ID   CAHH_RABPU              Reviewed;         304 AA.
AC   Q6RZI9;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   12-AUG-2020, entry version 63.
DE   RecName: Full=Cell surface-binding protein;
DE   AltName: Full=Carbonic anhydrase homolog;
GN   OrderedLocusNames=RPXV102;
OS   Rabbitpox virus (strain Utrecht) (RPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=45417;
OH   NCBI_TaxID=9986; Oryctolagus cuniculus (Rabbit).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16227218; DOI=10.1099/vir.0.81331-0;
RA   Li G., Chen N., Roper R.L., Feng Z., Hunter A.L., Danila M.,
RA   Lefkowitz E.J., Buller R.M.L., Upton C.;
RT   "Complete coding sequences of the rabbitpox virus genome.";
RL   J. Gen. Virol. 86:2969-2977(2005).
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000305}.
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DR   EMBL; AY484669; AAS49815.1; -; Genomic_DNA.
DR   SMR; Q6RZI9; -.
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; Membrane; Transmembrane;
KW   Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW   Virion; Virus entry into host cell.
FT   CHAIN           1..304
FT                   /note="Cell surface-binding protein"
FT                   /id="PRO_0000077447"
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"
SQ   SEQUENCE   304 AA;  35245 MW;  64E6B0A05096FFC7 CRC64;
     MPQQLSPINI ETKKAISNAR LKPLDIHYNE SKPTTIQNTG KLVRINFKGG YISGGFLPNE
     YVLSSLHIYW GKEDDYGSNH LIDVYKYSGE INLVHWNKKK YSSYEEAKKH DDGLIIISIF
     LQVSDHKNVY FQKIVNQLDS IRSANTSAPF DSVFYLDNLL PSTLDYFTYL GTTINHSADA
     AWIIFPTPIN IHSDQLSKFR TLLSSSNHDG KPHYITENYR NPYKLNDDTQ VYYSGEIIRA
     ATTSPARDNY FMRWLSDLRE TCFSYYQKYI EGNKTFAIIA IVFVFILTAI LFLMSRRYSR
     EKQN