P17_ASFM2
ID P17_ASFM2 Reviewed; 117 AA.
AC Q65223;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Minor capsid protein p17 {ECO:0000250|UniProtKB:Q89424};
GN OrderedLocusNames=Mal-115; ORFNames=i1L;
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].
RX PubMed=8021596; DOI=10.1099/0022-1317-75-7-1655;
RA Dixon L.K., Twigg S.R.F., Baylis S.A., Vydelingum S., Bristow C.,
RA Hammond J.M., Smith G.L.;
RT "Nucleotide sequence of a 55 kbp region from the right end of the genome of
RT a pathogenic African swine fever virus isolate (Malawi LIL20/1).";
RL J. Gen. Virol. 75:1655-1684(1994).
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: 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 (By similarity). Three
CC copies of p17 encircle each p72 capsomer in the inner capsid shell,
CC anchoring p72 capsomers on the inner membrane (By similarity). Required
CC for the assembly of the capsid and icosahedral morphogenesis (By
CC similarity). {ECO:0000250|UniProtKB:Q89424}.
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:0000250|UniProtKB:Q89424}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250|UniProtKB:Q89424};
CC Single-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum
CC membrane {ECO:0000250|UniProtKB:Q89424}; Single-pass membrane protein
CC {ECO:0000255}. Note=Found in the inner envelope of the virus.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the asfivirus minor capsid protein p17 family.
CC {ECO:0000305}.
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DR EMBL; X71982; CAA50814.1; -; Genomic_DNA.
DR EMBL; AY261361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Proteomes; UP000000860; 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 3: Inferred from homology;
KW Glycoprotein; Host endoplasmic reticulum; Host membrane; Membrane;
KW Transmembrane; Transmembrane helix; Virion.
FT CHAIN 1..117
FT /note="Minor capsid protein p17"
FT /id="PRO_0000373403"
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; 13138 MW; 3E86176BE8619AB5 CRC64;
MDTETSPLLS HNLSTREGIK QNTQGLLAHT IARHPGITAI ILGILILLVI ILIIVAIVYY
NRSVDCKSNM PRPPPSYSIQ QSEPHHHFPV FFRKRKNSTS QQAHIPSDEQ LAELVHS
