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NCAP_RABVE
ID   NCAP_RABVE              Reviewed;         450 AA.
AC   P0DOF3; Q7TBN9;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2017, sequence version 1.
DT   29-SEP-2021, entry version 24.
DE   RecName: Full=Nucleoprotein;
DE            Short=NP;
DE   AltName: Full=Nucleocapsid protein;
DE            Short=Protein N;
GN   Name=N;
OS   Rabies virus (strain ERA) (RABV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Lyssavirus.
OX   NCBI_TaxID=11295;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=40674; Mammalia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=CVS-2003;
RX   PubMed=12970438; DOI=10.1128/jvi.77.19.10537-10547.2003;
RA   Prehaud C., Lay S., Dietzschold B., Lafon M.;
RT   "Glycoprotein of nonpathogenic rabies viruses is a key determinant of human
RT   cell apoptosis.";
RL   J. Virol. 77:10537-10547(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=CVS-2001;
RA   Prehaud C.J., Lay S.J.;
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=ERA;
RA   Geue L., Schares S., Schnick C., Kliemt J., Beckert A., Hoffmann B.,
RA   Freuling C., Marston D., McElhinney L., Fooks A., Zanoni R., Peterhans E.,
RA   Cox J., Mueller T.;
RT   "Complete nucleotide sequencing of SAD derivatives of attenuated rabies
RT   virus vaccine strains.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (3.49 ANGSTROMS).
RX   PubMed=16778023; DOI=10.1126/science.1125280;
RA   Albertini A.A., Wernimont A.K., Muziol T., Ravelli R.B., Clapier C.R.,
RA   Schoehn G., Weissenhorn W., Ruigrok R.W.;
RT   "Crystal structure of the rabies virus nucleoprotein-RNA complex.";
RL   Science 313:360-363(2006).
CC   -!- FUNCTION: Encapsidates the genome in a ratio of one protein N per nine
CC       ribonucleotides, protecting it from nucleases. If expressed without
CC       protein P it binds non-specifically RNA and therefore can bind it's own
CC       mRNA. Interaction with protein P abolishes any non-specific RNA
CC       binding, and prevents phosphorylation. The soluble N-P complex
CC       encapsidates specifically the genomic RNA, with protein N protecting
CC       the genome like a pearl necklace. The encapsidated genomic RNA is
CC       termed the nucleocapsid (NC) and serves as template for viral
CC       transcription and replication. Protein N binds protein P in the NC
CC       through a different interaction, and can be phosphorylated. Subsequent
CC       viral replication is dependent on intracellular concentration of newly
CC       synthesized protein N. During replication, encapsidation by protein N
CC       is coupled to RNA synthesis and all replicative products are resistant
CC       to nucleases (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homomultimerizes to form the nucleocapsid. Binds to viral
CC       genomic RNA. In nucleocapsid, binds protein P and thereby positions the
CC       polymerase on the template. Protein P acts as a chaperone on free
CC       protein N to prevent it from aggregation before encapsidating genomic
CC       RNA (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm {ECO:0000250}.
CC   -!- PTM: Phosphorylated by host CK2. Unphosphorylated protein N seems to
CC       have a better affinity for leader viral promoter encapsidation.
CC       Phosphorylation of protein N in ribonucleocapsid may stabilize the
CC       interaction with protein P, thereby playing an important role in viral
CC       transcription/replication (By similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: Displays a superantigen activity in human and mouse,
CC       activating mostly V-beta-8 subtypes of T-cell receptor. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the lyssavirus nucleocapsid protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF406696; AAP81753.1; -; Genomic_RNA.
DR   EMBL; EF206707; ABN11291.1; -; Genomic_RNA.
DR   PDB; 2GTT; X-ray; 3.49 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=1-450.
DR   PDBsum; 2GTT; -.
DR   SMR; P0DOF3; -.
DR   Proteomes; UP000008619; 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   Gene3D; 1.10.3570.10; -; 1.
DR   Gene3D; 1.10.3610.10; -; 1.
DR   InterPro; IPR000448; Rhabdo_ncapsid.
DR   InterPro; IPR023331; Rhabdovirus_ncapsid_C.
DR   InterPro; IPR023330; Rhabdovirus_ncapsid_N.
DR   InterPro; IPR035961; Rhabdovirus_nucleoprotein-like.
DR   Pfam; PF00945; Rhabdo_ncap; 1.
DR   SUPFAM; SSF140809; SSF140809; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Helical capsid protein; Host cytoplasm;
KW   Phosphoprotein; Ribonucleoprotein; RNA-binding; Superantigen;
KW   Viral nucleoprotein; Virion.
FT   CHAIN           1..450
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000295209"
FT   MOD_RES         389
FT                   /note="Phosphoserine; by host CK2"
FT                   /evidence="ECO:0000250"
FT   STRAND          12..14
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   HELIX           50..54
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   TURN            55..60
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   HELIX           66..76
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   STRAND          100..102
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   HELIX           134..152
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   HELIX           158..172
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   TURN            173..175
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   STRAND          176..178
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   TURN            189..192
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   HELIX           201..216
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   HELIX           222..226
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   HELIX           229..231
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   HELIX           237..247
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   STRAND          248..250
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   HELIX           256..259
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   HELIX           265..272
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   STRAND          275..277
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   STRAND          279..281
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   HELIX           285..287
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   HELIX           289..292
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   TURN            302..305
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   HELIX           306..318
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   HELIX           322..325
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   STRAND          331..333
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   HELIX           335..349
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   STRAND          360..362
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   HELIX           363..370
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   HELIX           402..410
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   TURN            411..414
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   HELIX           418..429
FT                   /evidence="ECO:0007829|PDB:2GTT"
FT   HELIX           438..445
FT                   /evidence="ECO:0007829|PDB:2GTT"
SQ   SEQUENCE   450 AA;  50578 MW;  6B5A4419AAFCEE04 CRC64;
     MDADKIVFKV NNQVVSLKPE IIVDQHEYKY PAIKDLKKPC ITLGKAPDLN KAYKSVLSGM
     SAAKLDPDDV CSYLAAAMQF FEGTCPEDWT SYGIVIARKG DKITPGSLVE IKRTDVEGNW
     ALTGGMELTR DPTVPEHASL VGLLLSLYRL SKISGQNTGN YKTNIADRIE QIFETAPFVK
     IVEHHTLMTT HKMCANWSTI PNFRFLAGTY DMFFSRIEHL YSAIRVGTVV TAYEDCSGLV
     SFTGFIKQIN LTAREAILYF FHKNFEEEIR RMFEPGQETA VPHSYFIHFR SLGLSGKSPY
     SSNAVGHVFN LIHFVGCYMG QVRSLNATVI AACAPHEMSV LGGYLGEEFF GKGTFERRFF
     RDEKELQEYE AAELTKTDVA LADDGTVNSD DEDYFSGETR SPEAVYTRIM MNGGRLKRSH
     IRRYVSVSSN HQARPNSFAE FLNKTYSSDS
 
 
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