ID   NCAP_PI1HC              Reviewed;         524 AA.
AC   P24304;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   23-FEB-2022, entry version 68.
DE   RecName: Full=Nucleoprotein;
DE   AltName: Full=Nucleocapsid protein;
DE            Short=NP;
DE            Short=Protein N;
GN   Name=N; Synonyms=NP;
OS   Human parainfluenza 1 virus (strain C39) (HPIV-1).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Respirovirus.
OX   NCBI_TaxID=11210;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1847263; DOI=10.1016/0042-6822(91)90514-c;
RA   Matsuoka Y., Ray R.;
RT   "Sequence analysis and expression of the human parainfluenza type 1 virus
RT   nucleoprotein gene.";
RL   Virology 181:403-407(1991).
CC   -!- FUNCTION: Encapsidates the genome in a ratio of 1 N per 6
CC       ribonucleotides, protecting it from nucleases. The nucleocapsid (NC)
CC       has a helical structure. The encapsidated genomic RNA is termed the NC
CC       and serves as template for transcription and replication. During
CC       replication, encapsidation by N is coupled to RNA synthesis and all
CC       replicative products are resistant to nucleases (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homomultimerizes to form the nucleocapsid. Binds to viral
CC       genomic RNA. In nucleocapsid, binds the P protein and thereby positions
CC       the polymerase on the template.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm.
CC   -!- DOMAIN: Ncore is globular and carries regions required for N self-
CC       assembly and RNA-binding. Ntail is an intrinsically disordered
CC       monomeric domain (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the paramyxoviruses nucleocapsid family.
CC       {ECO:0000305}.
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DR   EMBL; M62850; AAA46828.1; -; mRNA.
DR   SMR; P24304; -.
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   2: Evidence at transcript 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_0000142672"
FT   REGION          1..400
FT                   /note="Ncore"
FT                   /evidence="ECO:0000250"
FT   REGION          401..524
FT                   /note="Ntail"
FT                   /evidence="ECO:0000250"
FT   REGION          490..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   524 AA;  57551 MW;  7C4B734BD226590A CRC64;
     MAGLLSTFDT FSSRRSESIN KSGGGAIIPG QRSTVSVFIL GPSVTDDADK LLIATTFLAH
     SLDTDKQHSQ RGGFLVSLLA MAYSSPELYL TTNGVNADVK YVIYNIERDP KRTKTDGFIV
     KTRDMEYERT TEWLFGPMIN KNPLFQGQRE NADLEALLQT YGYPACLGAI IVQVWIVLVK
     AITSSSGLRK GFFNRLEAFR QDGTVKSALV FTGDTVEGIG AVMRSQQSLV SLMVETLVTM
     NTSRSDLTTL EKNIQIVGNY IRESGLASFM NTIKYGVETK MAALTLSNLR PDINKLRSLV
     DIYLSKGARA PFTCILRDPV HGEFAPGNYP ALWSYAMGVA VVQNKAMQQY VTGRTYLDME
     MFLLGQAVAK DADSKISSAL EEELGVTDTA KERLRHHLTN LSGGDGAYHK PTGGGAIEVA
     IDHTDITFGA EDTADRDNKN WTNNSNERWM NHSINNHTIT ISGAEELEEE TNDEDITDIE
     NKIARRLADR KQRLSQANNR QDASSDADHE NDDDATAAAG IGGI