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Q66915

- CAPSD_FCVUR

UniProt

Q66915 - CAPSD_FCVUR

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Protein
Capsid protein
Gene
ORF2
Organism
Feline calicivirus (strain Cat/United States/Urbana/1960) (FCV)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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 feline junctional adhesion molecule A (F11R) and/or to alpha-2,6-linked sialic acid. 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei124 – 1252Cleavage; by calicivirin

Names & Taxonomyi

Protein namesi
Recommended name:
Capsid protein
Alternative name(s):
Coat protein
Short name:
CP
Cleaved into the following chain:
Gene namesi
ORF Names:ORF2
OrganismiFeline calicivirus (strain Cat/United States/Urbana/1960) (FCV)
Taxonomic identifieri292349 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageCaliciviridaeVesivirus
Virus hostiFelis catus (Cat) (Felis silvestris catus) [TaxID: 9685]
ProteomesiUP000001098: Genome

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi124 – 1241E → H, K or L: Complete loss of precursor cleavage by viral calcivirin. 1 Publication
Mutagenesisi124 – 1241E → Q or D: Partial loss of precursor cleavage by calcivirin. 1 Publication
Mutagenesisi125 – 1251A → G, H, L, R or V: No effect on precursor cleavage by calcivirin. 1 Publication
Mutagenesisi125 – 1251A → P: Complete loss of precursor cleavage by viral calcivirin. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 124124 By similarity
PRO_0000036880Add
BLAST
Chaini125 – 668544Capsid protein By similarity
PRO_0000036881Add
BLAST
Chaini?465 – 668204Protein 40k
PRO_0000341625Add
BLAST

Post-translational modificationi

Cleaved by virus calcivirin to produce mature capsid protein.
Cleaved by host caspase-2 and caspase-6 to generate protein p40 By similarity.

Interactioni

Subunit structurei

Homodimerizes, then multimerizes. May bind to VP3 and Vpg proteins. Binds to alpha-2,6-linked sialic acid at surface of target cells. Interacts with host F11R By similarity.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ66915.
SMRiQ66915. Positions 129-662.

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.

Q66915-1 [UniParc]FASTAAdd to Basket

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MCSTCANVLK YYNWDPHFKL VINPNKFLSI GFCDNPLMCC YPELLPEFGT    50
VWDCDQSPLQ IYLESILGDD EWSSTYEAID PVVPPMHWNE AGKIFQPHPG 100
VLMHHIIGEV AKAWDPNLPL FRLEADDGSI TAPEQGTVVG GVIAEPSSQM 150
STAADMASGK SVDSEWEAFF SFHTSVNWST SETQGKILFK QSLGPLLNPY 200
LEHLSKLYVA WSGSVEVRFS ISGSGVFGGK LAAIVVPPGV DPIQSTSMLQ 250
YPHVLFDARQ VEPVIFTIPD LRSTLYHLMS DTDTTSLVIM VYNDLINPYA 300
NDSNSSGCIV TVETKPGSDF KFHLLKPPGS MLTHGSVPSD LIPKTSSLWI 350
GNRFWSDITD FVIRPFVFQA NRHFDFNQET AGWSTPRFRP ITVTISEKNG 400
AKLGVGVATD FIVPGIPDGW PDTTIGEKLV PAGDYAITNG SGNDITTANQ 450
YDAADIIRNN TNFKGMYICG SLQRAWGDKK ISNTAFITTA TVEGNDLIPS 500
NVIDQTKIAI FQDNHVQDEV QTSDDTLALL GYTGIGEEAI GANRERVVRI 550
STLPETGARG GNHPIFYKNS IKLGYVIRSI DVFNSQILHT SRQLSLNHYL 600
LPPDSFAVYR IIDSNGSWFD VGIDFDGFSF VGVSDVGKLE FPLTASYMGI 650
QLAKIRLASN IRSTMTKL 668
Length:668
Mass (Da):73,518
Last modified:November 1, 1996 - v1
Checksum:iC1E38D92BB6E5FA6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L40021 Genomic RNA. Translation: AAA79324.1.
RefSeqiNP_783197.1. NC_001481.2.

Genome annotation databases

GeneIDi1502251.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L40021 Genomic RNA. Translation: AAA79324.1 .
RefSeqi NP_783197.1. NC_001481.2.

3D structure databases

ProteinModelPortali Q66915.
SMRi Q66915. Positions 129-662.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 1502251.

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. "RNA transcripts derived from a cloned full-length copy of the feline calicivirus genome do not require VpG for infectivity."
    Sosnovtsev S.V., Green K.Y.
    Virology 210:383-390(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Cleavage of the feline calicivirus capsid precursor is mediated by a virus-encoded proteinase."
    Sosnovtsev S.V., Sosnovtseva S.A., Green K.Y.
    J. Virol. 72:3051-3059(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE, MUTAGENESIS OF GLU-124 AND ALA-125.
  3. "Feline calicivirus capsid protein expression and self-assembly in cultured feline cells."
    Geissler K., Parrish C.R., Schneider K., Truyen U.
    Vet. Microbiol. 69:63-66(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  4. "Analysis of protein-protein interactions in the feline calicivirus replication complex."
    Kaiser W.J., Chaudhry Y., Sosnovtsev S.V., Goodfellow I.G.
    J. Gen. Virol. 87:363-368(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VP3 AND VPG.

Entry informationi

Entry nameiCAPSD_FCVUR
AccessioniPrimary (citable) accession number: Q66915
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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