P54_ASFB7
ID P54_ASFB7 Reviewed; 183 AA.
AC Q65194;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Inner membrane protein p54 {ECO:0000305};
DE AltName: Full=pE183L {ECO:0000303|PubMed:30185597};
GN OrderedLocusNames=Ba71V-126; ORFNames=E183L;
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 [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 [2]
RP CHARACTERIZATION.
RX PubMed=7933107; DOI=10.1128/jvi.68.11.7244-7252.1994;
RA Rodriguez F., Alcaraz C., Eiras A., Yanez R.J., Rodriguez J.M., Alonso C.,
RA Rodriguez J.F., Escribano J.M.;
RT "Characterization and molecular basis of heterogeneity of the African swine
RT fever virus envelope protein p54.";
RL J. Virol. 68:7244-7252(1994).
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 FUNCTION.
RX PubMed=9568043; DOI=10.1006/viro.1998.9068;
RA Gomez-Puertas P., Rodriguez F., Oviedo J.M., Brun A., Alonso C.,
RA Escribano J.M.;
RT "The African swine fever virus proteins p54 and p30 are involved in two
RT distinct steps of virus attachment and both contribute to the antibody-
RT mediated protective immune response.";
RL Virology 243:461-471(1998).
RN [5]
RP INTERACTION WITH HOST DYNLL1, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=11559815; DOI=10.1128/jvi.75.20.9819-9827.2001;
RA Alonso C., Miskin J., Hernaez B., Fernandez-Zapatero P., Soto L., Canto C.,
RA Rodriguez-Crespo I., Dixon L., Escribano J.M.;
RT "African swine fever virus protein p54 interacts with the microtubular
RT motor complex through direct binding to light-chain dynein.";
RL J. Virol. 75:9819-9827(2001).
RN [6]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=15047843; DOI=10.1128/jvi.78.8.4299-4313.2004;
RA Rodriguez J.M., Garcia-Escudero R., Salas M.L., Andres G.;
RT "African swine fever virus structural protein p54 is essential for the
RT recruitment of envelope precursors to assembly sites.";
RL J. Virol. 78:4299-4313(2004).
RN [7]
RP FUNCTION.
RX PubMed=15225638; DOI=10.1016/j.febslet.2004.06.001;
RA Hernaez B., Diaz-Gil G., Garcia-Gallo M., Ignacio Quetglas J.,
RA Rodriguez-Crespo I., Dixon L., Escribano J.M., Alonso C.;
RT "The African swine fever virus dynein-binding protein p54 induces infected
RT cell apoptosis.";
RL FEBS Lett. 569:224-228(2004).
RN [8]
RP INTERACTION WITH HOST DYNLL1.
RX PubMed=20686048; DOI=10.1128/jvi.01168-10;
RA Hernaez B., Tarrago T., Giralt E., Escribano J.M., Alonso C.;
RT "Small peptide inhibitors disrupt a high-affinity interaction between
RT cytoplasmic dynein and a viral cargo protein.";
RL J. Virol. 84:10792-10801(2010).
RN [9]
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 [10]
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 [11]
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).
CC -!- FUNCTION: Inner envelope protein involved, through its interaction with
CC host dynein, in the intracellular microtubule-dependent transport of
CC viral capsid toward viral factories (PubMed:11559815). Seems to induce
CC caspase-3 activation and apoptosis (PubMed:15225638). Plays a role in
CC virion morphogenesis by recruiting and transforming the host ER
CC membranes into the precursors of the viral envelope (PubMed:15047843).
CC Involved in virus attachment to the host cell (PubMed:8764090,
CC PubMed:9568043). {ECO:0000269|PubMed:11559815,
CC ECO:0000269|PubMed:15047843, ECO:0000269|PubMed:15225638,
CC ECO:0000269|PubMed:8764090, ECO:0000269|PubMed:9568043}.
CC -!- SUBUNIT: Interacts with the host light chain cytoplasmic dynein DYNLL1;
CC this interaction is critical for intracellular microtubule-dependent
CC virus transport toward viral factories. {ECO:0000269|PubMed:11559815,
CC ECO:0000269|PubMed:20686048}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305|PubMed:30185597};
CC Single-pass membrane protein {ECO:0000305}. Host cytoplasm, host
CC cytoskeleton {ECO:0000269|PubMed:11559815}. Host endoplasmic reticulum
CC membrane {ECO:0000269|PubMed:15047843}. Note=Localizes to the viral
CC factory at 16 hpi (PubMed:33429879). Host DYNLL1 and viral p54 interact
CC at the microtubular organizing center (PubMed:11559815). Found in the
CC inner envelope of the virus (PubMed:30185597).
CC {ECO:0000269|PubMed:11559815, ECO:0000269|PubMed:30185597,
CC ECO:0000269|PubMed:33429879}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000269|PubMed:32075923}.
CC -!- SIMILARITY: Belongs to the asfivirus envelope protein p54 family.
CC {ECO:0000305}.
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DR EMBL; U18466; AAA65354.1; -; Genomic_DNA.
DR RefSeq; NP_042818.1; NC_001659.2.
DR DNASU; 1488889; -.
DR GeneID; 22220355; -.
DR KEGG; vg:22220355; -.
DR BRENDA; 4.1.1.39; 3078.
DR Proteomes; UP000000624; Genome.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044163; C:host cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0039701; P:microtubule-dependent intracellular transport of viral material towards cell periphery; IEA:UniProtKB-KW.
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 InterPro; IPR008385; ASFV_p54.
DR Pfam; PF05568; ASFV_J13L; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Host cytoplasm; Host cytoskeleton; Host endoplasmic reticulum;
KW Host membrane; Host-virus interaction; Late protein; Membrane;
KW Microtubular outwards viral transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW Viral release from host cell; Virion; Virus entry into host cell.
FT CHAIN 1..183
FT /note="Inner membrane protein p54"
FT /id="PRO_0000373415"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 81..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..161
FT /note="Interaction with host DYNLL1"
FT /evidence="ECO:0000269|PubMed:11559815,
FT ECO:0000269|PubMed:20686048"
FT COMPBIAS 81..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 183 AA; 19861 MW; 98ECD7C57B50E47A CRC64;
MDSEFFQPVY PRHYGECLSP VTPPSFFSTH MYTILIAIVV LVIIIIVLIY LFSSRKKKAA
AAIEEEDIQF INPYQDQQWA EVTPQPGTSK PAGATTASAG KPVTGRPATN RPATNKPVTD
NPVTDRLVMA TGGPAAAPAA ASAHPTEPYT TVTTQNTASQ TMSAIENLRQ RNTYTHKDLE
NSL
