NCAP_MERS1
ID NCAP_MERS1 Reviewed; 411 AA.
AC K9N4V7;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Nucleoprotein {ECO:0000255|HAMAP-Rule:MF_04096};
DE AltName: Full=Nucleocapsid protein {ECO:0000255|HAMAP-Rule:MF_04096};
DE Short=NC {ECO:0000255|HAMAP-Rule:MF_04096};
DE Short=Protein N {ECO:0000255|HAMAP-Rule:MF_04096};
GN Name=N {ECO:0000255|HAMAP-Rule:MF_04096}; ORFNames=6;
OS Middle East respiratory syndrome-related coronavirus (isolate United
OS Kingdom/H123990006/2012) (MERS-CoV) (Betacoronavirus England 1).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Merbecovirus.
OX NCBI_TaxID=1263720;
OH NCBI_TaxID=9838; Camelus dromedarius (Dromedary) (Arabian camel).
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=23078800;
RA Bermingham A., Chand M.A., Brown C.S., Aarons E., Tong C., Langrish C.,
RA Hoschler K., Brown K., Galiano M., Myers R., Pebody R.G., Green H.K.,
RA Boddington N.L., Gopal R., Price N., Newsholme W., Drosten C.,
RA Fouchier R.A., Zambon M.;
RT "Severe respiratory illness caused by a novel coronavirus, in a patient
RT transferred to the United Kingdom from the Middle East, September 2012.";
RL Eurosurveillance 17:20290-20290(2012).
RN [2]
RP ADP-RIBOSYLATION.
RX PubMed=29199039; DOI=10.1016/j.virol.2017.11.020;
RA Grunewald M.E., Fehr A.R., Athmer J., Perlman S.;
RT "The coronavirus nucleocapsid protein is ADP-ribosylated.";
RL Virology 517:62-68(2018).
CC -!- FUNCTION: Packages the positive strand viral genome RNA into a helical
CC ribonucleocapsid (RNP) and plays a fundamental role during virion
CC assembly through its interactions with the viral genome and membrane
CC protein M. Plays an important role in enhancing the efficiency of
CC subgenomic viral RNA transcription as well as viral replication.
CC {ECO:0000255|HAMAP-Rule:MF_04096}.
CC -!- SUBUNIT: Homooligomer. Both monomeric and oligomeric forms interact
CC with RNA. Interacts with protein M. Interacts with NSP3; this
CC interaction serves to tether the genome to the newly translated
CC replicase-transcriptase complex at a very early stage of infection.
CC {ECO:0000255|HAMAP-Rule:MF_04096}.
CC -!- INTERACTION:
CC K9N4V7; Q13283: G3BP1; Xeno; NbExp=5; IntAct=EBI-25592177, EBI-1047359;
CC K9N4V7; P62136: PPP1CA; Xeno; NbExp=2; IntAct=EBI-25592177, EBI-357253;
CC K9N4V7; Q14258: TRIM25; Xeno; NbExp=2; IntAct=EBI-25592177, EBI-2341129;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04096}. Host
CC endoplasmic reticulum-Golgi intermediate compartment
CC {ECO:0000255|HAMAP-Rule:MF_04096}. Host Golgi apparatus
CC {ECO:0000255|HAMAP-Rule:MF_04096}. Note=Located inside the virion,
CC complexed with the viral RNA. Probably associates with ER-derived
CC membranes where it participates in viral RNA synthesis and virus
CC budding. {ECO:0000255|HAMAP-Rule:MF_04096}.
CC -!- PTM: ADP-ribosylated. The ADP-ribosylation is retained in the virion
CC during infection. {ECO:0000255|HAMAP-Rule:MF_04096,
CC ECO:0000269|PubMed:29199039}.
CC -!- PTM: Phosphorylated on serine and threonine residues.
CC {ECO:0000255|HAMAP-Rule:MF_04096}.
CC -!- SIMILARITY: Belongs to the betacoronavirus nucleocapsid protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04096}.
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DR EMBL; KC164505; AFY13314.1; -; Genomic_RNA.
DR PDB; 6KL2; X-ray; 2.63 A; A/B/C/D=39-165.
DR PDB; 6KL5; X-ray; 3.09 A; A/B/C/D=39-165.
DR PDB; 6KL6; X-ray; 2.77 A; A/B/C/D=39-165.
DR PDB; 6LNN; X-ray; 2.63 A; A/B/C/D=39-165.
DR PDB; 6LZ6; X-ray; 2.65 A; A/B/C/D=39-165.
DR PDB; 6LZ8; X-ray; 2.59 A; A/B/C/D=39-165.
DR PDBsum; 6KL2; -.
DR PDBsum; 6KL5; -.
DR PDBsum; 6KL6; -.
DR PDBsum; 6LNN; -.
DR PDBsum; 6LZ6; -.
DR PDBsum; 6LZ8; -.
DR SASBDB; K9N4V7; -.
DR SMR; K9N4V7; -.
DR BioGRID; 4383878; 7.
DR ComplexPortal; CPX-5770; MERS-CoV nucleocapsid complex.
DR IntAct; K9N4V7; 236.
DR Proteomes; UP000139997; Genome.
DR GO; GO:0044172; C:host cell endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0044177; C:host cell Golgi apparatus; IC:ComplexPortal.
DR GO; GO:0019028; C:viral capsid; IC:ComplexPortal.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019074; P:viral RNA genome packaging; IDA:ComplexPortal.
DR CDD; cd21595; CoV_N-CTD; 1.
DR CDD; cd21554; CoV_N-NTD; 1.
DR HAMAP; MF_04096; BETA_CORONA_NCAP; 1.
DR InterPro; IPR044344; N_prot_C_CoV.
DR InterPro; IPR044345; N_prot_N_CoV.
DR InterPro; IPR043505; NCAP_bCoV.
DR InterPro; IPR001218; Nucleocap_CoV.
DR InterPro; IPR037179; Nucleocapsid_C.
DR InterPro; IPR037195; Nucleocapsid_N.
DR Pfam; PF00937; CoV_nucleocap; 1.
DR PIRSF; PIRSF003888; Corona_nucleocap; 1.
DR SUPFAM; SSF103068; SSF103068; 1.
DR SUPFAM; SSF110304; SSF110304; 1.
DR PROSITE; PS51929; COV_N_CTD; 1.
DR PROSITE; PS51928; COV_N_NTD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Host Golgi apparatus; Phosphoprotein;
KW Ribonucleoprotein; RNA-binding; Transcription; Transcription regulation;
KW Viral nucleoprotein; Virion.
FT CHAIN 1..411
FT /note="Nucleoprotein"
FT /id="PRO_0000422434"
FT DOMAIN 39..164
FT /note="CoV N NTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01276"
FT DOMAIN 239..362
FT /note="CoV N CTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01277"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 33..175
FT /note="RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT REGION 156..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..360
FT /note="Dimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT REGION 361..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 133
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT MOD_RES 148
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT MOD_RES 396
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:6KL2"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:6LZ8"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:6LZ8"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:6LZ8"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:6LZ8"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:6LZ8"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:6LZ8"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:6LZ8"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:6LZ8"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:6KL2"
SQ SEQUENCE 411 AA; 44857 MW; 8AF44237C8308608 CRC64;
MASPAAPRAV SFADNNDITN TNLSRGRGRN PKPRAAPNNT VSWYTGLTQH GKVPLTFPPG
QGVPLNANST PAQNAGYWRR QDRKINTGNG IKQLAPRWYF YYTGTGPEAA LPFRAVKDGI
VWVHEDGATD APSTFGTRNP NNDSAIVTQF APGTKLPKNF HIEGTGGNSQ SSSRASSVSR
NSSRSSSQGS RSGNSTRGTS PGPSGIGAVG GDLLYLDLLN RLQALESGKV KQSQPKVITK
KDAAAAKNKM RHKRTSTKSF NMVQAFGLRG PGDLQGNFGD LQLNKLGTED PRWPQIAELA
PTASAFMGMS QFKLTHQNND DHGNPVYFLR YSGAIKLDPK NPNYNKWLEL LEQNIDAYKT
FPKKEKKQKA PKEESTDQMS EPPKEHRVQG TQRTRTRPSV QPGPMIDVNT D
