CAPSH_ASFB7
ID CAPSH_ASFB7 Reviewed; 646 AA.
AC P22776;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Hexon protein p72 {ECO:0000303|PubMed:31624094};
DE AltName: Full=Major capsid protein;
DE Short=MCP;
DE AltName: Full=p72;
DE AltName: Full=p73;
GN OrderedLocusNames=Ba71V-081; ORFNames=B646L;
OS African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V)
OS (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=10498;
OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2327074; DOI=10.1016/0042-6822(90)90432-q;
RA Lopez-Otin C., Freije J.M.P., Parra F., Mendez E., Vinuela E.;
RT "Mapping and sequence of the gene coding for protein p72, the major capsid
RT protein of African swine fever virus.";
RL Virology 175:477-484(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11831707; DOI=10.1006/viro.1995.1149;
RA Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C.,
RA Rodriguez J.F., Vinuela E.;
RT "Analysis of the complete nucleotide sequence of African swine fever
RT virus.";
RL Virology 208:249-278(1995).
RN [3]
RP FUNCTION.
RX PubMed=8764090; DOI=10.1128/jvi.70.8.5689-5694.1996;
RA Gomez-Puertas P., Rodriguez F., Oviedo J.M., Ramiro-Ibanez F.,
RA Ruiz-Gonzalvo F., Alonso C., Escribano J.M.;
RT "Neutralizing antibodies to different proteins of African swine fever virus
RT inhibit both virus attachment and internalization.";
RL J. Virol. 70:5689-5694(1996).
RN [4]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=8970959; DOI=10.1128/jvi.70.12.8382-8390.1996;
RA Cobbold C., Whittle J.T., Wileman T.;
RT "Involvement of the endoplasmic reticulum in the assembly and envelopment
RT of African swine fever virus.";
RL J. Virol. 70:8382-8390(1996).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9580160; DOI=10.1128/jvi.72.4.3185-3195.1998;
RA Garcia-Escudero R., Andres G., Almazan F., Vinuela E.;
RT "Inducible gene expression from African swine fever virus recombinants:
RT analysis of the major capsid protein p72.";
RL J. Virol. 72:3185-3195(1998).
RN [6]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=9573294; DOI=10.1128/jvi.72.6.5215-5223.1998;
RA Cobbold C., Wileman T.;
RT "The major structural protein of African swine fever virus, p73, is
RT packaged into large structures, indicative of viral capsid or matrix
RT precursors, on the endoplasmic reticulum.";
RL J. Virol. 72:5215-5223(1998).
RN [7]
RP INTERACTION WITH PROTEIN P14.5/PE120R.
RX PubMed=11435554; DOI=10.1128/jvi.75.15.6758-6768.2001;
RA Andres G., Garcia-Escudero R., Vinuela E., Salas M.L., Rodriguez J.M.;
RT "African swine fever virus structural protein pE120R is essential for virus
RT transport from assembly sites to plasma membrane but not for infectivity.";
RL J. Virol. 75:6758-6768(2001).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=30185597; DOI=10.1128/jvi.01293-18;
RA Alejo A., Matamoros T., Guerra M., Andres G.;
RT "A Proteomic Atlas of the African Swine Fever Virus Particle.";
RL J. Virol. 92:0-0(2018).
RN [9]
RP INDUCTION.
RX PubMed=32075923; DOI=10.1128/jvi.00119-20;
RA Cackett G., Matelska D., Sykora M., Portugal R., Malecki M., Baehler J.,
RA Dixon L., Werner F.;
RT "The African Swine Fever Virus Transcriptome.";
RL J. Virol. 94:0-0(2020).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=33429879; DOI=10.3390/v13010077;
RA Aicher S.M., Monaghan P., Netherton C.L., Hawes P.C.;
RT "Unpicking the Secrets of African Swine Fever Viral Replication Sites.";
RL Viruses 13:0-0(2021).
RN [11] {ECO:0007744|PDB:6KU9}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.67 ANGSTROMS), AND FUNCTION.
RX PubMed=31530894; DOI=10.1038/s41422-019-0232-x;
RA Liu Q., Ma B., Qian N., Zhang F., Tan X., Lei J., Xiang Y.;
RT "Structure of the African swine fever virus major capsid protein p72.";
RL Cell Res. 29:953-955(2019).
RN [12] {ECO:0007744|PDB:6L2T}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.1 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, SUBUNIT, INTERACTION WITH THE MINOR CAPSID PROTEIN M1249L, AND
RP INTERACTION WITH THE MINOR CAPSID PROTEIN P17.
RX PubMed=31624094; DOI=10.1126/science.aaz1439;
RA Wang N., Zhao D., Wang J., Zhang Y., Wang M., Gao Y., Li F., Wang J.,
RA Bu Z., Rao Z., Wang X.;
RT "Architecture of African swine fever virus and implications for viral
RT assembly.";
RL Science 366:640-644(2019).
CC -!- FUNCTION: Capsid protein that self-assembles to form the pseudo-
CC hexameric capsomers of the icosahedral capsid (PubMed:31624094). 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 (PubMed:31624094). The capsid encapsulates the DNA-containing nucleoid,
CC the core shell and the inner membrane (PubMed:9580160). Plays an
CC essential role in virion assembly (PubMed:9580160). Involved in virus
CC attachment to the host cell (PubMed:8764090).
CC {ECO:0000269|PubMed:31624094, ECO:0000269|PubMed:8764090,
CC ECO:0000269|PubMed:9580160}.
CC -!- SUBUNIT: Homotrimer (PubMed:31624094). The membrane-bound form, but not
CC the cytosolic one, assembles into large complexes (PubMed:9573294).
CC Interacts with the minor capsid proteins M1249L and p17; these
CC interactions form a rigid zipper structure that stabilizes the
CC capsomers (PubMed:31624094). {ECO:0000269|PubMed:31624094,
CC ECO:0000269|PubMed:9573294}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:30185597,
CC ECO:0000269|PubMed:31624094, ECO:0000269|PubMed:33429879,
CC ECO:0000269|PubMed:9573294}. Host endoplasmic reticulum membrane;
CC Peripheral membrane protein {ECO:0000269|PubMed:8970959,
CC ECO:0000269|PubMed:9573294}. Host cytoplasm, host cytosol
CC {ECO:0000269|PubMed:9573294}. Note=Present in the outer part of the
CC capsid shell (PubMed:31624094). Localizes to the viral factory at 16
CC hpi (PubMed:33429879). {ECO:0000269|PubMed:31624094,
CC ECO:0000269|PubMed:33429879}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000269|PubMed:32075923, ECO:0000269|PubMed:8970959}.
CC -!- SIMILARITY: Belongs to the NCLDV major capsid protein family.
CC {ECO:0000305}.
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DR EMBL; M34142; AAA42730.1; -; Genomic_DNA.
DR EMBL; U18466; AAA65311.1; -; Genomic_DNA.
DR PIR; A34745; VCXFAS.
DR RefSeq; NP_042775.1; NC_001659.2.
DR PDB; 6KU9; EM; 2.67 A; A/B/C=1-646.
DR PDB; 6L2T; EM; 4.10 A; A/B/C=1-646.
DR PDBsum; 6KU9; -.
DR PDBsum; 6L2T; -.
DR SMR; P22776; -.
DR GeneID; 22220311; -.
DR KEGG; vg:22220311; -.
DR Proteomes; UP000000624; 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 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Direct protein sequencing; Host cytoplasm;
KW Host endoplasmic reticulum; Host membrane; Host-virus interaction;
KW Late protein; Membrane; Reference proteome; Viral attachment to host cell;
KW Virion; Virus entry into host cell.
FT CHAIN 1..646
FT /note="Hexon protein p72"
FT /id="PRO_0000221942"
FT CONFLICT 93
FT /note="G -> A (in Ref. 1; AAA42730)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 646 AA; 73179 MW; BE5443B56C8C6EC1 CRC64;
MASGGAFCLI ANDGKADKII LAQDLLNSRI SNIKNVNKSY GKPDPEPTLS QIEETHLVHF
NAHFKPYVPV GFEYNKVRPH TGTPTLGNKL TFGIPQYGDF FHDMVGHHIL GACHSSWQDA
PIQGTAQMGA HGQLQTFPRN GYDWDNQTPL EGAVYTLVDP FGRPIVPGTK NAYRNLVYYC
EYPGERLYEN VRFDVNGNSL DEYSSDVTTL VRKFCIPGDK MTGYKHLVGQ EVSVEGTSGP
LLCNIHDLHK PHQSKPILTD ENDTQRTCSH TNPKFLSQHF PENSHNIQTA GKQDITPITD
ATYLDIRRNV HYSCNGPQTP KYYQPPLALW IKLRFWFNEN VNLAIPSVSI PFGERFITIK
LASQKDLVNE FPGLFIRQSR FIPGRPSRRN IRFKPWFIPG VINEISLTNN ELYINNLFVT
PEIHNLFVKR VRFSLIRVHK TQVTHTNNNH HDEKLMSALK WPIEYMFIGL KPTWNISDQN
PHQHRDWHKF GHVVNAIMQP THHAEISFQD RDTALPDACS SISDISPVTY PITLPIIKNI
SVTAHGINLI DKFPSKFCSS YIPFHYGGNA IKTPDDPGAM MITFALKPRE EYQPSGHINV
SRAREFYISW DTDYVGSITT ADLVVSASAI NFLLLQNGSA VLRYST
