ID   CAHH_VACCT              Reviewed;         304 AA.
AC   Q9JFA1;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Cell surface-binding protein;
DE   AltName: Full=Carbonic anhydrase homolog;
GN   ORFNames=TD8L;
OS   Vaccinia virus (strain Tian Tan) (VACV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10253;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Jin Q., Hou Y.D., Cheng N.H., Yao E.M., Cheng S.X., Yang X.K., Jing D.Y.,
RA   Yu W.H., Yuan J.S., Ma X.J.;
RT   "Complete genomic sequence of vaccinia virus (Tian Tan strain).";
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
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; AF095689; AAF33977.1; -; Genomic_DNA.
DR   SMR; Q9JFA1; -.
DR   ABCD; Q9JFA1; 3 sequenced antibodies.
DR   Proteomes; UP000163220; 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   Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW   Viral envelope protein; Virion; Virus entry into host cell.
FT   CHAIN           1..304
FT                   /note="Cell surface-binding protein"
FT                   /id="PRO_0000077450"
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;  35444 MW;  921F3ECD3DF6800D CRC64;
     MPQQLSPINI ETKKAISNAR LKPLDIHYNE SKPTTIQNTG KLVRINFKGG YISGGFLPNE
     YVLSSLHIYW GKEDDYGSNH LIDVYKYSGE INLVHWNKKK YSSYEEAKKH DDGLIIISIF
     LQVSDHKNVY FQKIVNQLDS IRSANTSAPF DSVFYLDNLL PSKLDYFTYL GTTINHSADA
     VWIIFPTPIN IHSDQLSKFR TLLSSSNHEG KPHYITENYR NPYKLNDDTQ VYYSGEIIRA
     ATTPPARENY FMRWLSDLRE TCFSYYQKYI EENKTFAIIA IVFVFILTAI LFFMSRRYSR
     EKQN