NCAP_SENDF
ID NCAP_SENDF Reviewed; 524 AA.
AC Q07097;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 75.
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 Fushimi) (SeV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Respirovirus.
OX NCBI_TaxID=11195;
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].
RX PubMed=1850185; DOI=10.1007/bf00571728;
RA Neubert W.J., Eckerskorn C., Homann H.E.;
RT "Sendai virus NP gene codes for a 524 amino acid NP protein.";
RL Virus Genes 5:25-32(1991).
RN [2]
RP HOMOMULTIMERIZATION, AND MUTAGENESIS OF TYR-260; 299-LEU-ILE-300; ILE-313
RP AND PHE-324.
RX PubMed=9126246; DOI=10.1006/viro.1996.8429;
RA Myers T.M., Pieters A., Moyer S.A.;
RT "A highly conserved region of the Sendai virus nucleocapsid protein
RT contributes to the NP-NP binding domain.";
RL Virology 229:322-335(1997).
RN [3]
RP MUTAGENESIS OF GLU-107; 108-LYS-ASP-109; 111-LYS-ARG-112; 114-LYS--ASP-116;
RP 121-LYS--ASP-124 AND 126-GLU--ARG-129.
RX PubMed=8995608; DOI=10.1128/jvi.71.2.918-924.1997;
RA Myers T.M., Moyer S.A.;
RT "An amino-terminal domain of the Sendai virus nucleocapsid protein is
RT required for template function in viral RNA synthesis.";
RL J. Virol. 71:918-924(1997).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF PHE-362; 364-LEU-GLY-365; 370-LYS-ASP-371 AND
RP 373-GLU--LYS-375.
RX PubMed=10374955; DOI=10.1099/0022-1317-80-6-1383;
RA Myers T.M., Smallwood S., Moyer S.A.;
RT "Identification of nucleocapsid protein residues required for Sendai virus
RT nucleocapsid formation and genome replication.";
RL J. Gen. Virol. 80:1383-1391(1999).
RN [5]
RP INTERACTION WITH P PROTEIN, AND MUTAGENESIS OF 435-ASP--ARG-439;
RP 444-GLU--ARG-448; 458-PHE--LEU-461; 465-GLU-ARG-466; 468-GLU--GLU-470;
RP 473-ASP--ASP-475; 478-ASP--ARG-482 AND 489-GLU--ARG-491.
RX PubMed=15246262; DOI=10.1016/j.virol.2004.05.012;
RA Cevik B., Kaesberg J., Smallwood S., Feller J.A., Moyer S.A.;
RT "Mapping the phosphoprotein binding site on Sendai virus NP protein
RT assembled into nucleocapsids.";
RL Virology 325:216-224(2004).
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.
CC {ECO:0000269|PubMed:10374955}.
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.
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; X17218; CAA35092.1; -; Genomic_RNA.
DR PIR; S72316; S72316.
DR BMRB; Q07097; -.
DR SMR; Q07097; -.
DR Proteomes; UP000006825; 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 GO; GO:0039697; P:negative stranded viral RNA transcription; IDA:UniProtKB.
DR InterPro; IPR002021; Paramyx_ncap.
DR Pfam; PF00973; Paramyxo_ncap; 1.
PE 1: Evidence at protein level;
KW Capsid protein; Helical capsid protein; Host cytoplasm; Ribonucleoprotein;
KW RNA-binding; Viral nucleoprotein; Virion.
FT CHAIN 1..524
FT /note="Nucleoprotein"
FT /id="PRO_0000142681"
FT REGION 462..471
FT /note="Binding of N in nucleoprotein to P protein"
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 MUTAGEN 107
FT /note="E->A: 29% loss of in vitro replication."
FT /evidence="ECO:0000269|PubMed:8995608"
FT MUTAGEN 108..109
FT /note="KD->AA: 32% loss of in vitro replication."
FT /evidence="ECO:0000269|PubMed:8995608"
FT MUTAGEN 111..112
FT /note="KR->AA: 31% loss of in vitro replication."
FT /evidence="ECO:0000269|PubMed:8995608"
FT MUTAGEN 114..116
FT /note="KTD->ATA: 72% loss of in vitro replication."
FT /evidence="ECO:0000269|PubMed:8995608"
FT MUTAGEN 121..124
FT /note="KTRD->ATAA: Complete loss of in vitro replication."
FT /evidence="ECO:0000269|PubMed:8995608"
FT MUTAGEN 126..129
FT /note="EYER->AYAA: 82% loss of in vitro replication."
FT /evidence="ECO:0000269|PubMed:8995608"
FT MUTAGEN 260
FT /note="Y->D: Alters homomultimerization. Complete loss of
FT in vitro replication."
FT /evidence="ECO:0000269|PubMed:9126246"
FT MUTAGEN 299..300
FT /note="LI->IV: Complete loss of in vitro replication. No
FT effect on homomultimerization."
FT /evidence="ECO:0000269|PubMed:9126246"
FT MUTAGEN 313
FT /note="I->F: Complete loss of in vitro replication. No
FT effect on homomultimerization."
FT /evidence="ECO:0000269|PubMed:9126246"
FT MUTAGEN 324
FT /note="F->I: Unstable form with complete loss of
FT homomultimerization and replication."
FT /evidence="ECO:0000269|PubMed:9126246"
FT MUTAGEN 324
FT /note="F->V: Unstable form with complete loss of
FT homomultimerization and replication."
FT /evidence="ECO:0000269|PubMed:9126246"
FT MUTAGEN 362
FT /note="F->A: 95% loss of in vitro replication."
FT /evidence="ECO:0000269|PubMed:10374955"
FT MUTAGEN 364..365
FT /note="LG->AA: Unstable form with almost complete loss of
FT homomultimerization."
FT /evidence="ECO:0000269|PubMed:10374955"
FT MUTAGEN 370..371
FT /note="KD->AA: 92% loss of in vitro replication. No effect
FT on homomultimerization."
FT /evidence="ECO:0000269|PubMed:10374955"
FT MUTAGEN 373..375
FT /note="ESK->ASA: 140% increase of in vitro replication."
FT /evidence="ECO:0000269|PubMed:10374955"
FT MUTAGEN 435..439
FT /note="DQDAR->AQAAA: 33% loss of replication."
FT /evidence="ECO:0000269|PubMed:15246262"
FT MUTAGEN 444..448
FT /note="ESGER->ASGAA: 44% loss of replication."
FT /evidence="ECO:0000269|PubMed:15246262"
FT MUTAGEN 458..461
FT /note="FVTL->AATA: 44% loss of replication."
FT /evidence="ECO:0000269|PubMed:15246262"
FT MUTAGEN 465..466
FT /note="ER->AA: 34% loss of replication."
FT /evidence="ECO:0000269|PubMed:15246262"
FT MUTAGEN 468..470
FT /note="EEE->AAA: 42% loss of replication."
FT /evidence="ECO:0000269|PubMed:15246262"
FT MUTAGEN 473..475
FT /note="DED->AAA: 32% loss of replication."
FT /evidence="ECO:0000269|PubMed:15246262"
FT MUTAGEN 478..482
FT /note="DIERR->AAAAA: 29% loss of replication."
FT /evidence="ECO:0000269|PubMed:15246262"
FT MUTAGEN 489..491
FT /note="ERR->AAA: No effect on replication."
FT /evidence="ECO:0000269|PubMed:15246262"
SQ SEQUENCE 524 AA; 56951 MW; 9A6F758505603C35 CRC64;
MAGLLSTFDT FSSRRSESIN KSGGGAVIPG QRSTVSVFVL GPSVTDDADK LFIATTFLAH
SLDTDKQHSQ RGGFLVSLLA MAYSSPELYL TTNGVNADVK YVIYNIEKDP KRTKTDGFIV
KTRDMEYERT TEWLFGPMVN KSPLFQGQRV AADPDTLLQT YGYPACLGAI IVQVWIVLVK
AITSSAGLRK GFFNRLEAFR QDGTVKGALV FTGETVEGIG SVMRSQQSLV SLMVETLVTM
NTARSDLTTL EKNIQIVGNY IRDAGLASFM NTIKYGVETK MAALTLSNLR PDINKLRSLI
DTYLSKGPRA PFICILKDPV HGEFAPGNYP ALWSYAMGVA VVQNKAMQQY VTGGTYLDME
MFLLGQAVAK DAESKISSAL EDELGVTDTA KERLRHHLAN LSGGDGAYHE PTGGGAIEVA
LDNADIDLET EAHADQDARG WGGESGERWA RQVSGGHFVT LHGAERLEEE TNDEDVSDIE
RRIAMRLAER RQEDSATHGD EGRNNGVDHD EDDDAAAVAG IGGI
