NCAP_MUMPJ
ID NCAP_MUMPJ Reviewed; 549 AA.
AC Q77IS8;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=Nucleoprotein;
DE AltName: Full=Nucleocapsid protein;
DE Short=NP;
DE Short=Protein N;
GN Name=N; Synonyms=NP;
OS Mumps virus (strain Jeryl-Lynn) (MuV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC Orthorubulavirus; Mumps orthorubulavirus.
OX NCBI_TaxID=11168;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Jeryl-Lynn;
RX PubMed=12350348; DOI=10.1006/viro.2002.1499;
RA Amexis G., Rubin S., Chizhikov V., Pelloquin F., Carbone K., Chumakov K.;
RT "Sequence diversity of Jeryl Lynn strain of mumps virus: quantitative
RT mutant analysis for vaccine quality control.";
RL Virology 300:171-179(2002).
RN [2]
RP INTERACTION WITH P PROTEIN.
RX PubMed=15280472; DOI=10.1128/jvi.78.16.8630-8640.2004;
RA Kingston R.L., Baase W.A., Gay L.S.;
RT "Characterization of nucleocapsid binding by the measles virus and mumps
RT virus phosphoproteins.";
RL J. Virol. 78:8630-8640(2004).
CC -!- FUNCTION: Encapsidates the genome, protecting it from nucleases. The
CC nucleocapsid (NC) has a helical structure, approximately 20 nm in
CC diameter, with a hollow central cavity approximately 5 nm in diameter.
CC The encapsidated genomic RNA is termed the NC and serves as template
CC for transcription and replication. During replication, encapsidation by
CC N is coupled to RNA synthesis and all replicative products are
CC resistant to nucleases (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homomultimerizes to form the nucleocapsid. Binds to viral
CC genomic RNA. In nucleocapsid, binds the P protein and thereby positions
CC the polymerase on the template (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm.
CC -!- DOMAIN: Ncore is globular and carries regions required for N self-
CC assembly and RNA-binding. Ntail is an intrinsically disordered
CC monomeric domain (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the paramyxoviruses nucleocapsid family.
CC {ECO:0000305}.
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DR EMBL; AF338106; AAK83227.1; -; Genomic_RNA.
DR PDB; 7EWQ; EM; 3.50 A; A=1-549.
DR PDBsum; 7EWQ; -.
DR SMR; Q77IS8; -.
DR Proteomes; UP000163835; 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 Ribonucleoprotein; RNA-binding; Viral nucleoprotein; Virion.
FT CHAIN 1..549
FT /note="Nucleoprotein"
FT /id="PRO_0000142660"
FT REGION 1..400
FT /note="Ncore"
FT /evidence="ECO:0000250"
FT REGION 1..398
FT /note="P protein-binding"
FT REGION 1..375
FT /note="Homomultimerization"
FT REGION 401..549
FT /note="Ntail"
FT /evidence="ECO:0000250"
FT REGION 517..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 3..17
FT /evidence="ECO:0007829|PDB:7EWQ"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:7EWQ"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:7EWQ"
FT HELIX 45..60
FT /evidence="ECO:0007829|PDB:7EWQ"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:7EWQ"
FT HELIX 84..91
FT /evidence="ECO:0007829|PDB:7EWQ"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:7EWQ"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:7EWQ"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:7EWQ"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:7EWQ"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:7EWQ"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:7EWQ"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:7EWQ"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:7EWQ"
FT HELIX 160..179
FT /evidence="ECO:0007829|PDB:7EWQ"
FT TURN 180..183
FT /evidence="ECO:0007829|PDB:7EWQ"
FT HELIX 190..201
FT /evidence="ECO:0007829|PDB:7EWQ"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:7EWQ"
FT HELIX 213..224
FT /evidence="ECO:0007829|PDB:7EWQ"
FT HELIX 228..240
FT /evidence="ECO:0007829|PDB:7EWQ"
FT HELIX 249..261
FT /evidence="ECO:0007829|PDB:7EWQ"
FT HELIX 267..276
FT /evidence="ECO:0007829|PDB:7EWQ"
FT HELIX 283..286
FT /evidence="ECO:0007829|PDB:7EWQ"
FT HELIX 290..306
FT /evidence="ECO:0007829|PDB:7EWQ"
FT HELIX 308..312
FT /evidence="ECO:0007829|PDB:7EWQ"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:7EWQ"
FT HELIX 319..322
FT /evidence="ECO:0007829|PDB:7EWQ"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:7EWQ"
FT HELIX 330..343
FT /evidence="ECO:0007829|PDB:7EWQ"
FT HELIX 346..349
FT /evidence="ECO:0007829|PDB:7EWQ"
FT HELIX 359..373
FT /evidence="ECO:0007829|PDB:7EWQ"
SQ SEQUENCE 549 AA; 61415 MW; D15FC936E29D27B5 CRC64;
MSSVLKAFER FTIEQELQDR GEEGSIPPET LKSAVKVFVI NTPNPTTRYQ MLNFCLRIIC
SQNARASHRV GALITLFSLP SAGMQNHIRL ADRSPEAQIE RCEIDGFEPG TYRLIPNARA
NLTANEIAAY ALLADDLPPT INNGTPYVHA DVEGQPCDEI EQFLDRCYSV LIQAWVMVCK
CMTAYDQPAG SADRRFAKYQ QQGRLEARYM LQPEAQRLIQ TAIRKSLVVR QYLTFELQLA
RRQGLLSNRY YAMVGDIGKY IENSGLTAFF LTLKYALGTK WSPLSLAAFT GELTKLRSLM
MLYRGLGEQA RYLALLEAPQ IMDFAPGGYP LIFSYAMGVG TVLDVQMRNY TYARPFLNGY
YFQIGVETAR RQQGTVDNRV ADDLGLTPEQ RTEVTQLVDR LARGRGAGIP GGPVNPFVPP
VQQQQPAAVY EDIPALEESD DDGDEDGGAG FQNGVQLPAV RQGGQTDFRA QPLQDPIQAQ
LFMPLYPQVS NMPNNQNHQI NRIGGLEHQD LLRYNENGDS QQDARGEHVN TFPNNPNQNA
QLQVGDWDE
