NCAP_BDV1
ID NCAP_BDV1 Reviewed; 370 AA.
AC P0C796; Q01552;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Nucleoprotein;
DE Short=N protein;
DE AltName: Full=Nucleocapsid protein;
DE AltName: Full=p38;
DE AltName: Full=p40;
GN Name=N;
OS Borna disease virus 1 (BoDV-1).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Bornaviridae; Orthobornavirus.
OX NCBI_TaxID=1714621;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=9352; Bradypodidae (three-fingered sloths).
OH NCBI_TaxID=9925; Capra hircus (Goat).
OH NCBI_TaxID=9850; Cervidae (deer).
OH NCBI_TaxID=109474; Crocidura leucodon (Bicoloured white-toothed shrew) (Celebes shrew).
OH NCBI_TaxID=9788; Equidae (horses).
OH NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
OH NCBI_TaxID=56798; Hexaprotodon liberiensis (Pygmy hippopotamus) (Choeropsis liberiensis).
OH NCBI_TaxID=9844; Lama glama (Llama).
OH NCBI_TaxID=9986; Oryctolagus cuniculus (Rabbit).
OH NCBI_TaxID=9940; Ovis aries (Sheep).
OH NCBI_TaxID=8801; Struthio camelus (Common ostrich).
OH NCBI_TaxID=9455; Varecia variegata (Black-and-white ruffed lemur) (Lemur variegatus).
OH NCBI_TaxID=30538; Vicugna pacos (Alpaca) (Lama pacos).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Clone B8;
RX PubMed=8317098; DOI=10.1006/viro.1993.1364;
RA Pyper J.M., Richt J.A., Brown L., Rott R., Narayan O., Clements J.E.;
RT "Genomic organization of the structural proteins of borna disease virus
RT revealed by a cDNA clone encoding the 38-kDa protein.";
RL Virology 195:229-238(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=7906311; DOI=10.1128/jvi.68.3.1382-1396.1994;
RA Cubitt B., Oldstone C., de la Torre J.C.;
RT "Sequence and genome organization of Borna disease virus.";
RL J. Virol. 68:1382-1396(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Halle B1/91;
RX PubMed=8254777; DOI=10.1128/jvi.68.1.63-68.1994;
RA Schneider P.A., Briese T., Zimmermann W., Ludwig H., Lipkin W.I.;
RT "Sequence conservation in field and experimental isolates of Borna disease
RT virus.";
RL J. Virol. 68:63-68(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=HE/80-1;
RX PubMed=1404604; DOI=10.1128/jvi.66.11.6572-6577.1992;
RA McClure M.A., Thibault K.J., Hatalski C.G., Lipkin W.I.;
RT "Sequence similarity between Borna disease virus p40 and a duplicated
RT domain within the paramyxovirus and rhabdovirus polymerase proteins.";
RL J. Virol. 66:6572-6577(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 10-370.
RC STRAIN=Giessen / HE/80-3;
RA Binz T., Riehle H., Yamasaki J., Richt J.A., Grebenstein O., Rott R.,
RA Niemann H.;
RT "The 39/39k antigen of borna disease virus.";
RL Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP ALTERNATIVE INITIATION.
RX PubMed=9188580; DOI=10.1128/jvi.71.7.5133-5139.1997;
RA Pyper J.M., Gartner A.E.;
RT "Molecular basis for the differential subcellular localization of the
RT 38- and 39-kilodalton structural proteins of Borna disease virus.";
RL J. Virol. 71:5133-5139(1997).
RN [7]
RP INTERACTION WITH P PROTEIN.
RX PubMed=9535888; DOI=10.1074/jbc.273.15.9007;
RA Schwemmle M., Salvatore M., Shi L., Richt J., Lee C.H., Lipkin W.I.;
RT "Interactions of the borna disease virus P, N, and X proteins and their
RT functional implications.";
RL J. Biol. Chem. 273:9007-9012(1998).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=9527928; DOI=10.1006/viro.1998.9049;
RA Kobayashi T., Shoya Y., Koda T., Takashima I., Lai P.K., Ikuta K.,
RA Kakinuma M., Kishi M.;
RT "Nuclear targeting activity associated with the amino terminal region of
RT the Borna disease virus nucleoprotein.";
RL Virology 243:188-197(1998).
RN [9]
RP FUNCTION.
RX PubMed=11238866; DOI=10.1128/jvi.75.7.3404-3412.2001;
RA Kobayashi T., Kamitani W., Zhang G., Watanabe M., Tomonaga K., Ikuta K.;
RT "Borna disease virus nucleoprotein requires both nuclear localization and
RT export activities for viral nucleocytoplasmic shuttling.";
RL J. Virol. 75:3404-3412(2001).
RN [10]
RP REVIEW.
RX PubMed=11932200; DOI=10.1016/s1286-4579(02)01564-2;
RA Tomonaga K., Kobayashi T., Ikuta K.;
RT "Molecular and cellular biology of Borna disease virus infection.";
RL Microbes Infect. 4:491-500(2002).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS).
RX PubMed=14527390; DOI=10.1016/j.str.2003.08.011;
RA Rudolph M.G., Kraus I., Dickmanns A., Eickmann M., Garten W., Ficner R.;
RT "Crystal structure of the borna disease virus nucleoprotein.";
RL Structure 11:1219-1226(2003).
CC -!- FUNCTION: Encapsidates the genome, protecting it from nucleases. The
CC encapsidated genomic RNA is termed the NC and serves as template for
CC transcription and replication. Targets viral NC to the nucleus. Could
CC be involved in the transport of nucleoprotein particles from the
CC nucleus to the cytoplasm. The nuclear export signal is masked by the
CC interaction with the P protein. {ECO:0000269|PubMed:11238866}.
CC -!- SUBUNIT: Homomultimerizes to form the nucleocapsid. Binds to viral
CC genomic RNA (By similarity). Interacts with P protein. {ECO:0000250,
CC ECO:0000269|PubMed:9535888}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host nucleus
CC {ECO:0000269|PubMed:9527928}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=p40;
CC IsoId=P0C796-1; Sequence=Displayed;
CC Name=p38;
CC IsoId=P0C796-2; Sequence=VSP_018913;
CC -!- MISCELLANEOUS: Isoform P38 does not have the nuclear localization
CC signal, nonetheless it is localized in the nucleus.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA73385.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAB27261.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA48458.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; S62821; AAB27261.1; ALT_INIT; Genomic_RNA.
DR EMBL; L27077; AAA20663.1; -; Genomic_RNA.
DR EMBL; S67502; AAB29214.1; -; Genomic_RNA.
DR EMBL; M99375; AAA73385.1; ALT_INIT; mRNA.
DR EMBL; X68392; CAA48458.1; ALT_INIT; mRNA.
DR PIR; A49528; A49528.
DR PDB; 1N93; X-ray; 1.76 A; X=1-370.
DR PDB; 1PP1; X-ray; 1.90 A; X=1-370.
DR PDBsum; 1N93; -.
DR PDBsum; 1PP1; -.
DR SMR; P0C796; -.
DR EvolutionaryTrace; P0C796; -.
DR Proteomes; UP000185272; Genome.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0039592; P:suppression by virus of G2/M transition of host mitotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3040.10; -; 1.
DR Gene3D; 1.10.3050.10; -; 1.
DR InterPro; IPR009441; P40_nucleoprot_BD-vir.
DR InterPro; IPR036260; P40_nucleoprot_sf_BD-vir.
DR InterPro; IPR015969; P40_nucleoprot_sub1_BD-vir.
DR InterPro; IPR015970; P40_nucleoprot_sub2_BD-vir.
DR Pfam; PF06407; BDV_P40; 1.
DR SUPFAM; SSF101399; SSF101399; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Capsid protein;
KW Helical capsid protein; Host G2/M cell cycle arrest by virus; Host nucleus;
KW Host-virus interaction; Modulation of host cell cycle by virus;
KW Viral nucleoprotein; Viral penetration into host nucleus; Virion;
KW Virus entry into host cell.
FT CHAIN 1..370
FT /note="Nucleoprotein"
FT /id="PRO_0000045268"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 3..11
FT /note="Nuclear localization signal"
FT MOTIF 128..141
FT /note="Nuclear export signal"
FT VAR_SEQ 1..13
FT /note="Missing (in isoform p38)"
FT /evidence="ECO:0000305"
FT /id="VSP_018913"
FT VARIANT 47
FT /note="I -> T (in strain: HE/80-1)"
FT VARIANT 56
FT /note="N -> S (in strain: Halle B1/91)"
FT VARIANT 357
FT /note="I -> V (in strain: Halle B1/91)"
FT VARIANT 362
FT /note="R -> K (in strain: Halle B1/91)"
FT CONFLICT 1..2
FT /note="MP -> LK (in Ref. 4; AAA73385)"
FT /evidence="ECO:0000305"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:1N93"
FT HELIX 53..59
FT /evidence="ECO:0007829|PDB:1N93"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:1N93"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:1N93"
FT HELIX 86..92
FT /evidence="ECO:0007829|PDB:1N93"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:1N93"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:1PP1"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:1N93"
FT HELIX 130..149
FT /evidence="ECO:0007829|PDB:1N93"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:1N93"
FT HELIX 160..172
FT /evidence="ECO:0007829|PDB:1N93"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:1N93"
FT TURN 184..187
FT /evidence="ECO:0007829|PDB:1N93"
FT HELIX 191..198
FT /evidence="ECO:0007829|PDB:1N93"
FT HELIX 203..212
FT /evidence="ECO:0007829|PDB:1N93"
FT HELIX 219..230
FT /evidence="ECO:0007829|PDB:1N93"
FT TURN 231..234
FT /evidence="ECO:0007829|PDB:1N93"
FT HELIX 236..247
FT /evidence="ECO:0007829|PDB:1N93"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:1N93"
FT HELIX 256..276
FT /evidence="ECO:0007829|PDB:1N93"
FT HELIX 277..282
FT /evidence="ECO:0007829|PDB:1N93"
FT TURN 283..287
FT /evidence="ECO:0007829|PDB:1N93"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:1N93"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:1N93"
FT HELIX 300..313
FT /evidence="ECO:0007829|PDB:1N93"
FT HELIX 333..340
FT /evidence="ECO:0007829|PDB:1N93"
FT HELIX 355..363
FT /evidence="ECO:0007829|PDB:1N93"
SQ SEQUENCE 370 AA; 40981 MW; C02454BDAB5E4E53 CRC64;
MPPKRRLVDD ADAMEDQDLY EPPASLPKLP GKFLQYTVGG SDPHPGIGHE KDIRQNAVAL
LDQSRRDMFH TVTPSLVFLC LLIPGLHAAF VHGGVPRESY LSTPVTRGEQ TVVKTAKFYG
EKTTQRDLTE LEISSIFSHC CSLLIGVVIG SSSKIKAGAE QIKKRFKTMM AALNRPSHGE
TATLLQMFNP HEAIDWINGQ PWVGSFVLSL LTTDFESPGK EFMDQIKLVA SYAQMTTYTT
IKEYLAECMD ATLTIPVVAY EIRDFLEVSA KLKEEHADLF PFLGAIRHPD AIKLAPRSFP
NLASAAFYWS KKENPTMAGY RASTIQPGAS VKETQLARYR RREISRGEDG AELSGEISAI
MRMIGVTGLN
