ID   NCAP_PI4HB              Reviewed;         551 AA.
AC   P17241;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   02-JUN-2021, entry version 72.
DE   RecName: Full=Nucleoprotein;
DE   AltName: Full=Nucleocapsid protein;
DE            Short=NP;
DE            Short=Protein N;
GN   Name=N; Synonyms=NP;
OS   Human parainfluenza 4b virus (strain 68-333) (HPIV-4b).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC   Orthorubulavirus; Human orthorubulavirus 4.
OX   NCBI_TaxID=11227;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2152988; DOI=10.1016/0042-6822(90)90047-u;
RA   Kondo K., Bando H., Kawano M., Tsurudome M., Komada H., Nishio M., Ito Y.;
RT   "Sequencing analyses and comparison of parainfluenza virus type 4A and 4B
RT   NP protein genes.";
RL   Virology 174:1-8(1990).
CC   -!- FUNCTION: Encapsidates the genome, protecting it from nucleases. The
CC       nucleocapsid (NC) has a helical structure. The encapsidated genomic RNA
CC       is termed the NC and serves as template for transcription and
CC       replication. During replication, encapsidation by N 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. In nucleocapsid, binds the P protein and thereby positions
CC       the polymerase on the template (By similarity). {ECO:0000250}.
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; M32983; AAA46802.1; -; mRNA.
DR   PIR; B33772; VHNZ4B.
DR   SMR; P17241; -.
DR   PRIDE; P17241; -.
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..551
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000142669"
FT   REGION          1..400
FT                   /note="Ncore"
FT                   /evidence="ECO:0000250"
FT   REGION          401..551
FT                   /note="Ntail"
FT                   /evidence="ECO:0000250"
FT   REGION          509..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        522..543
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   551 AA;  62426 MW;  D33B4F143F8F4B1E CRC64;
     MSSVLAAYEQ FLQTTEDRSF GDQQFVQSDT LKAEIPVFVL NTNDPQQRFT LMNFCLRLAV
     SSSAKSAIKQ GALLSLLSLQ ATSMQNHLMI AARAPDAALR IIEVDAIDPQ DYTLTINPRS
     GWDDIKIRAY RALSRDLPIS LADRTVFVSR DAEHAVCDDM DTYLNRIFSV LIQIWIMVCK
     CMTAYDQPTG SEERRLAKYK QQGRMLEKYQ LQTDARKIIQ LVIRESMVIR QFLVQEMLTA
     DKVGAYTNRY YAMVGDIAKY IANVGMSAFF LTLKFGLGNR WKPLALAAFS GELVKLKSFM
     SLYRRLGDRS RYLALLESPE LMEFAPANYP LLFSYAMGVG SVQDPLIRNY QFGRNFLNTS
     YFQYGVETAM KHQGTVDPKL ALELGITDED RVDIMQSVEK HISGKAGDDI SQPAGAFTMS
     LSRSAFINNN TSQDFSGARL SNYEQGWSGT NQDETRDVYP ESTMHRLQNI EPTDSDHNEL
     LMPELESDSN PFNRPRFTVR APLIPEISHQ NPTTRMNRNI NTRDNTRADH QDTNEDRGSN
     VPDDILGDLD N