NCAP_VSIVA
ID NCAP_VSIVA Reviewed; 422 AA.
AC P03521;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 23-FEB-2022, entry version 111.
DE RecName: Full=Nucleoprotein;
DE Short=NP;
DE AltName: Full=Nucleocapsid protein;
DE Short=Protein N;
GN Name=N;
OS Vesicular stomatitis Indiana virus (strain San Juan) (VSIV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Vesiculovirus.
OX NCBI_TaxID=11285;
OH NCBI_TaxID=7158; Aedes.
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=58271; Culicoides.
OH NCBI_TaxID=9793; Equus asinus (Donkey) (Equus africanus asinus).
OH NCBI_TaxID=9796; Equus caballus (Horse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=252607; Lutzomyia.
OH NCBI_TaxID=7370; Musca domestica (House fly).
OH NCBI_TaxID=7190; Simuliidae (black flies).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6268841; DOI=10.1128/jvi.39.2.529-535.1981;
RA Gallione C.J., Greene J.R., Iverson L.E., Rose J.K.;
RT "Nucleotide sequences of the mRNA's encoding the vesicular stomatitis virus
RT N and NS proteins.";
RL J. Virol. 39:529-535(1981).
RN [2]
RP FUNCTION.
RC STRAIN=Mudd-Summers;
RX PubMed=2986844; DOI=10.1016/0092-8674(85)90079-0;
RA Arnheiter H., Davis N.L., Wertz G., Schubert M., Lazzarini R.A.;
RT "Role of the nucleocapsid protein in regulating vesicular stomatitis virus
RT RNA synthesis.";
RL Cell 41:259-267(1985).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=1850035; DOI=10.1128/jvi.65.5.2622-2628.1991;
RA Rigaut K.D., Birk D.E., Lenard J.;
RT "Intracellular distribution of input vesicular stomatitis virus proteins
RT after uncoating.";
RL J. Virol. 65:2622-2628(1991).
RN [4]
RP INTERACTION WITH PHOSPHOPROTEIN.
RX PubMed=3016338; DOI=10.1128/jvi.59.3.751-754.1986;
RA Davis N.L., Arnheiter H., Wertz G.W.;
RT "Vesicular stomatitis virus N and NS proteins form multiple complexes.";
RL J. Virol. 59:751-754(1986).
RN [5]
RP RNA-BINDING, AND INTERACTION WITH PHOSPHOPROTEIN.
RX PubMed=11000221; DOI=10.1128/jvi.74.20.9515-9524.2000;
RA Green T.J., Macpherson S., Qiu S., Lebowitz J., Wertz G.W., Luo M.;
RT "Study of the assembly of vesicular stomatitis virus N protein: role of the
RT P protein.";
RL J. Virol. 74:9515-9524(2000).
RN [6]
RP INTERACTION WITH PHOSPHOPROTEIN.
RX PubMed=21207454; DOI=10.1002/pro.587;
RA Leyrat C., Jensen M.R., Ribeiro E.A. Jr., Gerard F.C., Ruigrok R.W.,
RA Blackledge M., Jamin M.;
RT "The N(0)-binding region of the vesicular stomatitis virus phosphoprotein
RT is globally disordered but contains transient alpha-helices.";
RL Protein Sci. 20:542-556(2011).
RN [7]
RP FUNCTION.
RX PubMed=22875970; DOI=10.1128/jvi.01238-12;
RA Harouaka D., Wertz G.W.;
RT "Second-site mutations selected in transcriptional regulatory sequences
RT compensate for engineered mutations in the vesicular stomatitis virus
RT nucleocapsid protein.";
RL J. Virol. 86:11266-11275(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS).
RX PubMed=16778022; DOI=10.1126/science.1126953;
RA Green T.J., Zhang X., Wertz G.W., Luo M.;
RT "Structure of the vesicular stomatitis virus nucleoprotein-RNA complex.";
RL Science 313:357-360(2006).
CC -!- FUNCTION: Encapsidates the genome in a ratio of one N per nine
CC ribonucleotides, protecting it from nucleases. The encapsidated genomic
CC RNA is termed the NC and serves as template for transcription and
CC replication. Nucleocapsid assembly is concommitant with replication,
CC therefore viral replication depends on the intracellular concentration
CC of free N, termed N(0). All replicative products are resistant to
CC nucleases. {ECO:0000269|PubMed:22875970, ECO:0000269|PubMed:2986844}.
CC -!- SUBUNIT: Homomultimerizes to form the nucleocapsid. Binds to viral
CC genomic RNA (PubMed:11000221). N in nucleocapsid binds the P protein
CC and thereby positions the polymerase on the template (PubMed:3016338).
CC Interaction of N(0) with the P protein prevents the uncontrolled
CC aggregation of N(0) (PubMed:21207454). {ECO:0000269|PubMed:11000221,
CC ECO:0000269|PubMed:21207454, ECO:0000269|PubMed:3016338}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:1850035}. Host
CC cytoplasm. Note=The nucleocapsid is synthesized in the cytoplasm, and
CC is subsequently transported via microtubules to the cell periphery.
CC -!- SIMILARITY: Belongs to the vesiculovirus nucleocapsid protein family.
CC {ECO:0000305}.
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DR EMBL; J02428; AAA48367.1; -; Genomic_RNA.
DR RefSeq; NP_041712.1; NC_001560.1.
DR PDB; 1FZJ; X-ray; 1.90 A; P=52-59.
DR PDB; 1FZM; X-ray; 1.80 A; P=52-59.
DR PDB; 2GIC; X-ray; 2.92 A; A/B/C/D/E=1-422.
DR PDB; 2QVJ; X-ray; 2.80 A; A/B/C/D/E=2-422.
DR PDB; 2WYY; EM; 10.00 A; A/C/D/F/H/I/J/K/L/M=1-422.
DR PDB; 3PTO; X-ray; 3.01 A; A/B/C/D/E=2-422.
DR PDB; 3PTX; X-ray; 3.00 A; A/B/C/D/E=2-422.
DR PDB; 3PU0; X-ray; 3.09 A; A/B/C/D/E=2-422.
DR PDB; 3PU1; X-ray; 3.14 A; A/B/C/D/E=2-422.
DR PDB; 3PU4; X-ray; 3.00 A; A/B/C/D/E=2-422.
DR PDB; 5UK4; X-ray; 3.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-422.
DR PDB; 6BJY; X-ray; 3.46 A; A/B/C/D/E=2-422.
DR PDB; 6WL2; X-ray; 3.30 A; B/E/H=52-59.
DR PDB; 6WL3; X-ray; 3.45 A; B/E/H=52-59.
DR PDB; 6WL4; X-ray; 3.60 A; B/E/H=52-59.
DR PDBsum; 1FZJ; -.
DR PDBsum; 1FZM; -.
DR PDBsum; 2GIC; -.
DR PDBsum; 2QVJ; -.
DR PDBsum; 2WYY; -.
DR PDBsum; 3PTO; -.
DR PDBsum; 3PTX; -.
DR PDBsum; 3PU0; -.
DR PDBsum; 3PU1; -.
DR PDBsum; 3PU4; -.
DR PDBsum; 5UK4; -.
DR PDBsum; 6BJY; -.
DR PDBsum; 6WL2; -.
DR PDBsum; 6WL3; -.
DR PDBsum; 6WL4; -.
DR SMR; P03521; -.
DR ABCD; P03521; 4 sequenced antibodies.
DR DNASU; 1489831; -.
DR GeneID; 1489831; -.
DR KEGG; vg:1489831; -.
DR EvolutionaryTrace; P03521; -.
DR Proteomes; UP000002327; Genome.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019013; C:viral nucleocapsid; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0039703; P:RNA replication; IDA:UniProtKB.
DR GO; GO:0019083; P:viral transcription; IDA:UniProtKB.
DR Gene3D; 1.10.3570.10; -; 1.
DR Gene3D; 1.10.3610.10; -; 1.
DR InterPro; IPR000448; Rhabdo_ncapsid.
DR InterPro; IPR023331; Rhabdovirus_ncapsid_C.
DR InterPro; IPR023330; Rhabdovirus_ncapsid_N.
DR InterPro; IPR035961; Rhabdovirus_nucleoprotein-like.
DR Pfam; PF00945; Rhabdo_ncap; 1.
DR SUPFAM; SSF140809; SSF140809; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Helical capsid protein; Host cytoplasm;
KW Reference proteome; Ribonucleoprotein; RNA-binding; Viral nucleoprotein;
KW Viral RNA replication; Virion.
FT CHAIN 1..422
FT /note="Nucleoprotein"
FT /id="PRO_0000222823"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:2GIC"
FT TURN 8..11
FT /evidence="ECO:0007829|PDB:2GIC"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:2GIC"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:2GIC"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:2GIC"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:5UK4"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:2GIC"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:2GIC"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:2GIC"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2GIC"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:2GIC"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:5UK4"
FT TURN 130..133
FT /evidence="ECO:0007829|PDB:2GIC"
FT HELIX 134..144
FT /evidence="ECO:0007829|PDB:2GIC"
FT HELIX 151..163
FT /evidence="ECO:0007829|PDB:2GIC"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:2GIC"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:2GIC"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:2GIC"
FT HELIX 189..204
FT /evidence="ECO:0007829|PDB:2GIC"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:3PU0"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:2GIC"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:2GIC"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:2GIC"
FT TURN 221..224
FT /evidence="ECO:0007829|PDB:2GIC"
FT HELIX 226..238
FT /evidence="ECO:0007829|PDB:2GIC"
FT HELIX 242..247
FT /evidence="ECO:0007829|PDB:2GIC"
FT HELIX 252..261
FT /evidence="ECO:0007829|PDB:2GIC"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:2GIC"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:3PU1"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:2GIC"
FT TURN 278..282
FT /evidence="ECO:0007829|PDB:2GIC"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:5UK4"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:3PTX"
FT HELIX 295..307
FT /evidence="ECO:0007829|PDB:2GIC"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:2GIC"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:2GIC"
FT HELIX 324..340
FT /evidence="ECO:0007829|PDB:2GIC"
FT STRAND 348..352
FT /evidence="ECO:0007829|PDB:5UK4"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:3PTX"
FT HELIX 375..383
FT /evidence="ECO:0007829|PDB:2GIC"
FT TURN 384..387
FT /evidence="ECO:0007829|PDB:2GIC"
FT HELIX 391..401
FT /evidence="ECO:0007829|PDB:2GIC"
FT HELIX 412..420
FT /evidence="ECO:0007829|PDB:2GIC"
SQ SEQUENCE 422 AA; 47409 MW; 7345C01BAB3C710E CRC64;
MSVTVKRIID NTVIVPKLPA NEDPVEYPAD YFRKSKEIPL YINTTKSLSD LRGYVYQGLK
SGNVSIIHVN SYLYGALKDI RGKLDKDWSS FGINIGKAGD TIGIFDLVSL KALDGVLPDG
VSDASRTSAD DKWLPLYLLG LYRVGRTQMP EYRKKLMDGL TNQCKMINEQ FEPLVPEGRD
IFDVWGNDSN YTKIVAAVDM FFHMFKKHEC ASFRYGTIVS RFKDCAALAT FGHLCKITGM
STEDVTTWIL NREVADEMVQ MMLPGQEIDK ADSYMPYLID FGLSSKSPYS SVKNPAFHFW
GQLTALLLRS TRARNARQPD DIEYTSLTTA GLLYAYAVGS SADLAQQFCV GDNKYTPDDS
TGGLTTNAPP QGRDVVEWLG WFEDQNRKPT PDMMQYAKRA VMSLQGLREK TIGKYAKSEF
DK
