ID   CAPSD_LORDV             Reviewed;         539 AA.
AC   P54635;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   07-OCT-2020, entry version 68.
DE   RecName: Full=Capsid protein;
DE            Short=CP;
DE   AltName: Full=VP1;
DE   Contains:
DE     RecName: Full=Soluble capsid protein;
GN   ORFNames=ORF2;
OS   Lordsdale virus (strain GII/Human/United Kingdom/Lordsdale/1993) (Human
OS   enteric calicivirus) (Hu/NV/LD/1993/UK).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Caliciviridae; Norovirus.
OX   NCBI_TaxID=82658;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=7561776; DOI=10.1099/0022-1317-76-9-2349;
RA   Dingle K.E., Lambden P.R., Caul E.O., Clarke I.N.;
RT   "Human enteric Caliciviridae: the complete genome sequence and expression
RT   of virus-like particles from a genetic group II small round structured
RT   virus.";
RL   J. Gen. Virol. 76:2349-2355(1995).
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 (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Soluble capsid protein may play a role in viral
CC       immunoevasion. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimerizes, then multimerizes. Binds to histo-blood group
CC       antigens at surface of target cells (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm {ECO:0000250}.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the caliciviridae capsid protein family.
CC       {ECO:0000305}.
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DR   EMBL; X86557; CAA60255.1; -; Genomic_RNA.
DR   SMR; P54635; -.
DR   Proteomes; UP000007767; 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   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   3: Inferred from homology;
KW   Capsid protein; Host cytoplasm; T=3 icosahedral capsid protein; Virion.
FT   CHAIN           1..539
FT                   /note="Capsid protein"
FT                   /id="PRO_0000100118"
FT   CHAIN           223..539
FT                   /note="Soluble capsid protein"
FT                   /id="PRO_0000341982"
FT   REGION          1..221
FT                   /note="Shell domain"
FT                   /evidence="ECO:0000250"
FT   REGION          222..539
FT                   /note="Protruding domain"
FT                   /evidence="ECO:0000250"
FT   REGION          222..274
FT                   /note="P1 su-bdomain 1"
FT                   /evidence="ECO:0000250"
FT   REGION          275..417
FT                   /note="P2 sub-domain"
FT                   /evidence="ECO:0000250"
FT   REGION          418..539
FT                   /note="P1 sub-domain 2"
FT                   /evidence="ECO:0000250"
FT   SITE            223..224
FT                   /note="Cleavage; by host"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   539 AA;  58775 MW;  5E5C63E7F2C5FD21 CRC64;
     MKMASNDANP SDGSAANLVP EVNNEVMALE PVVGAAIAAP VAGQQNVIDP WIRNNFVQAP
     GGEFTVSPRN APGEILWSAP LGPDLNPYLS HLSRMYNGYA GGFEVQVILA GNAFTAGKVI
     FAAVPPNFPT EGLSPSQVTM FPHIIVDVRQ LEPVLIPLPD VRNNFYHYNQ ANDSTLKLIA
     MLYTPLRANN AGDDVFTVSC RVLTRPSPDF DFIFLVPPTV ESRTKPFTVP VLTVEEMSNS
     RFPIPLEKLY TGPSSAFVVQ PQNGRCTTDG VLLGTTQLSA VNICNFRGDV THIAGSHDYT
     MNLASQNWSN YDPTEEIPAP LGTPDFVGKI QGLLTQTTRA DGSTRAHKAT VSTGSVHFTP
     KLGSVQFTTD TNNDFQAGQN TKFTPVGVIQ DGDHHQNEPQ QWSLPNYSGR TGHNVHLAPA
     VAPTFPGEQL LFFRSTMPGC SGYPNMNLDC LLPQEWVLHF YQEAAPAQSD VALLRFVNPD
     TGRVLFECKL HKSGYITVAH TGPYDLVLPP NGYFRFDSWV NQFYTLAPMG NGTGRRRAL