CAPSD_NVN68
ID CAPSD_NVN68 Reviewed; 530 AA.
AC Q83884;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Capsid protein VP1;
DE Short=CP;
DE AltName: Full=p59;
DE Contains:
DE RecName: Full=Soluble capsid protein;
DE AltName: Full=Protein 30k;
DE Short=p30;
GN ORFNames=ORF2;
OS Norwalk virus (strain GI/Human/United States/Norwalk/1968)
OS (Hu/NV/NV/1968/US).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Caliciviridae; Norovirus.
OX NCBI_TaxID=524364;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8391187; DOI=10.1006/viro.1993.1345;
RA Jiang X., Wang M., Wang K., Estes M.K.;
RT "Sequence and genomic organization of Norwalk virus.";
RL Virology 195:51-61(1993).
RN [2]
RP CLEAVAGE.
RX PubMed=7853506; DOI=10.1128/jvi.69.3.1693-1698.1995;
RA Hardy M.E., White L.J., Ball J.M., Estes M.K.;
RT "Specific proteolytic cleavage of recombinant Norwalk virus capsid
RT protein.";
RL J. Virol. 69:1693-1698(1995).
RN [3]
RP CELL-RECEPTOR BINDING.
RX PubMed=8794293; DOI=10.1128/jvi.70.10.6589-6597.1996;
RA White L.J., Ball J.M., Hardy M.E., Tanaka T.N., Kitamoto N., Estes M.K.;
RT "Attachment and entry of recombinant Norwalk virus capsids to cultured
RT human and animal cell lines.";
RL J. Virol. 70:6589-6597(1996).
RN [4]
RP CAPSID ASSEMBLY.
RX PubMed=9311906; DOI=10.1128/jvi.71.10.8066-8072.1997;
RA White L.J., Hardy M.E., Estes M.K.;
RT "Biochemical characterization of a smaller form of recombinant Norwalk
RT virus capsids assembled in insect cells.";
RL J. Virol. 71:8066-8072(1997).
RN [5]
RP CELL-RECEPTOR BINDING.
RX PubMed=12055602; DOI=10.1053/gast.2002.33661;
RA Marionneau S., Ruvoen N., Le Moullac-Vaidye B., Clement M.,
RA Cailleau-Thomas A., Ruiz-Palacois G., Huang P., Jiang X., Le Pendu J.;
RT "Norwalk virus binds to histo-blood group antigens present on
RT gastroduodenal epithelial cells of secretor individuals.";
RL Gastroenterology 122:1967-1977(2002).
RN [6]
RP STABILIZATION BY VP2.
RX PubMed=14557646; DOI=10.1128/jvi.77.21.11603-11615.2003;
RA Bertolotti-Ciarlet A., Crawford S.E., Hutson A.M., Estes M.K.;
RT "The 3' end of Norwalk virus mRNA contains determinants that regulate the
RT expression and stability of the viral capsid protein VP1: a novel function
RT for the VP2 protein.";
RL J. Virol. 77:11603-11615(2003).
RN [7]
RP CELL-RECEPTOR BINDING.
RX PubMed=12825167; DOI=10.1086/375742;
RA Huang P., Farkas T., Marionneau S., Zhong W., Ruvoen-Clouet N.,
RA Morrow A.L., Altaye M., Pickering L.K., Newburg D.S., LePendu J., Jiang X.;
RT "Noroviruses bind to human ABO, Lewis, and secretor histo-blood group
RT antigens: identification of 4 distinct strain-specific patterns.";
RL J. Infect. Dis. 188:19-31(2003).
RN [8]
RP FUNCTION.
RX PubMed=16840313; DOI=10.1128/jvi.00233-06;
RA Tan M., Meller J., Jiang X.;
RT "C-terminal arginine cluster is essential for receptor binding of norovirus
RT capsid protein.";
RL J. Virol. 80:7322-7331(2006).
RN [9]
RP REVIEW.
RX PubMed=16168575; DOI=10.1016/j.femsle.2005.08.031;
RA Hardy M.E.;
RT "Norovirus protein structure and function.";
RL FEMS Microbiol. Lett. 253:1-8(2005).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS).
RX PubMed=10514371; DOI=10.1126/science.286.5438.287;
RA Prasad B.V.V., Hardy M.E., Dokland T., Bella J., Rossmann M.G., Estes M.K.;
RT "X-ray crystallographic structure of the Norwalk virus capsid.";
RL Science 286:287-290(1999).
CC -!- FUNCTION: Capsid protein self assembles to form an icosahedral capsid
CC with a T=3 symmetry, about 38 nm in diameter, and consisting of 180
CC capsid proteins. A smaller form of capsid with a diameter of 23 nm
CC might be capsid proteins assembled as icosahedron with T=1 symmetry.
CC The capsid encapsulate the genomic RNA and VP2 proteins. Attaches
CC virion to target cells by binding histo-blood group antigens present on
CC gastroduodenal epithelial cells. {ECO:0000269|PubMed:16840313}.
CC -!- FUNCTION: Soluble capsid protein may play a role in viral
CC immunoevasion. {ECO:0000269|PubMed:16840313}.
CC -!- SUBUNIT: Homodimerizes, then multimerizes. Binds to histo-blood group
CC antigens at surface of target cells.
CC -!- INTERACTION:
CC Q83884; Q83884: ORF2; NbExp=2; IntAct=EBI-15713903, EBI-15713903;
CC -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm.
CC -!- DOMAIN: The shell domain (S domain) contains elements essential for the
CC formation of the icosahedron. The Protruding domain (P domain) is
CC divided into sub-domains P1 and P2. P domain interacts in dimeric
CC contacts that increase the stability of the capsid and form the
CC protrusions on the virion. An hypervariable region in P2 is thought to
CC play an important role in receptor binding and immune reactivity.
CC -!- PTM: May be cleaved by host protease to generate soluble capsid
CC protein. Assembled capsid cannot be cleaved.
CC {ECO:0000269|PubMed:7853506}.
CC -!- SIMILARITY: Belongs to the caliciviridae capsid protein family.
CC {ECO:0000305}.
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DR EMBL; M87661; AAB50466.2; -; Genomic_RNA.
DR PIR; B37471; B37471.
DR RefSeq; NP_056821.2; NC_001959.2.
DR PDB; 1IHM; X-ray; 3.40 A; A/B/C=1-530.
DR PDB; 2ZL5; X-ray; 1.47 A; A/B=225-518.
DR PDB; 2ZL6; X-ray; 1.43 A; A/B=225-519.
DR PDB; 2ZL7; X-ray; 1.35 A; A/B=225-519.
DR PDB; 3BY1; X-ray; 2.69 A; A=218-530.
DR PDB; 3BY2; X-ray; 2.60 A; A=218-522.
DR PDB; 3D26; X-ray; 2.30 A; A/B=230-530.
DR PDB; 5KW9; X-ray; 2.30 A; A=225-518.
DR PDB; 5N7M; X-ray; 1.73 A; A/B=225-519.
DR PDB; 6CRJ; EM; 8.00 A; A/B/C=10-221.
DR PDB; 6H6Y; X-ray; 1.58 A; A/B/C/D=227-518.
DR PDB; 6H6Z; X-ray; 2.08 A; A/B=227-518.
DR PDB; 6H70; X-ray; 1.83 A; A/B=227-518.
DR PDB; 6H71; X-ray; 2.31 A; A/B=227-518.
DR PDB; 6H72; X-ray; 2.30 A; A/B=227-518.
DR PDB; 6OUT; EM; 2.60 A; A/B/C=9-520.
DR PDB; 7KJP; EM; 3.86 A; A/B/C=1-530.
DR PDBsum; 1IHM; -.
DR PDBsum; 2ZL5; -.
DR PDBsum; 2ZL6; -.
DR PDBsum; 2ZL7; -.
DR PDBsum; 3BY1; -.
DR PDBsum; 3BY2; -.
DR PDBsum; 3D26; -.
DR PDBsum; 5KW9; -.
DR PDBsum; 5N7M; -.
DR PDBsum; 6CRJ; -.
DR PDBsum; 6H6Y; -.
DR PDBsum; 6H6Z; -.
DR PDBsum; 6H70; -.
DR PDBsum; 6H71; -.
DR PDBsum; 6H72; -.
DR PDBsum; 6OUT; -.
DR PDBsum; 7KJP; -.
DR SMR; Q83884; -.
DR UniLectin; Q83884; -.
DR PRIDE; Q83884; -.
DR ABCD; Q83884; 4 sequenced antibodies.
DR GeneID; 1491972; -.
DR KEGG; vg:1491972; -.
DR EvolutionaryTrace; Q83884; -.
DR Proteomes; UP000000826; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0039617; C:T=3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR CDD; cd00205; rhv_like; 1.
DR Gene3D; 2.60.120.20; -; 1.
DR InterPro; IPR004005; Calicivirus_coat.
DR InterPro; IPR013643; Calicivirus_coat_C.
DR InterPro; IPR033703; Rhv-like.
DR InterPro; IPR029053; Viral_coat.
DR Pfam; PF00915; Calici_coat; 1.
DR Pfam; PF08435; Calici_coat_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Host cytoplasm; Reference proteome;
KW T=3 icosahedral capsid protein; Virion.
FT CHAIN 1..530
FT /note="Capsid protein VP1"
FT /id="PRO_0000341626"
FT CHAIN 228..530
FT /note="Soluble capsid protein"
FT /id="PRO_0000341627"
FT REGION 1..225
FT /note="Shell domain"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..530
FT /note="Protruding domain"
FT REGION 226..278
FT /note="P1 su-bdomain 1"
FT REGION 279..405
FT /note="P2 sub-domain"
FT REGION 406..530
FT /note="P1 sub-domain 2"
FT SITE 227..228
FT /note="Cleavage; by host"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:6OUT"
FT TURN 39..45
FT /evidence="ECO:0007829|PDB:6OUT"
FT TURN 54..58
FT /evidence="ECO:0007829|PDB:6OUT"
FT STRAND 61..70
FT /evidence="ECO:0007829|PDB:6OUT"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:6OUT"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:6OUT"
FT HELIX 91..96
FT /evidence="ECO:0007829|PDB:6OUT"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:6OUT"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:6OUT"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:6OUT"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:6OUT"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:6OUT"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:6OUT"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:6OUT"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:6OUT"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:6OUT"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:6OUT"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:6OUT"
FT STRAND 202..210
FT /evidence="ECO:0007829|PDB:6OUT"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:6OUT"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:2ZL7"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:2ZL7"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:2ZL7"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:2ZL7"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:2ZL7"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:2ZL7"
FT STRAND 296..302
FT /evidence="ECO:0007829|PDB:2ZL7"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:6H6Y"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:2ZL7"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:2ZL7"
FT STRAND 325..333
FT /evidence="ECO:0007829|PDB:2ZL7"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:6H71"
FT STRAND 341..345
FT /evidence="ECO:0007829|PDB:2ZL7"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:6H6Y"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:2ZL7"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:2ZL7"
FT STRAND 366..377
FT /evidence="ECO:0007829|PDB:2ZL7"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:2ZL7"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:2ZL7"
FT HELIX 400..403
FT /evidence="ECO:0007829|PDB:6H72"
FT STRAND 416..425
FT /evidence="ECO:0007829|PDB:2ZL7"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:2ZL7"
FT STRAND 431..437
FT /evidence="ECO:0007829|PDB:2ZL7"
FT HELIX 439..448
FT /evidence="ECO:0007829|PDB:2ZL7"
FT STRAND 455..462
FT /evidence="ECO:0007829|PDB:2ZL7"
FT TURN 464..466
FT /evidence="ECO:0007829|PDB:2ZL7"
FT STRAND 469..476
FT /evidence="ECO:0007829|PDB:2ZL7"
FT TURN 477..479
FT /evidence="ECO:0007829|PDB:2ZL7"
FT STRAND 480..483
FT /evidence="ECO:0007829|PDB:2ZL7"
FT TURN 487..489
FT /evidence="ECO:0007829|PDB:2ZL6"
FT HELIX 492..494
FT /evidence="ECO:0007829|PDB:2ZL7"
FT STRAND 500..507
FT /evidence="ECO:0007829|PDB:2ZL7"
SQ SEQUENCE 530 AA; 56589 MW; 7AEF61A8F66D139C CRC64;
MMMASKDATS SVDGASGAGQ LVPEVNASDP LAMDPVAGSS TAVATAGQVN PIDPWIINNF
VQAPQGEFTI SPNNTPGDVL FDLSLGPHLN PFLLHLSQMY NGWVGNMRVR IMLAGNAFTA
GKIIVSCIPP GFGSHNLTIA QATLFPHVIA DVRTLDPIEV PLEDVRNVLF HNNDRNQQTM
RLVCMLYTPL RTGGGTGDSF VVAGRVMTCP SPDFNFLFLV PPTVEQKTRP FTLPNLPLSS
LSNSRAPLPI SSMGISPDNV QSVQFQNGRC TLDGRLVGTT PVSLSHVAKI RGTSNGTVIN
LTELDGTPFH PFEGPAPIGF PDLGGCDWHI NMTQFGHSSQ TQYDVDTTPD TFVPHLGSIQ
ANGIGSGNYV GVLSWISPPS HPSGSQVDLW KIPNYGSSIT EATHLAPSVY PPGFGEVLVF
FMSKMPGPGA YNLPCLLPQE YISHLASEQA PTVGEAALLH YVDPDTGRNL GEFKAYPDGF
LTCVPNGASS GPQQLPINGV FVFVSWVSRF YQLKPVGTAS SARGRLGLRR
