NCAP_PI1HW
ID NCAP_PI1HW Reviewed; 524 AA.
AC P26590;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 02-JUN-2021, entry version 67.
DE RecName: Full=Nucleoprotein;
DE AltName: Full=Nucleocapsid protein;
DE Short=NP;
DE Short=Protein N;
GN Name=N; Synonyms=NP;
OS Human parainfluenza 1 virus (strain Washington/1957) (HPIV-1).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Respirovirus.
OX NCBI_TaxID=11211;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1707951; DOI=10.1099/0022-1317-72-4-983;
RA Lyn D., Gill D.S., Scroggs R.A., Portner A.;
RT "The nucleoproteins of human parainfluenza virus type 1 and Sendai virus
RT share amino acid sequences and antigenic and structural determinants.";
RL J. Gen. Virol. 72:983-987(1991).
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.
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; D01070; BAA00873.1; -; mRNA.
DR PIR; A38401; VHNZT1.
DR PDB; 2CII; X-ray; 2.55 A; C=324-332.
DR PDBsum; 2CII; -.
DR SMR; P26590; -.
DR EvolutionaryTrace; P26590; -.
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..524
FT /note="Nucleoprotein"
FT /id="PRO_0000142673"
FT REGION 1..400
FT /note="Ncore"
FT /evidence="ECO:0000250"
FT REGION 401..524
FT /note="Ntail"
FT /evidence="ECO:0000250"
FT REGION 489..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 524 AA; 57545 MW; D931FE19A9F6F208 CRC64;
MAGLLSTFDT FSSRRSESIN KSGGGAIIPG QRSTVSVFIL GPSVTDDADK LLIATTFLAH
SLDTDKQHSQ RGGFLVSLLA MAIRSPELYL TTNGVNADVK YVIYNIERDP KRTKTDGFIV
KTRDMEYERT TEWLFGPMIN KNPLFQGQRE NADLEALLQT YGYPACLGAI IVQVWIVLVK
AITSSAGLRK GFFNRLEAFR QDGTVKSALV FTGDTVEGIG AVMRSQQSLV SLMVETLVTM
NTSRSDLTTL EKNIQIVGNY IRDAGLASFM NTIKYGVETK MAALTLSNLR PDINKLRSLV
DIYLSKGARA PFICILRDPV HGEFAPGNYP ALWSYAMGVA VVQNKAMQQY VTGRTYLDME
MFLLGQAVAK DADSKISSAL EEELNVTDTA KERLRHHLTN LSGGDGAYHK PTGGGAIEVA
IDHTDITFGA EDTADRDNKN WTNNSNERWS NHSINNHTIT ISGAEQLEEE TNDEDITDIE
NKIARRLADK KQRLSQANNK QDANSDADYE NDDDATAAAG IGGI
