPHVS QSGRLHTFDE LFGARIHCHG NLSVVPALKD RYYIRHVTKR
     VVSLEKDTLL IDLHGTTQLS NKRYNCWASF SDLERDSCNG VYGNITKNAL LVYYCWLSDA
     QSKASTYVSF ELDYLG
 
 
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