ID   C23L_VACCW              Reviewed;         244 AA.
AC   Q805H7;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   02-JUN-2021, entry version 59.
DE   RecName: Full=Inactive chemokine-binding protein;
DE            Short=vCKBP;
GN   Name=C23L; OrderedLocusNames=VACWR001;
GN   and
GN   Name=B29R; OrderedLocusNames=VACWR218;
OS   Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS   WR)).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10254;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA   Wohlhueter R.;
RT   "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT   redundancy and an error rate of 0.16/10kb.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   CHARACTERIZATION, FUNCTION, AND CHEMOKINE-BINDING.
RX   PubMed=9551896;
RA   Alcami A., Symons J.A., Collins P.D., Williams T.J., Smith G.L.;
RT   "Blockade of chemokine activity by a soluble chemokine binding protein from
RT   vaccinia virus.";
RL   J. Immunol. 160:624-633(1998).
CC   -!- FUNCTION: The protein is truncated in this vaccinal strain and
CC       presumably inactive, because the lack of signal peptide prevents the
CC       protein of being secreted. In the wild-type viruses inhibits host
CC       immune defense by binding to host chemokines. Binds host CC chemokines
CC       (beta chemokines) such as RANTES with high affinity, but not CXC or C
CC       chemokines (alpha and gamma chemokines). {ECO:0000269|PubMed:9551896}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}. Note=the wild-type
CC       protein is secreted, but this strain encodes a truncated form which
CC       lacks the signal peptide.
CC   -!- SIMILARITY: Belongs to the poxviridae chemokine-binding protein family.
CC       {ECO:0000305}.
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DR   EMBL; AY243312; AAO89280.1; -; Genomic_DNA.
DR   EMBL; AY243312; AAO89497.1; -; Genomic_DNA.
DR   RefSeq; YP_232883.1; NC_006998.1.
DR   RefSeq; YP_233100.1; NC_006998.1.
DR   BMRB; Q805H7; -.
DR   SMR; Q805H7; -.
DR   DNASU; 3707615; -.
DR   GeneID; 3707615; -.
DR   GeneID; 3707616; -.
DR   KEGG; vg:3707615; -.
DR   KEGG; vg:3707616; -.
DR   Proteomes; UP000000344; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   Gene3D; 2.60.240.10; -; 1.
DR   InterPro; IPR009173; Chemkine-bd_vir.
DR   InterPro; IPR003184; Orthopox_35kDa.
DR   InterPro; IPR036540; Pox_vCCI-like_sf.
DR   Pfam; PF02250; Orthopox_35kD; 1.
DR   PIRSF; PIRSF003696; VAC_C23L; 1.
DR   SUPFAM; SSF49889; SSF49889; 1.
PE   1: Evidence at protein level;
KW   Early protein; Host cytoplasm; Reference proteome.
FT   CHAIN           1..244
FT                   /note="Inactive chemokine-binding protein"
FT                   /id="PRO_0000412904"
FT   REGION          1..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..74
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   244 AA;  26366 MW;  E0490D23DAD616B2 CRC64;
     MHVPASLQQS SSSSSSCTEE ENKHHMGIDV IIKVTKQDQT PTNDKICQSV TEITESESDP
     DPEVESEDDS TSVEDVDPPT TYYSIIGGGL RMNFGFTKCP QIKSISESAD GNTVNARLSS
     VSPGQGKDSP AITHEEALAM IKDCEVSIDI RCSEEEKDSD IKTHPVLGSN ISHKKVSYED
     IIGSTIVDTK CVKNLEFSVR IGDMCKESSE LEVKDGFKYV DGSASEGATD DTSLIDSTKL
     KACV