ID   CAPSD_FCVC6             Reviewed;         668 AA.
AC   P27404;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   08-NOV-2023, entry version 80.
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 CFI/68 FIV) (FCV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Caliciviridae; Vesivirus; Feline calicivirus.
OX   NCBI_TaxID=11979;
OH   NCBI_TaxID=9681; Felidae (cat family).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=1716692; DOI=10.1128/jvi.65.10.5440-5447.1991;
RA   Neill J.D., Reardon I.M., Heinrikson R.L.;
RT   "Nucleotide sequence and expression of the capsid protein gene of feline
RT   calicivirus.";
RL   J. Virol. 65:5440-5447(1991).
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 (By similarity). {ECO:0000250}.
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; M32819; AAA42925.1; -; Genomic_RNA.
DR   EMBL; U13992; AAC13993.1; -; Genomic_RNA.
DR   PIR; A40507; VCWWFF.
DR   SMR; P27404; -.
DR   Proteomes; UP000008667; 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; Direct protein sequencing; Host cytoplasm;
KW   T=3 icosahedral capsid protein; Virion.
FT   PROPEP          1..124
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036874"
FT   CHAIN           125..668
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036875"
FT   CHAIN           ?465..668
FT                   /note="Protein 40k"
FT                   /id="PRO_0000341979"
FT   SITE            124..125
FT                   /note="Cleavage; by calicivirin"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   668 AA;  73550 MW;  9E52312108D4D441 CRC64;
     MCSTCANVLK YYDWDPHIKL VINPNKFLHV GFCDNPLMCC YPELLPEFGT MWDCDQSPLQ
     VYLESILGDD EWSSTHEAID PVVPPMHWDE AGKIFQPHPG VLMHHLICKV AEGWDPNLPL
     FRLEADDGSI TTPEQGTMVG GVIAEPNAQM STAADMATGK SVDSEWEAFF SFHTSVNWST
     SETQGKILFK QSLGPLLNPY LTHLAKLYVA WSGSVDVRFS ISGSGVFGGK LAAIVVPPGI
     DPVQSTSMLQ YPHVLFDARQ VEPVIFSIPD LRSTLYHLMS DTDTTSLVIM VYNDLINPYA
     NDSNSSGCIV TVETKPGPDF KFHLLKPPGS MLTHGSIPSD LIPKSSSLWI GNRFWSDITD
     FVIRPFVFQA NRHFDFNQET AGWSTPRFRP ITITISVKES AKLGIGVATD YIVPGIPDGW
     PDTTIPGELV PVGDYAITNG TNNDITTAAQ YDAATEIRNN TNFRGMYICG SLQRAWGDKK
     ISNTAFITTG TVDGAKLIPS NTIDQTKIAV FQDTHANKHV QTSDDTLALL GYTGIGEEAI
     GADRDRVVRI SVLPERGARG GNHPIFHKNS IKLGYVIRSI DVFNSQILHT SRQLSLNHYL
     LSPDSFAVYR IIDSNGSWFD IGIDNDGFSF VGVSSIGKLE FPLTASYMGI QLAKIRLASN
     IRSVMTKL
//