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NCAP_MUMP1
ID   NCAP_MUMP1              Reviewed;         553 AA.
AC   P21277;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   07-APR-2021, entry version 68.
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 SBL-1) (MuV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC   Orthorubulavirus; Mumps orthorubulavirus.
OX   NCBI_TaxID=11173;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2718626; DOI=10.1016/0168-1702(89)90055-5;
RA   Elango N.;
RT   "The mumps virus nucleocapsid mRNA sequence and homology among the
RT   Paramyxoviridae proteins.";
RL   Virus Res. 12:77-86(1989).
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; X57997; CAA41061.1; -; mRNA.
DR   PIR; A42759; VHNZSB.
DR   SMR; P21277; -.
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   2: Evidence at transcript level;
KW   Capsid protein; Helical capsid protein; Host cytoplasm; Ribonucleoprotein;
KW   RNA-binding; Viral nucleoprotein; Virion.
FT   CHAIN           1..553
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000142662"
FT   REGION          1..400
FT                   /note="Ncore"
FT                   /evidence="ECO:0000250"
FT   REGION          1..398
FT                   /note="P protein-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          1..375
FT                   /note="Homomultimerization"
FT                   /evidence="ECO:0000250"
FT   REGION          401..553
FT                   /note="Ntail"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   553 AA;  61787 MW;  F60BBB19AD963165 CRC64;
     MSSVLKAFER FTIEQELQDR GEEGSIPPET LKSAVKVFVI NTPNPTTRYQ MLNFCLRIIC
     SQNRRASHRV GALIALFSLP SAGMQNHIRL ADRSPEAQIE RCEIDGFEPG TYRLIPNARA
     NLTANEIAAY ALLADDLPPT INNGTPYVHA DVELQPCDEI EQFLDRCYSV LIQAWVMVCK
     CMTAYDQPAG SADRRFAKYQ QQGRLEARYM LQPEAQRLIQ TAIRKSLVVR QYLTFELQLA
     RRQGLLSNRY YAMVGDIGKY IENSGLTAFF LTLKYALGTK WSPLSLAAFT GELTKLRSLM
     MLYRDIGEQA RYLALLEAPQ IMDFAPGGYP LIFSYAMGVG SVLDVQMRNY TYARPFLNGY
     YFQIGVETAR RQQGTVDNRV ADDLGLTPEQ RNEVTQLVDR LARGRGAGIP GGPVNPFVPP
     VQQQQPAAVY ADIPALEESD DDGDEDGGAG FQNGVQVPAV RQGGQTDFRA QPLQDPIQAQ
     LFMPLYPQVS NIPNNRIIRS IASGGWKTKI YYDTTRMVIL NKMQGANTET LSQTIPIKTH
     SCKWATGMSK SLT
 
 
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