P17_ASFB7
ID P17_ASFB7 Reviewed; 117 AA.
AC Q89424;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 23-FEB-2022, entry version 67.
DE RecName: Full=Minor capsid protein p17 {ECO:0000303|PubMed:31624094};
GN OrderedLocusNames=Ba71V-107; ORFNames=D117L;
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].
RX PubMed=7856088; DOI=10.1006/viro.1995.1039;
RA Simon-Mateo C., Freije J.M.P., Andres G., Lopez-Otin C., Vinuela E.;
RT "Mapping and sequence of the gene encoding protein p17, a major African
RT swine fever virus structural protein.";
RL Virology 206:1140-1144(1995).
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 SUBCELLULAR LOCATION.
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 [4]
RP SUBCELLULAR LOCATION.
RX PubMed=9499098; DOI=10.1128/jvi.72.3.2373-2387.1998;
RA Rouiller I., Brookes S.M., Hyatt A.D., Windsor M., Wileman T.;
RT "African swine fever virus is wrapped by the endoplasmic reticulum.";
RL J. Virol. 72:2373-2387(1998).
RN [5]
RP FUNCTION.
RX PubMed=20504920; DOI=10.1128/jvi.00600-10;
RA Suarez C., Gutierrez-Berzal J., Andres G., Salas M.L., Rodriguez J.M.;
RT "African swine fever virus protein p17 is essential for the progression of
RT viral membrane precursors toward icosahedral intermediates.";
RL J. Virol. 84:7484-7499(2010).
RN [6]
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 [7]
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 [8]
RP STRUCTURE BY ELECTRON MICROSCOPY (4.8 ANGSTROMS) OF THE ASFV CAPSID,
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION, INTERACTION WITH HEXON
RP CAPSID PROTEIN P72, AND INTERACTION WITH MINOR CAPSID PROTEIN M1249L.
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: Together with the penton and the other minor capsid proteins
CC (M1249L, p49), forms a complicated network immediately below the outer
CC capsid shell, stabilizing the whole capsid (PubMed:31624094). Three
CC copies of p17 encircle each p72 capsomer in the inner capsid shell,
CC anchoring p72 capsomers on the inner membrane (PubMed:31624094).
CC Required for the assembly of the capsid and icosahedral morphogenesis
CC (PubMed:20504920). {ECO:0000269|PubMed:20504920,
CC ECO:0000269|PubMed:31624094}.
CC -!- SUBUNIT: Interacts with the minor capsid protein M1249L and with the
CC hexon capsid protein p72 capsomers; these interactions form a rigid
CC zipper structure that stabilizes the capsomers.
CC {ECO:0000269|PubMed:31624094}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:9499098,
CC ECO:0000305|PubMed:30185597}; Single-pass membrane protein
CC {ECO:0000255}. Host endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:8970959, ECO:0000269|PubMed:9499098}; Single-pass
CC membrane protein {ECO:0000255}. Note=Found in the inner envelope of the
CC virus.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000269|PubMed:32075923}.
CC -!- SIMILARITY: Belongs to the asfivirus minor capsid protein p17 family.
CC {ECO:0000305}.
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DR EMBL; U18466; AAA65336.1; -; Genomic_DNA.
DR EMBL; U15193; AAA67883.1; -; Genomic_DNA.
DR RefSeq; NP_042800.1; NC_001659.2.
DR GeneID; 22220336; -.
DR KEGG; vg:22220336; -.
DR Proteomes; UP000000624; Genome.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Glycoprotein; Host endoplasmic reticulum; Host membrane; Late protein;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix; Virion.
FT CHAIN 1..117
FT /note="Minor capsid protein p17"
FT /id="PRO_0000373401"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 117 AA; 13115 MW; 5633D5377E0D7D8D CRC64;
MDTETSPLLS HNLSTREGIK QSTQGLLAHT IARYPGTTAI LLGILILLVI ILIIVAIVYY
NRSVDCKSSM PKPPPSYYVQ QPEPHHHFPV FFRKRKNSTS LQSHIPSDEQ LAELAHS
