ID   CAPSD_CACV4             Reviewed;         691 AA.
AC   O72120;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   23-FEB-2022, entry version 77.
DE   RecName: Full=Capsid protein;
DE   AltName: Full=Coat protein;
DE            Short=CP;
DE   AltName: Full=VP1;
DE   Flags: Precursor;
GN   ORFNames=ORF2;
OS   Canine calicivirus (strain 48) (CaCV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Caliciviridae; Vesivirus; unclassified Vesivirus.
OX   NCBI_TaxID=292348;
OH   NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=10211962; DOI=10.1099/0022-1317-80-4-929;
RA   Roerink F., Hashimoto M., Tohya Y., Mochizuki M.;
RT   "Organization of the canine calicivirus genome from the RNA polymerase gene
RT   to the poly(A) tail.";
RL   J. Gen. Virol. 80:929-935(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=12206310; DOI=10.1023/a:1020174225622;
RA   Matsuura Y., Tohya Y., Nakamura K., Shimojima M., Roerink F., Mochizuki M.,
RA   Takase K., Akashi H., Sugimura T.;
RT   "Complete nucleotide sequence, genome organization and phylogenic analysis
RT   of the canine calicivirus.";
RL   Virus Genes 25:67-73(2002).
RN   [3]
RP   PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF GLU-157 AND SER-158.
RX   PubMed=10640558; DOI=10.1099/0022-1317-81-1-195;
RA   Matsuura Y., Tohya Y., Onuma M., Roerink F., Mochizuki M., Sugimura T.;
RT   "Expression and processing of the canine calicivirus capsid precursor.";
RL   J. Gen. Virol. 81:195-199(2000).
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 specific cellular receptor. 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 (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   -!- SIMILARITY: Belongs to the caliciviridae capsid protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF053720; AAC16446.1; -; Genomic_RNA.
DR   EMBL; AB070225; BAB83602.1; -; Genomic_RNA.
DR   SMR; O72120; -.
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; T=3 icosahedral capsid protein; Virion.
FT   PROPEP          1..157
FT                   /id="PRO_0000036872"
FT   CHAIN           158..691
FT                   /note="Capsid protein"
FT                   /id="PRO_0000036873"
FT   SITE            157..158
FT                   /note="Cleavage; by 3C-like protease"
FT   MUTAGEN         157
FT                   /note="E->K: Complete loss of processing by the viral
FT                   protease."
FT                   /evidence="ECO:0000269|PubMed:10640558"
FT   MUTAGEN         158
FT                   /note="S->P: Complete loss of processing by the viral
FT                   protease."
FT                   /evidence="ECO:0000269|PubMed:10640558"
SQ   SEQUENCE   691 AA;  76181 MW;  F1C9774C9217AEF4 CRC64;
     MARYLELNPQ NYSDEEYDYD SYNPFPNFEK NLASHYGTDF VPRINLDDFF LDDEDFEFCD
     DPLNCCFPDY LASLGEEEFI YEGDEPYIVL KHQLVSSTMW DDGTFTYPIL PPFKTSSISY
     FLPKPGEVLH RCLMAVAKGM DPDLQVAVGT EFQFRAESDS SHPPDITTED QGTVVATGPQ
     PSAPAMATLA TAATGTMPEE WKNFFSYYTT INWATTDETG KVLFVQNLAP RMNPFLDHIA
     KMYTGWSGSM EVRFTISGSG VFGGKVAAVL VPPGISTEGG TNLLQFPHVL VDARQTEPVI
     FTIPDIRTQL WHDMHDTSTS HLVILVYNDL VNPFQGGENG TSCTITVETR GGTDFEFHLL
     KPPTRKMIFG ADPSRLIPRR SQFWEGNRLP GVITSFVCLP RMFQANRHFD CKRQTFGWSR
     PVHKGIEVRV DATNKDAANT TDIGIHVVTA RNAIKSDIPD GWPDYYRTGE QVYNNTTQTF
     QEVKESVMGS AVPDSTATAM TWHHLPTVVF GHGTAVGSKT TNSKVLSGNF YAIGNFDQSG
     NIKLYPSYWI AKEQSAGGAP IGAYEDMVKR IDVLPTAQTT GGNFPVAFVS KFASSHNGNG
     VSVYNSQILT TSALLAQDVY DIGPNALAVF KIKGSGGYWF DLGISADGFS YVGGGNLNFS
     SLQFPLEATY VGMASLHNKL QYNLGGSATT L