NCAP_HMPVC
ID NCAP_HMPVC Reviewed; 394 AA.
AC Q6WBA1;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 02-JUN-2021, entry version 41.
DE RecName: Full=Nucleoprotein;
DE Short=Protein N;
DE AltName: Full=Nucleocapsid protein;
GN Name=N;
OS Human metapneumovirus (strain CAN97-83) (HMPV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Metapneumovirus.
OX NCBI_TaxID=694067;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=14592754; DOI=10.1016/s0042-6822(03)00528-2;
RA Biacchesi S., Skiadopoulos M.H., Boivin G., Hanson C.T., Murphy B.R.,
RA Collins P.L., Buchholz U.J.;
RT "Genetic diversity between human metapneumovirus subgroups.";
RL Virology 315:1-9(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16306583; DOI=10.1128/jvi.79.24.15114-15122.2005;
RA Pham Q.N., Biacchesi S., Skiadopoulos M.H., Murphy B.R., Collins P.L.,
RA Buchholz U.J.;
RT "Chimeric recombinant human metapneumoviruses with the nucleoprotein or
RT phosphoprotein open reading frame replaced by that of avian metapneumovirus
RT exhibit improved growth in vitro and attenuation in vivo.";
RL J. Virol. 79:15114-15122(2005).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=28978704; DOI=10.1128/jvi.01282-17;
RA Cifuentes-Munoz N., Branttie J., Slaughter K.B., Dutch R.E.;
RT "Human Metapneumovirus Induces Formation of Inclusion Bodies for Efficient
RT Genome Replication and Transcription.";
RL J. Virol. 91:0-0(2017).
CC -!- FUNCTION: Encapsidates the viral RNA genome by forming a left-handed
CC helical nucleocapsid that protects the RNA from nucleases. RNA
CC replication depends on the availability of soluble nucleoprotein. The
CC encapsidated genomic RNA is termed the NC and serves as template for
CC transcription and replication. {ECO:0000250|UniProtKB:P03418}.
CC -!- SUBUNIT: Homomultimerizes to form the nucleocapsid. Binds to viral
CC genomic RNA. Interacts with the phosphoprotein P. When in a monomeric
CC RNA-free form, interacts with the phosphoprotein (via N-terminus).
CC Interacts with protein M2-1; this interaction allows the association of
CC nucleocapsid with the matrix protein. {ECO:0000250|UniProtKB:P03418}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P03418}. Host
CC cytoplasm {ECO:0000269|PubMed:28978704}. Note=Localizes in cytoplasmic
CC inclusion bodies. {ECO:0000269|PubMed:28978704}.
CC -!- SIMILARITY: Belongs to the paramyxoviruses nucleocapsid family.
CC {ECO:0000305}.
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DR EMBL; AY297749; AAQ67692.1; -; Genomic_RNA.
DR RefSeq; YP_012605.1; NC_004148.2.
DR SMR; Q6WBA1; -.
DR PRIDE; Q6WBA1; -.
DR Proteomes; UP000001398; 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 InterPro; IPR004930; Pneumo_ncap.
DR Pfam; PF03246; Pneumo_ncap; 1.
PE 3: Inferred from homology;
KW Capsid protein; Helical capsid protein; Host cytoplasm; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Viral nucleoprotein; Virion.
FT CHAIN 1..394
FT /note="Nucleoprotein"
FT /id="PRO_0000394805"
SQ SEQUENCE 394 AA; 43538 MW; A9D91AC924CA2551 CRC64;
MSLQGIHLSD LSYKHAILKE SQYTIKRDVG TTTAVTPSSL QQEITLLCGE ILYAKHADYK
YAAEIGIQYI STALGSERVQ QILRNSGSEV QVVLTRTYSL GKVKNNKGED LQMLDIHGVE
KSWVEEIDKE ARKTMATLLK ESSGNIPQNQ RPSAPDTPII LLCVGALIFT KLASTIEVGL
ETTVRRANRV LSDALKRYPR MDIPKIARSF YDLFEQKVYY RSLFIEYGKA LGSSSTGSKA
ESLFVNIFMQ AYGAGQTMLR WGVIARSSNN IMLGHVSVQA ELKQVTEVYD LVREMGPESG
LLHLRQSPKA GLLSLANCPN FASVVLGNAS GLGIIGMYRG RVPNTELFSA AESYAKSLKE
SNKINFSSLG LTDEEKEAAE HFLNVSDDSQ NDYE