PROF_ECTVM
ID PROF_ECTVM Reviewed; 134 AA.
AC Q8JL78;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 12-AUG-2020, entry version 64.
DE RecName: Full=Profilin;
GN OrderedLocusNames=EVM141;
OS Ectromelia virus (strain Moscow) (ECTV) (Mousepox virus).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX NCBI_TaxID=265874;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14675635; DOI=10.1016/s0042-6822(03)00520-8;
RA Chen N., Danila M.I., Feng Z., Buller R.M., Wang C., Han X.,
RA Lefkowitz E.J., Upton C.;
RT "The genomic sequence of Ectromelia virus, the causative agent of
RT mousepox.";
RL Virology 317:165-186(2003).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HOST TPM1 AND PROTEIN
RP A25.
RX PubMed=17650322; DOI=10.1186/1743-422x-4-76;
RA Butler-Cole C., Wagner M.J., Da Silva M., Brown G.D., Burke R.D., Upton C.;
RT "An ectromelia virus profilin homolog interacts with cellular tropomyosin
RT and viral A-type inclusion protein.";
RL Virol. J. 4:76-76(2007).
CC -!- FUNCTION: Participates in either intracellular transport of viral
CC proteins or intercellular spread of the virus. Cellular profilins
CC modulate actin filament dynamics (polymerization and depolymerization)
CC via direct binding to actin through an actin-binding domain as well as
CC by modulation of other actin-binding proteins. In contrast to cellular
CC homologs, the poxvirus profilins seem to bind actin only weakly.
CC {ECO:0000269|PubMed:17650322}.
CC -!- SUBUNIT: Interacts with host Tpm1. Interacts with protein A25.
CC {ECO:0000269|PubMed:17650322}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:17650322}.
CC Note=Localizes to inclusion bodies formed by viral A25/ATI protein in
CC the cytoplasm of the host cell.
CC -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR EMBL; AF012825; AAM92446.1; -; Genomic_DNA.
DR RefSeq; NP_671660.1; NC_004105.1.
DR SMR; Q8JL78; -.
DR IntAct; Q8JL78; 2.
DR MINT; Q8JL78; -.
DR GeneID; 951539; -.
DR KEGG; vg:951539; -.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0039680; P:actin-dependent intracellular transport of virus towards nucleus; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR InterPro; IPR005455; PFN.
DR InterPro; IPR036140; PFN_sf.
DR Pfam; PF00235; Profilin; 1.
DR SMART; SM00392; PROF; 1.
DR SUPFAM; SSF55770; SSF55770; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Actin-dependent inwards viral transport;
KW Cytoplasmic inwards viral transport; Host cytoplasm;
KW Host-virus interaction; Virus entry into host cell.
FT CHAIN 1..134
FT /note="Profilin"
FT /id="PRO_0000199689"
SQ SEQUENCE 134 AA; 15195 MW; 0335281EBE45AA6D CRC64;
MAAEWHKIIE DVSKNNKFED AAIVDYKTKK NVLAAIPNRT FAKIIPGEVI ALITNRNILK
PRIGQKFFIV YTNSLMDENT YTMELLTGYA PVSPIVIART HTALIFLMGK PTTSRREVYR
TCRDYATNVR ATGN