ID   CAPSD_FCVF4             Reviewed;         668 AA.
AC   P27405;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   08-NOV-2023, entry version 74.
DE   RecName: Full=Capsid protein;
DE   AltName: Full=Coat protein;
DE            Short=CP;
DE   AltName: Full=VP1;
DE   Contains:
DE     RecName: Full=Protein 40k;
DE   Flags: Precursor;
GN   ORFNames=ORF2;
OS   Feline calicivirus (strain Japanese F4) (FCV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Caliciviridae; Vesivirus; Feline calicivirus.
OX   NCBI_TaxID=11980;
OH   NCBI_TaxID=9681; Felidae (cat family).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1853578; DOI=10.1016/0042-6822(91)91016-a;
RA   Tohya Y., Taniguchi Y., Takahashi E., Utagawa E., Takeda N., Miyamura K.,
RA   Yamazaki S., Mikami T.;
RT   "Sequence analysis of the 3'-end of feline calicivirus genome.";
RL   Virology 183:810-814(1991).
RN   [2]
RP   INTERACTION WITH HOST F11R.
RX   PubMed=16611908; DOI=10.1128/jvi.80.9.4482-4490.2006;
RA   Makino A., Shimojima M., Miyazawa T., Kato K., Tohya Y., Akashi H.;
RT   "Junctional adhesion molecule 1 is a functional receptor for feline
RT   calicivirus.";
RL   J. Virol. 80:4482-4490(2006).
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 to feline junctional adhesion
CC       molecule A (F11R) and/or to alpha-2,6-linked sialic acid. Once
CC       attached, the virion is endocytosed. Acidification of the endosome
CC       induces conformational change of capsid protein thereby injecting virus
CC       genomic RNA into host cytoplasm (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimerizes, then multimerizes. May bind to VP3 and Vpg
CC       proteins. Binds to alpha-2,6-linked sialic acid at surface of target
CC       cells. Interacts with host F11R. {ECO:0000269|PubMed:16611908}.
CC   -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm {ECO:0000250}.
CC   -!- PTM: Cleaved by virus calcivirin to produce mature capsid protein.
CC       {ECO:0000250}.
CC   -!- PTM: Cleaved by host caspase-2 and caspase-6 to generate protein p40.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the caliciviridae capsid protein family.
CC       {ECO:0000305}.
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DR   EMBL; D90357; BAA14371.1; -; Genomic_RNA.
DR   PIR; B40481; VCWWFC.
DR   SMR; P27405; -.
DR   Proteomes; UP000008668; 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; IPR033703; Rhv-like.
DR   InterPro; IPR029053; Viral_coat.
DR   Pfam; PF00915; Calici_coat; 1.
DR   SUPFAM; SSF88633; Positive stranded ssRNA viruses; 1.
PE   1: Evidence at protein level;
KW   Capsid protein; Host cytoplasm; T=3 icosahedral capsid protein; Virion.
FT   PROPEP          1..124
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036876"
FT   CHAIN           125..668
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036877"
FT   CHAIN           ?465..668
FT                   /note="Protein 40k"
FT                   /id="PRO_0000341980"
FT   SITE            124..125
FT                   /note="Cleavage; by calicivirin"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   668 AA;  73589 MW;  85BBDCB85804E503 CRC64;
     MCSTCANVLK YYDWDPHFRL IINPNKFLPI GFCDNPLMCC YPDLLPEFGT VWDCDQSPLQ
     IYLESILGDD EWASTHEAID PSVPPMHWDS AGKIFQPHPG VLMHHLIGEV AKAWDPNLPL
     FRLEADDGSI TTPEQGTAVG GVIAEPSAQM STAADMASGK SVDSEWEAFF SFHTSVNWST
     SETQGKILFK QSLGPLLNPY LEHLSKLYVA WSGSIEVRFS ISGSGVFGGK LAAIVVPPGV
     DPVQSTSMLQ YPHVLFDARQ VEPVIFTIPD LRSTLYHVMS DTDTTSLVIM VYNDLINPYA
     NDSNSSGCIV TVETKPGPDF KFHLLKPPGS VLTHGSIPSD LIPKSSSLWI GNRYWTDITD
     FVIRPFVFQA NRHFDFNQET AGWSTPRFRP ITITISEKNG SKLGIGVATD YIIPGIPDGW
     PDTTIADKLI PAGDYSITTG EGNDIKTAQA YDTAAVVKNT TNFRGMYICG SLQRAWGDKK
     ISNTAFITTA IRDGNEIKPS NTIDMTKLAV YQDTHVEQEV QTSDDTLALL GYTGIGEEAI
     GSNRDRVVRI SVLPEAGARG GNHPIFYKNS IKLGYVIRSI DVFNSQILHT SRQLSLNHYL
     LPPDSFAVYR IIDSNGSWFD IGIDSEGFSF VGVSDIGKLE FPLSASYMGI QLAKIRLASN
     IRSRMTKL
//