NCAP_SENDO
ID NCAP_SENDO Reviewed; 524 AA.
AC O57286;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Nucleoprotein;
DE AltName: Full=Nucleocapsid protein;
DE Short=NP;
DE Short=Protein N;
GN Name=N; Synonyms=NP;
OS Sendai virus (strain Ohita) (SeV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Respirovirus.
OX NCBI_TaxID=302272;
OH NCBI_TaxID=10144; Cavia cutleri (Guinea pig).
OH NCBI_TaxID=36483; Cricetidae sp. (Hamster).
OH NCBI_TaxID=10090; Mus musculus (Mouse).
OH NCBI_TaxID=10116; Rattus norvegicus (Rat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate MVC11;
RX PubMed=9400971; DOI=10.1099/0022-1317-78-12-3207;
RA Itoh M., Isegawa Y., Hotta H., Homma M.;
RT "Isolation of an avirulent mutant of Sendai virus with two amino acid
RT mutations from a highly virulent field strain through adaptation to LLC-MK2
RT cells.";
RL J. Gen. Virol. 78:3207-3215(1997).
CC -!- FUNCTION: Encapsidates the genome in a ratio of one N per six
CC ribonucleotides, protecting it from nucleases. The nucleocapsid (NC)
CC has a helical structure with 13.07 N per turn. The encapsidated genomic
CC RNA is termed the NC and serves as template for transcription and
CC replication. Replication is dependent on intracellular concentration of
CC newly synthesized N, termed N(0), which corresponds to the protein not
CC associated with RNA. In contrast, when associated with RNA, it is
CC termed N. During replication, encapsidation by N(0) is coupled to RNA
CC synthesis and all replicative products are resistant to nucleases (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homomultimerizes to form the nucleocapsid. Binds to viral
CC genomic RNA. N in nucleocapsid binds the P protein and thereby
CC positions the polymerase on the template. Interaction of N(0) with the
CC P protein prevents the uncontrolled aggregation of N(0) (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm.
CC -!- DOMAIN: There are two distinct binding regions to the P protein, one
CC used by N(0) and the other by N in nucleocapsid. {ECO:0000250}.
CC -!- MISCELLANEOUS: Most abundant protein in the virion. There are 2564
CC molecules per encapsidated genome (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the paramyxoviruses nucleocapsid family.
CC {ECO:0000305}.
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DR EMBL; AB005795; BAA24384.1; -; Genomic_RNA.
DR EMBL; AB005796; BAA24393.1; -; Genomic_RNA.
DR RefSeq; NP_056871.1; NC_001552.1.
DR PDB; 4PG9; X-ray; 2.40 A; C=324-332.
DR PDB; 4PGB; X-ray; 2.80 A; C/F=324-332.
DR PDB; 4PGC; X-ray; 2.30 A; C/F=324-332.
DR PDB; 4PGD; X-ray; 2.70 A; C=324-331.
DR PDB; 4PGE; X-ray; 2.00 A; C=324-333.
DR PDB; 6GB5; X-ray; 2.30 A; E/F=324-330.
DR PDB; 6GB7; X-ray; 2.15 A; I/J/K/L=324-330.
DR PDB; 6M7D; EM; 2.90 A; A=1-524.
DR PDBsum; 4PG9; -.
DR PDBsum; 4PGB; -.
DR PDBsum; 4PGC; -.
DR PDBsum; 4PGD; -.
DR PDBsum; 4PGE; -.
DR PDBsum; 6GB5; -.
DR PDBsum; 6GB7; -.
DR PDBsum; 6M7D; -.
DR SMR; O57286; -.
DR GeneID; 1489779; -.
DR KEGG; vg:1489779; -.
DR Proteomes; UP000006563; Genome.
DR Proteomes; UP000007311; 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; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR InterPro; IPR002021; Paramyx_ncap.
DR Pfam; PF00973; Paramyxo_ncap; 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 Virion.
FT CHAIN 1..524
FT /note="Nucleoprotein"
FT /id="PRO_0000142683"
FT REGION 462..471
FT /note="Binding of N in nucleoprotein to P protein"
FT /evidence="ECO:0000250"
FT REGION 487..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:6M7D"
FT HELIX 11..19
FT /evidence="ECO:0007829|PDB:6M7D"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:6M7D"
FT HELIX 47..62
FT /evidence="ECO:0007829|PDB:6M7D"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:6M7D"
FT HELIX 68..80
FT /evidence="ECO:0007829|PDB:6M7D"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:6M7D"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:6M7D"
FT STRAND 97..108
FT /evidence="ECO:0007829|PDB:6M7D"
FT TURN 114..117
FT /evidence="ECO:0007829|PDB:6M7D"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:6M7D"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:6M7D"
FT HELIX 129..135
FT /evidence="ECO:0007829|PDB:6M7D"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:6M7D"
FT HELIX 163..181
FT /evidence="ECO:0007829|PDB:6M7D"
FT HELIX 188..202
FT /evidence="ECO:0007829|PDB:6M7D"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:6M7D"
FT HELIX 213..225
FT /evidence="ECO:0007829|PDB:6M7D"
FT HELIX 227..239
FT /evidence="ECO:0007829|PDB:6M7D"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:6M7D"
FT HELIX 249..261
FT /evidence="ECO:0007829|PDB:6M7D"
FT TURN 262..265
FT /evidence="ECO:0007829|PDB:6M7D"
FT HELIX 267..276
FT /evidence="ECO:0007829|PDB:6M7D"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:6M7D"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:6M7D"
FT HELIX 290..305
FT /evidence="ECO:0007829|PDB:6M7D"
FT HELIX 307..312
FT /evidence="ECO:0007829|PDB:6M7D"
FT TURN 313..317
FT /evidence="ECO:0007829|PDB:6M7D"
FT HELIX 319..324
FT /evidence="ECO:0007829|PDB:6M7D"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:6M7D"
FT HELIX 330..343
FT /evidence="ECO:0007829|PDB:6M7D"
FT HELIX 346..349
FT /evidence="ECO:0007829|PDB:6M7D"
FT HELIX 359..370
FT /evidence="ECO:0007829|PDB:6M7D"
FT TURN 372..375
FT /evidence="ECO:0007829|PDB:6M7D"
FT HELIX 381..384
FT /evidence="ECO:0007829|PDB:6M7D"
FT HELIX 388..401
FT /evidence="ECO:0007829|PDB:6M7D"
SQ SEQUENCE 524 AA; 57135 MW; 04FC3559338502D6 CRC64;
MAGLLSTFDT FSSRRSESIN KSGGGAVIPG QRSTVSVFVL GPSVTDDADK LSIATTFLAH
SLDTDKQHSQ RGGFLVSLLA MAYSSPELYL TTNGVNADVK YVIYNIEKDP KRTKTDGFIV
KTRDMEYERT TEWLFGPMVN KSPLFQGQRD AADPDTLLQI YGYPACLGAI IVQVWIVLVK
AITSSAGLRK GFFNRLEAFR QDGTVKGALV FTGETVEGIG SVMRSQQSLV SLMVETLVTM
NTARSDLTTL EKNIQIVGNY IRDAGLASFM NTIKYGVETK MAALTLSNLR PDINKLRSLI
DTYLSKGPRA PFICILKDPV HGEFAPGNYP ALWSYAMGVA VVQNKAMQQY VTGRTYLDME
MFLLGQAVAK DAESKISSAL EDELGVTDTA KERLRHHLAN LSGGDGAYHK PTGGGAIEVA
LDNADIDLEP EAHTDQDARG WGGDSGDRWA RSMGSGHFIT LHGAERLEEE TNDEDVSDIE
RRIARRLAER RQEDATTHED EGRNNGVDHD EEDDAAAAAG MGGI
