ID   CAPSD_SOUV3             Reviewed;         546 AA.
AC   Q04542;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   08-NOV-2023, entry version 74.
DE   RecName: Full=Capsid protein VP1;
DE            Short=CP;
DE   Contains:
DE     RecName: Full=Soluble capsid protein;
GN   ORFNames=ORF2;
OS   Southampton virus (strain GI/Human/United Kingdom/Southampton/1991) (SHV)
OS   (Hu/NV/SHV/1991/UK).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Caliciviridae; Norovirus; Norwalk virus.
OX   NCBI_TaxID=37129;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8380940; DOI=10.1126/science.8380940;
RA   Lambden P.R., Caul E.O., Ashley C.R., Clarke I.N.;
RT   "Sequence and genome organization of a human small round-structured
RT   (Norwalk-like) virus.";
RL   Science 259:516-519(1993).
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; L07418; AAA92984.1; -; Genomic_RNA.
DR   PIR; B37491; B37491.
DR   SMR; Q04542; -.
DR   Proteomes; UP000007226; 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   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   3: Inferred from homology;
KW   Capsid protein; Host cytoplasm; T=3 icosahedral capsid protein; Virion.
FT   CHAIN           1..546
FT                   /note="Capsid protein VP1"
FT                   /id="PRO_0000100119"
FT   CHAIN           228..546
FT                   /note="Soluble capsid protein"
FT                   /id="PRO_0000341983"
FT   REGION          1..226
FT                   /note="Shell domain"
FT                   /evidence="ECO:0000250"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          227..545
FT                   /note="Protruding domain"
FT                   /evidence="ECO:0000250"
FT   REGION          227..279
FT                   /note="P1 su-bdomain 1"
FT                   /evidence="ECO:0000250"
FT   REGION          280..416
FT                   /note="P2 sub-domain"
FT                   /evidence="ECO:0000250"
FT   REGION          417..546
FT                   /note="P1 sub-domain 2"
FT                   /evidence="ECO:0000250"
FT   SITE            228..229
FT                   /note="Cleavage; by host"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   546 AA;  58774 MW;  C82B2A85AD4B05EA CRC64;
     MMMASKDAPQ SADGASGAGQ LVPEVNTADP LPMEPVAGPT TAVATAGQVN MIDPWIVNNF
     VQSPQGEFTI SPNNTPGDIL FDLQLGPHLN PFLSHLSQMY NGWVGNMRVR ILLAGNAFSA
     GKIIVCCVPP GFTSSSLTIA QATLFPHVIA DVRTLEPIEM PLEDVRNVLY HTNDNQPTMR
     LVCMLYTPLR TGGGSGNSDS FVVAGRVLTA PSSDFSFLFL VPPTIEQKTR AFTVPNIPLQ
     TLSNSRFPSL IQGMILSPDA SQVVQFQNGR CLIDGQLLGT TPATSGQLFR VRGKINQGAR
     TLNLTEVDGK PFMAFDSPAP VGFPDFGKCD WHMRISKTPN NTGSGDPMRS VSVQTNVQGF
     VPHLGSIQFD EVFNHPTGDY IGTIEWISQP STPPGTDINL WEIPDYGSSL SQAANLAPPV
     FPPGFGEALV YFVSAFPGPN NRSAPNDVPC LLPQEYITHF VSEQAPTMGD AALLHYVDPD
     TNRNLGEFKL YPGGYLTCVP NGVGAGPQQL PLNGVFLFVS WVSRFYQLKP VGTASTARGR
     LGVRRI
//