ID   P17_ASFK5               Reviewed;         117 AA.
AC   P0C9Y8;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   23-FEB-2022, entry version 25.
DE   RecName: Full=Minor capsid protein p17 {ECO:0000250|UniProtKB:Q89424};
GN   OrderedLocusNames=Ken-119;
OS   African swine fever virus (isolate Pig/Kenya/KEN-50/1950) (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=561445;
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 [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; AY261360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; P0C9Y8; -.
DR   Proteomes; UP000000861; 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_0000373402"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          97..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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        98
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   117 AA;  13160 MW;  83D77C64618CD49D CRC64;
     MDTETSPLLS HNLSTREGIK QSTQGFLAHT IARHPGITAI ILGILILLVI ILIVVAIVYY
     NRSVDCKSTM PKLPPPGYYV QQPEPHHHFP VFFRKRKNST TQQHIPSDEQ LAELAHS