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 10-APR-2019, entry version 90. 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; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage; OC 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; 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; RA White L.J., Ball J.M., Hardy M.E., Tanaka T.N., Kitamoto N., RA 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; 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 RT the expression and stability of the viral capsid protein VP1: a novel RT function 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., RA 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 RT norovirus 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., RA 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 CC capsid with a T=3 symmetry, about 38 nm in diameter, and CC consisting of 180 capsid proteins. A smaller form of capsid with a CC diameter of 23 nm might be capsid proteins assembled as CC icosahedron with T=1 symmetry. The capsid encapsulate the genomic CC RNA and VP2 proteins. Attaches virion to target cells by binding CC histo-blood group antigens present on gastroduodenal epithelial CC 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 CC group antigens at surface of target cells. CC -!- INTERACTION: CC Self; NbExp=2; IntAct=EBI-15713903, EBI-15713903; CC -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm. CC -!- DOMAIN: The shell domain (S domain) contains elements essential CC for the formation of the icosahedron. The Protruding domain (P CC domain) is divided into sub-domains P1 and P2. P domain interacts CC in dimeric contacts that increase the stability of the capsid and CC form the protrusions on the virion. An hypervariable region in P2 CC is thought to play an important role in receptor binding and CC 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; 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 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; 6H6Y; -. DR PDBsum; 6H6Z; -. DR PDBsum; 6H70; -. DR PDBsum; 6H71; -. DR PDBsum; 6H72; -. DR ProteinModelPortal; Q83884; -. DR SMR; Q83884; -. DR UniLectin; Q83884; -. DR PRIDE; Q83884; -. 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; Complete proteome; Host cytoplasm; KW Reference proteome; T=3 icosahedral capsid protein; Virion. FT CHAIN 1 530 Capsid protein VP1. FT /FTId=PRO_0000341626. FT CHAIN 228 530 Soluble capsid protein. FT /FTId=PRO_0000341627. FT REGION 1 225 Shell domain. FT REGION 226 530 Protruding domain. FT REGION 226 278 P1 su-bdomain 1. FT REGION 279 405 P2 sub-domain. FT REGION 406 530 P1 sub-domain 2. FT SITE 227 228 Cleavage; by host. FT HELIX 14 16 {ECO:0000244|PDB:1IHM}. FT HELIX 42 44 {ECO:0000244|PDB:1IHM}. FT TURN 54 58 {ECO:0000244|PDB:1IHM}. FT STRAND 61 70 {ECO:0000244|PDB:1IHM}. FT STRAND 79 84 {ECO:0000244|PDB:1IHM}. FT HELIX 87 89 {ECO:0000244|PDB:1IHM}. FT HELIX 91 97 {ECO:0000244|PDB:1IHM}. FT STRAND 100 104 {ECO:0000244|PDB:1IHM}. FT STRAND 107 114 {ECO:0000244|PDB:1IHM}. FT STRAND 117 120 {ECO:0000244|PDB:1IHM}. FT STRAND 122 128 {ECO:0000244|PDB:1IHM}. FT HELIX 139 142 {ECO:0000244|PDB:1IHM}. FT STRAND 145 151 {ECO:0000244|PDB:1IHM}. FT STRAND 158 162 {ECO:0000244|PDB:1IHM}. FT STRAND 167 169 {ECO:0000244|PDB:1IHM}. FT STRAND 171 173 {ECO:0000244|PDB:1IHM}. FT STRAND 181 186 {ECO:0000244|PDB:1IHM}. FT STRAND 202 210 {ECO:0000244|PDB:1IHM}. FT HELIX 238 240 {ECO:0000244|PDB:2ZL7}. FT STRAND 244 247 {ECO:0000244|PDB:2ZL7}. FT STRAND 252 254 {ECO:0000244|PDB:2ZL7}. FT STRAND 266 268 {ECO:0000244|PDB:2ZL7}. FT HELIX 284 286 {ECO:0000244|PDB:2ZL7}. FT STRAND 289 294 {ECO:0000244|PDB:2ZL7}. FT STRAND 296 302 {ECO:0000244|PDB:2ZL7}. FT STRAND 306 308 {ECO:0000244|PDB:6H6Y}. FT HELIX 311 313 {ECO:0000244|PDB:2ZL7}. FT STRAND 315 317 {ECO:0000244|PDB:2ZL7}. FT STRAND 325 333 {ECO:0000244|PDB:2ZL7}. FT STRAND 335 337 {ECO:0000244|PDB:6H71}. FT STRAND 341 345 {ECO:0000244|PDB:2ZL7}. FT STRAND 347 349 {ECO:0000244|PDB:6H6Y}. FT HELIX 354 356 {ECO:0000244|PDB:2ZL7}. FT STRAND 358 360 {ECO:0000244|PDB:2ZL7}. FT STRAND 366 377 {ECO:0000244|PDB:2ZL7}. FT STRAND 380 382 {ECO:0000244|PDB:2ZL7}. FT STRAND 396 398 {ECO:0000244|PDB:2ZL7}. FT HELIX 400 403 {ECO:0000244|PDB:6H72}. FT STRAND 416 425 {ECO:0000244|PDB:2ZL7}. FT STRAND 427 429 {ECO:0000244|PDB:2ZL7}. FT STRAND 431 437 {ECO:0000244|PDB:2ZL7}. FT HELIX 439 448 {ECO:0000244|PDB:2ZL7}. FT STRAND 455 462 {ECO:0000244|PDB:2ZL7}. FT TURN 464 466 {ECO:0000244|PDB:2ZL7}. FT STRAND 469 476 {ECO:0000244|PDB:2ZL7}. FT TURN 477 479 {ECO:0000244|PDB:2ZL7}. FT STRAND 480 483 {ECO:0000244|PDB:2ZL7}. FT TURN 487 489 {ECO:0000244|PDB:2ZL6}. FT HELIX 492 494 {ECO:0000244|PDB:2ZL7}. FT STRAND 500 507 {ECO:0000244|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 //