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NCAP_SENDZ
ID   NCAP_SENDZ              Reviewed;         517 AA.
AC   P04858; P27563; Q88268;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   07-OCT-2020, entry version 80.
DE   RecName: Full=Nucleoprotein;
DE   AltName: Full=Nucleocapsid protein;
DE            Short=NP;
DE            Short=Protein N;
GN   Name=N; Synonyms=NP;
OS   Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ)).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Respirovirus.
OX   NCBI_TaxID=11198;
OH   NCBI_TaxID=10144; Cavia cutleri (Guinea pig).
OH   NCBI_TaxID=36483; Cricetidae sp. (Hamster).
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
OH   NCBI_TaxID=10116; Rattus norvegicus (Rat).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6316257; DOI=10.1093/nar/11.21.7317;
RA   Shioda T., Hidaka Y., Kanda T., Shibuta H., Nomoto A., Iwasaki K.;
RT   "Sequence of 3,687 nucleotides from the 3' end of Sendai virus genome RNA
RT   and the predicted amino acid sequences of viral NP, P and C proteins.";
RL   Nucleic Acids Res. 11:7317-7330(1983).
RN   [2]
RP   SEQUENCE REVISION.
RA   Shibuta H.;
RL   Submitted (FEB-1985) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Mutant F1-R, and Mutant ts-f1;
RX   PubMed=2161155; DOI=10.1016/0042-6822(90)90040-x;
RA   Middleton Y., Tashiro M., Thai T., Oh J., Seymour J., Pritzer E.,
RA   Klenk H.-D., Rott R., Seto J.T.;
RT   "Nucleotide sequence analyses of the genes encoding the HN, M, NP, P, and L
RT   proteins of two host range mutants of Sendai virus.";
RL   Virology 176:656-657(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Mutant F1-R / T-5 revertant, and Mutant F1-R / T-7 revertant;
RX   PubMed=1651590; DOI=10.1016/0042-6822(91)90839-4;
RA   Tashiro M., James I., Karri S., Wahn K., Tobita K., Klenk H.-D., Rott R.,
RA   Seto J.T.;
RT   "Pneumotropic revertants derived from a pantropic mutant, F1-R, of Sendai
RT   virus.";
RL   Virology 184:227-234(1991).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 324-332 COMPLEXED WITH MHC CLASS I
RP   H-2DB.
RX   PubMed=10023771; DOI=10.1016/s1074-7613(00)80007-2;
RA   Glithero A., Tormo J., Haurum J.S., Arsequell G., Valencia G., Edwards J.,
RA   Springer S., Townsend A., Pao Y.L., Wormald M., Dwek R.A., Jones E.Y.,
RA   Elliott T.;
RT   "Crystal structures of two H-2Db/glycopeptide complexes suggest a molecular
RT   basis for CTL cross-reactivity.";
RL   Immunity 10:63-74(1999).
CC   -!- FUNCTION: Encapsidates the genome in a ratio of one N per six
CC       ribonucleotides, protecting it from nucleases. The nucleocapsid (NC)
CC       has a helical structure with 13.07 N per turn. The encapsidated genomic
CC       RNA is termed the NC and serves as template for transcription and
CC       replication. Replication is dependent on intracellular concentration of
CC       newly synthesized N, termed N(0), which corresponds to the protein not
CC       associated with RNA. In contrast, when associated with RNA, it is
CC       termed N. During replication, encapsidation by N(0) is coupled to RNA
CC       synthesis and all replicative products are resistant to nucleases.
CC   -!- SUBUNIT: Homomultimerizes to form the nucleocapsid. Binds to viral
CC       genomic RNA. N in nucleocapsid binds the P protein and thereby
CC       positions the polymerase on the template. Interaction of N(0) with the
CC       P protein prevents the uncontrolled aggregation of N(0) (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm.
CC   -!- DOMAIN: There are two distinct binding regions to the P protein, one
CC       used by N(0) and the other by N in nucleocapsid. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Most abundant protein in the virion. There are 2564
CC       molecules per encapsidated genome (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the paramyxoviruses nucleocapsid family.
CC       {ECO:0000305}.
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DR   EMBL; X00087; CAA24945.1; -; Genomic_RNA.
DR   EMBL; M30202; AAB06278.1; -; Genomic_RNA.
DR   EMBL; M30203; AAB06284.1; -; Genomic_RNA.
DR   EMBL; M30204; AAB06196.1; -; Genomic_RNA.
DR   EMBL; M69046; AAB06290.1; -; Genomic_RNA.
DR   EMBL; M55565; AAB06297.1; -; Genomic_RNA.
DR   PIR; A04029; VHNZSV.
DR   PDB; 1CE6; X-ray; 2.90 A; C=324-332.
DR   PDBsum; 1CE6; -.
DR   BMRB; P04858; -.
DR   SMR; P04858; -.
DR   EvolutionaryTrace; P04858; -.
DR   Proteomes; UP000006560; Genome.
DR   Proteomes; UP000110830; Genome.
DR   Proteomes; UP000163956; Genome.
DR   Proteomes; UP000169749; Genome.
DR   Proteomes; UP000181310; 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   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   InterPro; IPR002021; Paramyx_ncap.
DR   Pfam; PF00973; Paramyxo_ncap; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Helical capsid protein; Host cytoplasm;
KW   Reference proteome; Ribonucleoprotein; RNA-binding; Viral nucleoprotein;
KW   Virion.
FT   CHAIN           1..517
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000142684"
FT   REGION          462..471
FT                   /note="Binding of N in nucleoprotein to P protein"
FT                   /evidence="ECO:0000250"
FT   VARIANT         24
FT                   /note="R -> G (in strain: Mutant F1-R, Mutant ts-f1, Mutant
FT                   F1-R / T-5 revertant and Mutant F1-R / T-7 revertant)"
FT   VARIANT         42
FT                   /note="L -> P (in strain: Mutant F1-R / T-5 revertant and
FT                   Mutant F1-R / T-7 revertant)"
FT   VARIANT         67
FT                   /note="R -> Q (in strain: Mutant F1-R, Mutant ts-f1, Mutant
FT                   F1-R / T-5 revertant and Mutant F1-R / T-7 revertant)"
FT   VARIANT         377
FT                   /note="S -> T (in strain: Mutant F1-R, Mutant ts-f1, Mutant
FT                   F1-R / T-5 revertant and Mutant F1-R / T-7 revertant)"
FT   VARIANT         388..389
FT                   /note="EA -> DT (in strain: Mutant F1-R, Mutant ts-f1,
FT                   Mutant F1-R / T-5 revertant and Mutant F1-R / T-7
FT                   revertant)"
FT   VARIANT         400
FT                   /note="S -> N (in strain: Mutant F1-R, Mutant ts-f1, Mutant
FT                   F1-R / T-5 revertant and Mutant F1-R / T-7 revertant)"
FT   VARIANT         405
FT                   /note="N -> D (in strain: Mutant F1-R, Mutant ts-f1, Mutant
FT                   F1-R / T-5 revertant and Mutant F1-R / T-7 revertant)"
FT   VARIANT         489
FT                   /note="E -> G (in strain: Mutant F1-R and Mutant F1-R / T-7
FT                   revertant)"
FT   VARIANT         494..517
FT                   /note="ILQPMEMKAAITVSIMTKMTIPQQ -> DSATHGDEGRNNGVDHDEDDDTAA
FT                   VAGVGGI (in strain: Mutant F1-R, Mutant ts-f1, Mutant F1-R
FT                   / T-5 revertant and Mutant F1-R / T-7 revertant)"
SQ   SEQUENCE   517 AA;  56762 MW;  AD25055F8A624973 CRC64;
     MAGLLSTFDT FSSRRSESIN KSGRGAVIPG QRSTVSVFVL GLSVTDDADK LFIATTFLAH
     SLDTDKRHSQ RGGFLVSLLA MAYSSPELYL TTNGVNADVK YVIYNIEKDP KRTKTDGFIV
     KTRDMEYERT TEWLFGPMVN KSPLFQGQRD AADPDTLLQI YGYPACLGAI IVQVWIVLVK
     AITSSAGLRK GFFNRLEAFR QDGTVKGALV FTGETVEGIG SVMRSQQSLV SLMVETLVTM
     NTARSDLTTL EKNIQIVGNY IRDAGLASFM NTIKYGVETK MAALTLSNLR PDINKLRSLI
     DTYLSKGPRA PFICILKDPV HGEFAPGNYP ALWSYAMGVA VVQNKAMQQY VTGRTYLDME
     MFLLGQAVAK DAESKISSAL EDELGVTEAA KGRLRHHLAS LSGGNGAYRK PTGGGAIEVA
     LDNADIDLET KAHADQDARG WGGDSGERWA RQVSGGHFVT LHGAERLEEE TNDEDVSDIE
     RRIAMRLAER RQEILQPMEM KAAITVSIMT KMTIPQQ
 
 
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