ID   CAHH_VACCW              Reviewed;         304 AA.
AC   P04195; Q76ZR9;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-1987, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Cell surface-binding protein;
DE   AltName: Full=Carbonic anhydrase homolog;
GN   OrderedLocusNames=VACWR113; ORFNames=D8L;
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].
RX   PubMed=3739227; DOI=10.1016/0042-6822(86)90011-5;
RA   Niles E.G., Condit R.C., Caro P., Davidson K., Matusick L., Seto J.;
RT   "Nucleotide sequence and genetic map of the 16-kb vaccinia virus HindIII D
RT   fragment.";
RL   Virology 153:96-112(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2104847; DOI=10.1016/s0021-9258(19)40055-0;
RA   Maa J.-S., Rodriguez J.F., Esteban M.;
RT   "Structural and functional characterization of a cell surface binding
RT   protein of vaccinia virus.";
RL   J. Biol. Chem. 265:1569-1577(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE 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   [4]
RP   IDENTIFICATION OF PROTEIN.
RX   PubMed=3418784; DOI=10.1128/jvi.62.10.3772-3778.1988;
RA   Niles E.G., Seto J.;
RT   "Vaccinia virus gene D8 encodes a virion transmembrane protein.";
RL   J. Virol. 62:3772-3778(1988).
CC   -!- FUNCTION: Binds to chondroitin sulfate on the cell surface to provide
CC       virion attachment to target cell. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}. Note=Component of
CC       the mature virion (MV) membrane. {ECO:0000305}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC   -!- PTM: Apparently non-glycosylated.
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000305}.
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DR   EMBL; J05190; AAA48233.1; -; Genomic_DNA.
DR   EMBL; AY243312; AAO89392.1; -; Genomic_DNA.
DR   PIR; A01146; CRVZW.
DR   RefSeq; YP_232995.1; NC_006998.1.
DR   SMR; P04195; -.
DR   ABCD; P04195; 5 sequenced antibodies.
DR   DNASU; 3707569; -.
DR   GeneID; 3707569; -.
DR   KEGG; vg:3707569; -.
DR   Proteomes; UP000000344; Genome.
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:0004089; F:carbonate dehydratase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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   Gene3D; 3.10.200.10; -; 1.
DR   InterPro; IPR001148; CA_dom.
DR   InterPro; IPR036398; CA_dom_sf.
DR   InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR   PANTHER; PTHR18952; PTHR18952; 1.
DR   Pfam; PF00194; Carb_anhydrase; 1.
DR   SMART; SM01057; Carb_anhydrase; 1.
DR   SUPFAM; SSF51069; SSF51069; 1.
DR   PROSITE; PS51144; ALPHA_CA_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Host-virus interaction; Late protein; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix;
KW   Viral attachment to host cell; Viral envelope protein; Virion;
KW   Virus entry into host cell.
FT   CHAIN           1..304
FT                   /note="Cell surface-binding protein"
FT                   /id="PRO_0000077451"
FT   TOPO_DOM        1..275
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        276..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        295..304
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1..235
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   DISULFID        262
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        139
FT                   /note="D -> H (in Ref. 2; AAA48233)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   304 AA;  35446 MW;  67F195C8875455BA CRC64;
     MPQQLSPINI ETKKAISNAR LKPLDIHYNE SKPTTIQNTG KLVRINFKGG YISGGFLPNE
     YVLSSLHIYW GKEDDYGSNH LIDVYKYSGE INLVHWNKKK YSSYEEAKKH DDGLIIISIF
     LQVLDHKNVY FQKIVNQLDS IRSANTSAPF DSVFYLDNLL PSKLDYFTYL GTTINHSADA
     VWIIFPTPIN IHSDQLSKFR TLLSSSNHDG KPHYITENYR NPYKLNDDTQ VYYSGEIIRA
     ATTSPARENY FMRWLSDLRE TCFSYYQKYI EENKTFAIIA IVFVFILTAI LFFMSRRYSR
     EKQN