CAPSH_ASFM2
ID CAPSH_ASFM2 Reviewed; 646 AA.
AC Q8V9S6;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Hexon protein p72 {ECO:0000250|UniProtKB:P22776};
DE AltName: Full=Major capsid protein;
DE Short=MCP;
DE AltName: Full=p72;
DE AltName: Full=p73;
GN OrderedLocusNames=Mal-089;
OS African swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=10500;
OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH NCBI_TaxID=85517; Phacochoerus aethiopicus (Warthog).
OH NCBI_TaxID=41426; Phacochoerus africanus (Warthog).
OH NCBI_TaxID=273792; Potamochoerus larvatus (Bushpig).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Roberts P.C., Lu Z., Rock D.L.;
RT "Nucleotide sequence and analysis of 16.25 kilobase pairs of the African
RT swine fever virus genome that span the central variable region.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kutish G.F., Rock D.L.;
RT "African swine fever virus genomes.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Capsid protein that self-assembles to form the pseudo-
CC hexameric capsomers of the icosahedral capsid (By similarity). The
CC capsid is constructed of 2760 pseudo-hexameric capsomers and 12
CC pentameric capsomers, with a T=277 symmetry, about 200 nm in diameter
CC (By similarity). The capsid encapsulates the DNA-containing nucleoid,
CC the core shell and the inner membrane (By similarity). Plays an
CC essential role in virion assembly (By similarity). Involved in virus
CC attachment to the host cell (By similarity).
CC {ECO:0000250|UniProtKB:P22776}.
CC -!- SUBUNIT: Homotrimer (By similarity). The membrane-bound form, but not
CC the cytosolic one, assembles into large complexes (By similarity).
CC Interacts with the minor capsid proteins M1249L and p17; these
CC interactions form a rigid zipper structure that stabilizes the
CC capsomers (By similarity). {ECO:0000250|UniProtKB:P22776}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P22776}. Host
CC endoplasmic reticulum membrane; Peripheral membrane protein. Host
CC cytoplasm, host cytosol {ECO:0000250|UniProtKB:P22776}. Note=Present in
CC the outer part of the capsid shell (By similarity). Localizes to the
CC viral factory at 16 hpi (By similarity).
CC {ECO:0000250|UniProtKB:P22776}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NCLDV major capsid protein family.
CC {ECO:0000305}.
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DR EMBL; AY261361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L00966; AAL31338.1; -; Genomic_DNA.
DR SMR; Q8V9S6; -.
DR Proteomes; UP000000860; Genome.
DR GO; GO:0044164; C:host cell cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR Gene3D; 2.70.9.20; -; 1.
DR InterPro; IPR007542; MCP_C.
DR InterPro; IPR038519; MCP_C_sf.
DR InterPro; IPR016112; VP_dsDNA_II.
DR Pfam; PF04451; Capsid_NCLDV; 1.
DR SUPFAM; SSF49749; SSF49749; 2.
PE 3: Inferred from homology;
KW Capsid protein; Host cytoplasm; Host endoplasmic reticulum; Host membrane;
KW Host-virus interaction; Late protein; Membrane;
KW Viral attachment to host cell; Virion; Virus entry into host cell.
FT CHAIN 1..646
FT /note="Hexon protein p72"
FT /id="PRO_0000373386"
SQ SEQUENCE 646 AA; 73263 MW; E9F16DB699E7ED5A CRC64;
MASGGAFCLI ANDGKADKII LAQDLLNSRI SNIKNVNKSY GKPDPEPTLS QIEETHMVHF
NAHFKPYVPI GFEYNKVRPH TGTPTLGNKL TFGIPQYGDF FHDMVGHHVL GACHSSWQDA
PIQGSSQMGA HGQLQTFPRN GYDWDNQTPL EGAVYTLVDP FGRPIVPGTK NAYRNLVYYC
EYPGERLYEN VRFDVNGNSL DEYSSDVTTL VRKFCIPGDK MTGYKHLVGQ EVSVEGTSGP
LLCNIHDLHK PHQSKPILTD ENDTQRTCTH TNPKFLSQHF PENSHNIQTA GKQDITPITD
TTYLDIRRNV QYSCNGPQTP KYYQPPLALW IKLRFWFNEN VNLAIPSVSI PFGERFITIK
LASQKDLVNE FPGLFVRQSR FIPGRPSRRN IRFKPWFIPG VINEISLTNN ELYINNLFVT
PEIHNLFVKR VRFSLIRVHK TQVTHTNNNH HDEKLMSALK WPIEYMFIGL KPTWNISDQN
PHQHRDWHKF GHVVNAIMQP THHAEISFQD RDTALPDACS SISDINPVTY PITLPIIKNI
SVTAHGINLI DKFPSKFCSS YIPFHYGGNS IKTPDDPGAM MITFALKPRE EYQPSGHINV
SRAREFYISW DTDYVGSITT ADLVVSASAI NFLLLQNGSA VLRYST