ID   NCAP_PTPV               Reviewed;         243 AA.
AC   P03515;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Nucleoprotein;
DE   AltName: Full=Nucleocapsid protein;
DE            Short=Protein N;
GN   Name=N;
OS   Punta toro phlebovirus.
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Ellioviricetes; Bunyavirales; Phenuiviridae; Phlebovirus.
OX   NCBI_TaxID=11587;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=29031; Phlebotomus papatasi (Sandfly).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6087547; DOI=10.1016/0042-6822(84)90166-1;
RA   Ihara T., Akashi H., Bishop D.H.L.;
RT   "Novel coding strategy (ambisense genomic RNA) revealed by sequence
RT   analyses of Punta toro phlebovirus S RNA.";
RL   Virology 136:293-306(1984).
CC   -!- FUNCTION: Encapsidates the genomic RNA, protecting it from nucleases.
CC       Displays high affinity for single-stranded nucleic acid. The
CC       encapsidated genomic RNA is termed the nucleocapsid (NC) or
CC       ribonucleoprotein. The ribonucleoprotein has a non-helical structure
CC       (By similarity). Serves as template for viral transcription and
CC       replication. After replication, the nucleocapsid is recruited to the
CC       host Golgi apparatus by glycoprotein Gn for packaging into virus
CC       particles (By similarity). {ECO:0000250|UniProtKB:D3K5I7,
CC       ECO:0000250|UniProtKB:P21700}.
CC   -!- SUBUNIT: Homodimer. Homohexamer; ring-shaped, necessary to form the
CC       nucleocapsid (By similarity). Homopentamers; opened pentamers in
CC       solution (By similarity). Binds to viral genomic RNA (By similarity).
CC       Interacts with glycoprotein Gn; this interaction allows packaging of
CC       nucleocapsids into virions (By similarity).
CC       {ECO:0000250|UniProtKB:D3K5I7, ECO:0000250|UniProtKB:P21700,
CC       ECO:0000250|UniProtKB:P21701}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:D3K5I7}. Host
CC       cytoplasm {ECO:0000250|UniProtKB:D3K5I7}. Host nucleus
CC       {ECO:0000250|UniProtKB:D3K5I7}. Host endoplasmic reticulum-Golgi
CC       intermediate compartment {ECO:0000250|UniProtKB:I6WJ72}. Host Golgi
CC       apparatus {ECO:0000250|UniProtKB:I6WJ72}.
CC   -!- SIMILARITY: Belongs to the phlebovirus nucleocapsid protein family.
CC       {ECO:0000305}.
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DR   EMBL; K02736; AAA47114.1; -; Genomic_RNA.
DR   PIR; A04107; VHVUPT.
DR   SMR; P03515; -.
DR   PRIDE; P03515; -.
DR   GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR009522; Capsid_Phlebovir/Tenuivir.
DR   InterPro; IPR015971; Nucleocapsid_Phlebovirus.
DR   Pfam; PF05733; Tenui_N; 1.
DR   PIRSF; PIRSF003953; N_PhelboV; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Helical capsid protein; Host cytoplasm;
KW   Host Golgi apparatus; Host nucleus; Ribonucleoprotein; RNA-binding;
KW   Viral nucleoprotein; Virion.
FT   CHAIN           1..243
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000221994"
FT   SITE            29
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:D3K5I7"
FT   SITE            32
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:D3K5I7"
FT   SITE            65
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:D3K5I7"
FT   SITE            66
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:D3K5I7"
FT   SITE            98
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:D3K5I7"
FT   SITE            105
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:D3K5I7"
SQ   SEQUENCE   243 AA;  26911 MW;  0CE34C9E1DBA0589 CRC64;
     MSYEEIAVQF ASESIDEQTV AGWVTDFAYQ GFDAKRVIAL VKDRGGEDWK QDVKKMIVLS
     LTRGNKPNKM ILKMSDKGKA MVNELVLKYK LKSGNPSRDD LTLSRITAAF AGWTCQAADY
     VQEYLPVTGR AMDAISSSYP RAMMHPSFAG LIDQELPADV FSEITQAHCL FMIQFSKTIN
     PSLRGLSKDE IVSSFERPMQ AAISSTFLTS ANRRAMLKTL GIINDNLKPS SSTVSAAKVF
     RSL