Q7TBN9 (NCAP_RABVE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nucleoprotein
Short name=NP

Alternative name(s):
Nucleocapsid protein
Short name=Protein N

Gene names

Name:

N

Organism

Rabies virus (strain ERA) (RABV) [Complete proteome]

Taxonomic identifier

11295 [NCBI]

Taxonomic lineage

Viruses › ssRNA viruses › ssRNA negative-strand viruses › Mononegavirales › Rhabdoviridae › Lyssavirus › Rabies virus

Virus host

Homo sapiens (Human) [TaxID: 9606]
Mammalia [TaxID: 40674]

Protein attributes

Sequence length	450 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Encapsidates the genome in a ratio of one protein N per nine ribonucleotides, protecting it from nucleases. If expressed without protein P it binds non-specifically RNA and therefore can bind it's own mRNA. Interaction with protein P abolishes any non-specific RNA binding, and prevents phosphorylation. The soluble N-P complex encapsidates specifically the genomic RNA, with protein N protecting the genome like a pearl necklace. The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for viral transcription and replication. Protein N binds protein P in the NC through a different interaction, and can be phosphorylated. Subsequent viral replication is dependent on intracellular concentration of newly synthesized protein N. During replication, encapsidation by protein N is coupled to RNA synthesis and all replicative products are resistant to nucleases By similarity.
Subunit structure	Homomultimerizes to form the nucleocapsid. Binds to viral genomic RNA. In nucleocapsid, binds protein P and thereby positions the polymerase on the template. Protein P acts as a chaperone on free protein N to prevent it from aggregation before encapsidating genomic RNA By similarity.
Subcellular location	Virion. Host cytoplasm By similarity.
Post-translational modification	Phosphorylated by host CK2. Unphosphorylated protein N seems to have a better affinity for leader viral promoter encapsidation. Phosphorylation of protein N in ribonucleocapsid may stabilize the interaction with protein P, thereby playing an important role in viral transcription/replication By similarity.
Miscellaneous	Displays a superantigen activity in human and mouse, activating mostly V-beta-8 subtypes of T-cell receptor By similarity.
Sequence similarities	Belongs to the lyssavirus nucleocapsid protein family.

Ontologies

Keywords
Cellular component	Host cytoplasm Virion
Ligand	RNA-binding Viral nucleoprotein
Molecular function	Ribonucleoprotein Superantigen
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Cellular_component	host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell ribonucleoprotein complex Inferred from electronic annotation. Source: UniProtKB-KW viral nucleocapsid Inferred from electronic annotation. Source: InterPro
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 450

450

Nucleoprotein

PRO_0000295209

Amino acid modifications

Modified residue

389

1

Phosphoserine; by host CK2 By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

450

Helix Strand Turn

Details...

Beta strand

12 – 14

3

Helix

50 – 54

5

Turn

55 – 60

6

Helix

66 – 76

11

Beta strand

100 – 102

3

Helix

134 – 152

19

Helix

158 – 172

15

Turn

173 – 175

3

Beta strand

176 – 178

3

Turn

189 – 192

4

Helix

201 – 216

16

Helix

222 – 226

5

Helix

229 – 231

3

Helix

237 – 247

11

Beta strand

248 – 250

3

Helix

256 – 259

4

Helix

265 – 272

8

Beta strand

275 – 277

3

Beta strand

279 – 281

3

Helix

285 – 287

3

Helix

289 – 292

4

Turn

302 – 305

4

Helix

306 – 318

13

Helix

322 – 325

4

Beta strand

331 – 333

3

Helix

335 – 349

15

Beta strand

360 – 362

3

Helix

363 – 370

8

Helix

402 – 410

9

Turn

411 – 414

4

Helix

418 – 429

12

Helix

438 – 445

8

Sequences

	Sequence		Length	Mass (Da)
	Q7TBN9 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 6B5A4419AAFCEE04	FASTA	450	50,578
	10 20 30 40 50 60 MDADKIVFKV NNQVVSLKPE IIVDQHEYKY PAIKDLKKPC ITLGKAPDLN KAYKSVLSGM 70 80 90 100 110 120 SAAKLDPDDV CSYLAAAMQF FEGTCPEDWT SYGIVIARKG DKITPGSLVE IKRTDVEGNW 130 140 150 160 170 180 ALTGGMELTR DPTVPEHASL VGLLLSLYRL SKISGQNTGN YKTNIADRIE QIFETAPFVK 190 200 210 220 230 240 IVEHHTLMTT HKMCANWSTI PNFRFLAGTY DMFFSRIEHL YSAIRVGTVV TAYEDCSGLV 250 260 270 280 290 300 SFTGFIKQIN LTAREAILYF FHKNFEEEIR RMFEPGQETA VPHSYFIHFR SLGLSGKSPY 310 320 330 340 350 360 SSNAVGHVFN LIHFVGCYMG QVRSLNATVI AACAPHEMSV LGGYLGEEFF GKGTFERRFF 370 380 390 400 410 420 RDEKELQEYE AAELTKTDVA LADDGTVNSD DEDYFSGETR SPEAVYTRIM MNGGRLKRSH 430 440 450 IRRYVSVSSN HQARPNSFAE FLNKTYSSDS

References

[1]	"Glycoprotein of nonpathogenic rabies viruses is a key determinant of human cell apoptosis." Prehaud C., Lay S., Dietzschold B., Lafon M. J. Virol. 77:10537-10547(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Strain: CVS-2003.
[2]	Prehaud C.J., Lay S.J. Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Strain: CVS-2001.
[3]	"Complete nucleotide sequencing of SAD derivatives of attenuated rabies virus vaccine strains." Geue L., Schares S., Schnick C., Kliemt J., Beckert A., Hoffmann B., Freuling C., Marston D., McElhinney L., Fooks A., Zanoni R., Peterhans E., Cox J., Mueller T. Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Strain: ERA, Isolate SAD1-3670 var 1 and Isolate SAD1-3670 var 2.
[4]	"Crystal structure of the rabies virus nucleoprotein-RNA complex." Albertini A.A., Wernimont A.K., Muziol T., Ravelli R.B., Clapier C.R., Schoehn G., Weissenhorn W., Ruigrok R.W. Science 313:360-363(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.49 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF406696 Genomic RNA. Translation: AAP81753.1.
EF206707 Genomic RNA. Translation: ABN11291.1.
EF206717 Genomic RNA. Translation: ABN11341.1.
EF206718 Genomic RNA. Translation: ABN11346.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GTT	X-ray	3.49	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V	1-450	[»]

ProteinModelPortal

Q7TBN9.

SMR

Q7TBN9. Positions 5-448.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

1.10.3570.10. 1 hit.
1.10.3610.10. 1 hit.

InterPro

IPR000448. Rhabdo_ncapsid.
IPR023331. Rhabdovirus_ncapsid_C.
IPR023330. Rhabdovirus_ncapsid_N.
[Graphical view]

Pfam

PF00945. Rhabdo_ncap. 1 hit.
[Graphical view]

ProDom

PD002087. Rhabd_nucleocap. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF140809. SSF140809. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q7TBN9.

Entry information

Entry name

NCAP_RABVE

Accession

Primary (citable) accession number: Q7TBN9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	October 1, 2003
Last modified:	April 3, 2013
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program