NCAP_PI3H4
ID NCAP_PI3H4 Reviewed; 515 AA.
AC P06159; Q81075;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Nucleoprotein;
DE AltName: Full=Nucleocapsid protein;
DE Short=NP;
DE Short=Protein N;
GN Name=N; Synonyms=NP;
OS Human parainfluenza 3 virus (strain Wash/47885/57) (HPIV-3) (Human
OS parainfluenza 3 virus (strain NIH 47885)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Respirovirus.
OX NCBI_TaxID=11217;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2878059; DOI=10.1099/0022-1317-67-11-2543;
RA Jambou R.C., Elango N., Venkatesan S., Collins P.L.;
RT "Complete sequence of the major nucleocapsid protein gene of human
RT parainfluenza type 3 virus: comparison with other negative strand
RT viruses.";
RL J. Gen. Virol. 67:2543-2548(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3012866; DOI=10.1016/0042-6822(86)90382-x;
RA Sanchez A., Banerjee A.K., Furuichi Y., Richardson M.A.;
RT "Conserved structures among the nucleocapsid proteins of the
RT paramyxoviridae: complete nucleotide sequence of human parainfluenza virus
RT type 3 NP mRNA.";
RL Virology 152:171-180(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA / MRNA].
RC STRAIN=Isolate 104B44;
RX PubMed=2418584; DOI=10.1016/0042-6822(86)90116-9;
RA Galinski M.S., Mink M.A., Lambert D.M., Wechsler S.L., Pons M.W.;
RT "Molecular cloning and sequence analysis of the human parainfluenza 3 virus
RT RNA encoding the nucleocapsid protein.";
RL Virology 149:139-151(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=JS;
RX PubMed=8266719; DOI=10.1016/0168-1702(93)90014-e;
RA Stokes A., Tierney E.L., Sarris C.M., Murphy B.R., Hall S.L.;
RT "The complete nucleotide sequence of two cold-adapted, temperature-
RT sensitive attenuated mutant vaccine viruses (cp12 and cp45) derived from
RT the JS strain of human parainfluenza virus type 3 (PIV3).";
RL Virus Res. 30:43-52(1993).
RN [5]
RP RNA-BINDING.
RC STRAIN=JS;
RX PubMed=9234948; DOI=10.1006/viro.1997.8633;
RA Durbin A.P., Siew J.W., Murphy B.R., Collins P.L.;
RT "Minimum protein requirements for transcription and RNA replication of a
RT minigenome of human parainfluenza virus type 3 and evaluation of the rule
RT of six.";
RL Virology 234:74-83(1997).
CC -!- FUNCTION: Encapsidates the genome in a ratio of 1 N per 6
CC ribonucleotides, protecting it from nucleases. The nucleocapsid (NC)
CC has a helical structure. The encapsidated genomic RNA is termed the NC
CC and serves as template for transcription and replication. During
CC replication, encapsidation by N is coupled to RNA synthesis and all
CC replicative products are resistant to nucleases (By similarity).
CC {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; D10025; BAA00915.1; -; mRNA.
DR EMBL; X04612; CAA28282.1; -; Genomic_RNA.
DR EMBL; M11849; AAA46863.1; -; Genomic_RNA.
DR EMBL; M14552; AAA46864.1; -; Genomic_RNA.
DR EMBL; U51116; AAB48684.1; -; Genomic_RNA.
DR PIR; A24285; VHNZP3.
DR PDB; 7EV8; X-ray; 3.23 A; A=29-374.
DR PDBsum; 7EV8; -.
DR SMR; P06159; -.
DR DIP; DIP-1086N; -.
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..515
FT /note="Nucleoprotein"
FT /id="PRO_0000142667"
FT REGION 1..400
FT /note="Ncore"
FT /evidence="ECO:0000250"
FT REGION 401..515
FT /note="Ntail"
FT /evidence="ECO:0000250"
FT REGION 450..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 45
FT /note="N -> D (in strain: Isolate 104B44)"
FT VARIANT 104
FT /note="E -> R (in strain: JS)"
FT VARIANT 129
FT /note="E -> D (in strain: JS)"
FT VARIANT 284
FT /note="T -> S (in strain: Isolate 104B44)"
FT VARIANT 389
FT /note="A -> S (in strain: JS)"
FT VARIANT 436
FT /note="D -> N (in strain: JS)"
FT VARIANT 457
FT /note="R -> Q (in strain: JS)"
FT VARIANT 489
FT /note="G -> S (in strain: JS)"
FT VARIANT 493
FT /note="S -> P (in strain: JS)"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:7EV8"
FT HELIX 44..58
FT /evidence="ECO:0007829|PDB:7EV8"
FT HELIX 65..78
FT /evidence="ECO:0007829|PDB:7EV8"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:7EV8"
FT STRAND 94..105
FT /evidence="ECO:0007829|PDB:7EV8"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:7EV8"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:7EV8"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:7EV8"
FT HELIX 155..160
FT /evidence="ECO:0007829|PDB:7EV8"
FT HELIX 162..180
FT /evidence="ECO:0007829|PDB:7EV8"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:7EV8"
FT HELIX 187..201
FT /evidence="ECO:0007829|PDB:7EV8"
FT HELIX 212..224
FT /evidence="ECO:0007829|PDB:7EV8"
FT HELIX 226..238
FT /evidence="ECO:0007829|PDB:7EV8"
FT HELIX 248..261
FT /evidence="ECO:0007829|PDB:7EV8"
FT HELIX 266..275
FT /evidence="ECO:0007829|PDB:7EV8"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:7EV8"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:7EV8"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:7EV8"
FT HELIX 289..305
FT /evidence="ECO:0007829|PDB:7EV8"
FT HELIX 306..311
FT /evidence="ECO:0007829|PDB:7EV8"
FT TURN 312..316
FT /evidence="ECO:0007829|PDB:7EV8"
FT TURN 318..323
FT /evidence="ECO:0007829|PDB:7EV8"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:7EV8"
FT HELIX 329..342
FT /evidence="ECO:0007829|PDB:7EV8"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:7EV8"
FT HELIX 358..373
FT /evidence="ECO:0007829|PDB:7EV8"
SQ SEQUENCE 515 AA; 57827 MW; 438044FE092A6271 CRC64;
MLSLFDTFNA RRQENITKSA GGAIIPGQKN TVSIFALGPT ITDDNEKMTL ALLFLSHSLD
NEKQHAQRAG FLVSLLSMAY ANPELYLTTN GSNADVKYVI YMIEKDLKRQ KYGGFVVKTR
EMIYEKTTEW IFGSDLDYDQ ETMLQNGRNN STIEDLVHTF GYPSCLGALI IQIWIVLVKA
ITSISGLRKG FFTRLEAFRQ DGTVQAGLVL SGDTVDQIGS IMRSQQSLVT LMVETLITMN
TSRNDLTTIE KNIQIVGNYI RDAGLASFFN TIRYGIETRM AALTLSTLRP DINRLKALME
LYLSKGPRAP FICILRDPIH GEFAPGNYPA IWSYAMGVAV VQNRAMQQYV TGRSYLDIDM
FQLGQAVARD AEAQMSSTLE DELGVTHEAK ESLKRHIRNI NSSETSFHKP TGGSAIEMAI
DEEPEQFEHR ADQEQDGEPQ SSIIQYAWAE GNRSDDRTEQ ATESDNIKTE QQNIRDRLNK
RLNDKKKQGS QPSTNPTNRT NQDEIDDLFN AFGSN
