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O72120

- CAPSD_CACV4

UniProt

O72120 - CAPSD_CACV4

Protein

Capsid protein

Gene

ORF2

Organism
Canine calicivirus (strain 48) (CaCV)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    Functioni

    Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulate the genomic RNA and VP2 proteins. Attaches virion to target cells by binding to specific cellular receptor. Once attached, the virion is endocytosed. Acidification of the endosome induces conformational change of capsid protein thereby injecting virus genomic RNA into host cytoplasm By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei157 – 1582Cleavage; by 3C-like protease

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Capsid protein
    Alternative name(s):
    Coat protein
    Short name:
    CP
    VP1
    Gene namesi
    ORF Names:ORF2
    OrganismiCanine calicivirus (strain 48) (CaCV)
    Taxonomic identifieri292348 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageCaliciviridae
    Virus hostiCanis familiaris (Dog) (Canis lupus familiaris) [TaxID: 9615]

    Subcellular locationi

    Virion. Host cytoplasm By similarity

    GO - Cellular componenti

    1. host cell cytoplasm Source: UniProtKB-SubCell
    2. T=3 icosahedral viral capsid Source: UniProtKB-KW

    Keywords - Cellular componenti

    Capsid protein, Host cytoplasm, T=3 icosahedral capsid protein, Virion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi157 – 1571E → K: Complete loss of processing by the viral protease. 1 Publication
    Mutagenesisi158 – 1581S → P: Complete loss of processing by the viral protease. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 157157PRO_0000036872Add
    BLAST
    Chaini158 – 691534Capsid proteinPRO_0000036873Add
    BLAST

    Post-translational modificationi

    Cleaved by virus calcivirin to produce mature capsid protein.By similarity

    Interactioni

    Subunit structurei

    Homodimerizes, then multimerizes. May bind to VP3 and Vpg proteins By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliO72120.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di2.60.120.20. 1 hit.
    InterProiIPR004005. Calicivirus_coat.
    IPR029053. Viral_coat.
    [Graphical view]
    PfamiPF00915. Calici_coat. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O72120-1 [UniParc]FASTAAdd to Basket

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    MARYLELNPQ NYSDEEYDYD SYNPFPNFEK NLASHYGTDF VPRINLDDFF    50
    LDDEDFEFCD DPLNCCFPDY LASLGEEEFI YEGDEPYIVL KHQLVSSTMW 100
    DDGTFTYPIL PPFKTSSISY FLPKPGEVLH RCLMAVAKGM DPDLQVAVGT 150
    EFQFRAESDS SHPPDITTED QGTVVATGPQ PSAPAMATLA TAATGTMPEE 200
    WKNFFSYYTT INWATTDETG KVLFVQNLAP RMNPFLDHIA KMYTGWSGSM 250
    EVRFTISGSG VFGGKVAAVL VPPGISTEGG TNLLQFPHVL VDARQTEPVI 300
    FTIPDIRTQL WHDMHDTSTS HLVILVYNDL VNPFQGGENG TSCTITVETR 350
    GGTDFEFHLL KPPTRKMIFG ADPSRLIPRR SQFWEGNRLP GVITSFVCLP 400
    RMFQANRHFD CKRQTFGWSR PVHKGIEVRV DATNKDAANT TDIGIHVVTA 450
    RNAIKSDIPD GWPDYYRTGE QVYNNTTQTF QEVKESVMGS AVPDSTATAM 500
    TWHHLPTVVF GHGTAVGSKT TNSKVLSGNF YAIGNFDQSG NIKLYPSYWI 550
    AKEQSAGGAP IGAYEDMVKR IDVLPTAQTT GGNFPVAFVS KFASSHNGNG 600
    VSVYNSQILT TSALLAQDVY DIGPNALAVF KIKGSGGYWF DLGISADGFS 650
    YVGGGNLNFS SLQFPLEATY VGMASLHNKL QYNLGGSATT L 691
    Length:691
    Mass (Da):76,181
    Last modified:August 1, 1998 - v1
    Checksum:iF1C9774C9217AEF4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF053720 Genomic RNA. Translation: AAC16446.1.
    AB070225 Genomic RNA. Translation: BAB83602.1.
    RefSeqiNP_777374.1. NC_004542.1.

    Genome annotation databases

    GeneIDi956315.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF053720 Genomic RNA. Translation: AAC16446.1 .
    AB070225 Genomic RNA. Translation: BAB83602.1 .
    RefSeqi NP_777374.1. NC_004542.1.

    3D structure databases

    ProteinModelPortali O72120.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 956315.

    Family and domain databases

    Gene3Di 2.60.120.20. 1 hit.
    InterProi IPR004005. Calicivirus_coat.
    IPR029053. Viral_coat.
    [Graphical view ]
    Pfami PF00915. Calici_coat. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Organization of the canine calicivirus genome from the RNA polymerase gene to the poly(A) tail."
      Roerink F., Hashimoto M., Tohya Y., Mochizuki M.
      J. Gen. Virol. 80:929-935(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Complete nucleotide sequence, genome organization and phylogenic analysis of the canine calicivirus."
      Matsuura Y., Tohya Y., Nakamura K., Shimojima M., Roerink F., Mochizuki M., Takase K., Akashi H., Sugimura T.
      Virus Genes 25:67-73(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    3. "Expression and processing of the canine calicivirus capsid precursor."
      Matsuura Y., Tohya Y., Onuma M., Roerink F., Mochizuki M., Sugimura T.
      J. Gen. Virol. 81:195-199(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING, MUTAGENESIS OF GLU-157 AND SER-158.

    Entry informationi

    Entry nameiCAPSD_CACV4
    AccessioniPrimary (citable) accession number: O72120
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 9, 2004
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 59 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3