ID   NCAP_UUKS               Reviewed;         254 AA.
AC   P22025;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Nucleoprotein;
DE   AltName: Full=Nucleocapsid protein;
DE            Short=Protein N;
GN   Name=N;
OS   Uukuniemi virus (strain S23) (UUKV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Ellioviricetes; Bunyavirales; Phenuiviridae; Phlebovirus.
OX   NCBI_TaxID=487099;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=34613; Ixodes ricinus (Common tick) (Acarus ricinus).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2136709; DOI=10.1128/jvi.64.1.247-255.1990;
RA   Simons J.F., Hellman U., Pettersson R.F.;
RT   "Uukuniemi virus S RNA segment: ambisense coding strategy, packaging of
RT   complementary strands into virions, and homology to members of the genus
RT   Phlebovirus.";
RL   J. Virol. 64:247-255(1990).
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; M33551; AAA47958.1; -; Genomic_RNA.
DR   PIR; A33559; VHVUUU.
DR   SMR; P22025; -.
DR   IntAct; P22025; 1.
DR   PRIDE; P22025; -.
DR   Proteomes; UP000008595; Genome.
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; Reference proteome; Ribonucleoprotein;
KW   RNA-binding; Viral nucleoprotein; Virion.
FT   CHAIN           1..254
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000221998"
FT   SITE            33
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:D3K5I7"
FT   SITE            36
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:D3K5I7"
FT   SITE            75
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:D3K5I7"
FT   SITE            76
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:D3K5I7"
FT   SITE            115
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:D3K5I7"
SQ   SEQUENCE   254 AA;  28508 MW;  922CBA7CDD7C6B12 CRC64;
     MAMPENWVRF AIEISDAQWE EEEIREFINL FQYQGFDAAV VLSRIFELAK KADLSRDQML
     RDIRALITLH LTRGNKLSSI EKRLSEEGKK EFALLKARYQ LVDKAKEAAD LTLSRIAIAN
     AGLTCRILPQ VVAHTAVTRS RMESLSADYP VCMMHNAFAG LIDETLPEDS IKALVDAHRL
     YLLEFSRTIN VKHRGMEAKE ILDANDSALQ AGLASSFLTP SQKRAYLLSF KLVDGNGKVN
     KAVQQAATVL RSLI