CAPSD_FCVUR
ID CAPSD_FCVUR Reviewed; 668 AA.
AC Q66915;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 02-DEC-2020, entry version 81.
DE RecName: Full=Capsid protein;
DE AltName: Full=Coat protein;
DE Short=CP;
DE Contains:
DE RecName: Full=Protein 40k;
DE Flags: Precursor;
GN ORFNames=ORF2;
OS Feline calicivirus (strain Cat/United States/Urbana/1960) (FCV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Caliciviridae; Vesivirus.
OX NCBI_TaxID=292349;
OH NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=7618275; DOI=10.1006/viro.1995.1354;
RA Sosnovtsev S.V., Green K.Y.;
RT "RNA transcripts derived from a cloned full-length copy of the feline
RT calicivirus genome do not require VpG for infectivity.";
RL Virology 210:383-390(1995).
RN [2]
RP CLEAVAGE, AND MUTAGENESIS OF GLU-124 AND ALA-125.
RX PubMed=9525628; DOI=10.1128/jvi.72.4.3051-3059.1998;
RA Sosnovtsev S.V., Sosnovtseva S.A., Green K.Y.;
RT "Cleavage of the feline calicivirus capsid precursor is mediated by a
RT virus-encoded proteinase.";
RL J. Virol. 72:3051-3059(1998).
RN [3]
RP CHARACTERIZATION.
RX PubMed=10515271; DOI=10.1016/s0378-1135(99)00089-9;
RA Geissler K., Parrish C.R., Schneider K., Truyen U.;
RT "Feline calicivirus capsid protein expression and self-assembly in cultured
RT feline cells.";
RL Vet. Microbiol. 69:63-66(1999).
RN [4]
RP INTERACTION WITH VP3 AND VPG.
RX PubMed=16432023; DOI=10.1099/vir.0.81456-0;
RA Kaiser W.J., Chaudhry Y., Sosnovtsev S.V., Goodfellow I.G.;
RT "Analysis of protein-protein interactions in the feline calicivirus
RT replication complex.";
RL J. Gen. Virol. 87:363-368(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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm.
CC -!- PTM: Cleaved by virus calcivirin to produce mature capsid protein.
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; L40021; AAA79324.1; -; Genomic_RNA.
DR RefSeq; NP_783197.1; NC_001481.2.
DR SMR; Q66915; -.
DR GeneID; 1502251; -.
DR KEGG; vg:1502251; -.
DR Proteomes; UP000001098; 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.
PE 1: Evidence at protein level;
KW Capsid protein; Host cytoplasm; Reference proteome;
KW T=3 icosahedral capsid protein; Virion.
FT PROPEP 1..124
FT /evidence="ECO:0000250"
FT /id="PRO_0000036880"
FT CHAIN 125..668
FT /note="Capsid protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036881"
FT CHAIN ?465..668
FT /note="Protein 40k"
FT /id="PRO_0000341625"
FT SITE 124..125
FT /note="Cleavage; by calicivirin"
FT MUTAGEN 124
FT /note="E->H,K,L: Complete loss of precursor cleavage by
FT viral calcivirin."
FT /evidence="ECO:0000269|PubMed:9525628"
FT MUTAGEN 124
FT /note="E->Q,D: Partial loss of precursor cleavage by
FT calcivirin."
FT /evidence="ECO:0000269|PubMed:9525628"
FT MUTAGEN 125
FT /note="A->G,H,L,R,V: No effect on precursor cleavage by
FT calcivirin."
FT /evidence="ECO:0000269|PubMed:9525628"
FT MUTAGEN 125
FT /note="A->P: Complete loss of precursor cleavage by viral
FT calcivirin."
FT /evidence="ECO:0000269|PubMed:9525628"
SQ SEQUENCE 668 AA; 73518 MW; C1E38D92BB6E5FA6 CRC64;
MCSTCANVLK YYNWDPHFKL VINPNKFLSI GFCDNPLMCC YPELLPEFGT VWDCDQSPLQ
IYLESILGDD EWSSTYEAID PVVPPMHWNE AGKIFQPHPG VLMHHIIGEV AKAWDPNLPL
FRLEADDGSI TAPEQGTVVG GVIAEPSSQM STAADMASGK SVDSEWEAFF SFHTSVNWST
SETQGKILFK QSLGPLLNPY LEHLSKLYVA WSGSVEVRFS ISGSGVFGGK LAAIVVPPGV
DPIQSTSMLQ YPHVLFDARQ VEPVIFTIPD LRSTLYHLMS DTDTTSLVIM VYNDLINPYA
NDSNSSGCIV TVETKPGSDF KFHLLKPPGS MLTHGSVPSD LIPKTSSLWI GNRFWSDITD
FVIRPFVFQA NRHFDFNQET AGWSTPRFRP ITVTISEKNG AKLGVGVATD FIVPGIPDGW
PDTTIGEKLV PAGDYAITNG SGNDITTANQ YDAADIIRNN TNFKGMYICG SLQRAWGDKK
ISNTAFITTA TVEGNDLIPS NVIDQTKIAI FQDNHVQDEV QTSDDTLALL GYTGIGEEAI
GANRERVVRI STLPETGARG GNHPIFYKNS IKLGYVIRSI DVFNSQILHT SRQLSLNHYL
LPPDSFAVYR IIDSNGSWFD VGIDFDGFSF VGVSDVGKLE FPLTASYMGI QLAKIRLASN
IRSTMTKL
