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 24-JAN-2024, entry version 109. 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 Norovirus (strain Human/NoV/United States/Norwalk/1968/GI) OS (Hu/NV/NV/1968/US). OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes; OC Picornavirales; Caliciviridae; Norovirus; Norwalk virus. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-20199; -. DR EMDB; EMD-20205; -. DR EMDB; EMD-22897; -. DR SMR; Q83884; -. DR UniLectin; Q83884; -. DR ABCD; Q83884; 4 sequenced antibodies. DR GeneID; 1491972; -. DR KEGG; vg:1491972; -. DR EvolutionaryTrace; Q83884; -. DR Proteomes; UP000000826; Segment. 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 Gene3D; 2.40.30.120; Positive stranded ssRNA viruses; 1. DR Gene3D; 2.40.510.10; Positive stranded ssRNA viruses; 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. DR SUPFAM; SSF88633; Positive stranded ssRNA viruses; 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 //