ID   CAHH_VACCA              Reviewed;         304 AA.
AC   O57211; A9J1U5;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   07-APR-2021, entry version 92.
DE   RecName: Full=Cell surface-binding protein;
DE   AltName: Full=Carbonic anhydrase homolog;
GN   OrderedLocusNames=MVA105L, ACAM3000_MVA_105; ORFNames=D8L;
OS   Vaccinia virus (strain Ankara) (VACV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=126794;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9601507; DOI=10.1006/viro.1998.9123;
RA   Antoine G., Scheiflinger F., Dorner F., Falkner F.G.;
RT   "The complete genomic sequence of the modified vaccinia Ankara strain:
RT   comparison with other orthopoxviruses.";
RL   Virology 244:365-396(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate Acambis 3000;
RA   Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S., Osborne J.,
RA   Khristova M., Wohlhueter R.M.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18024893; DOI=10.1099/vir.0.83156-0;
RA   Meisinger-Henschel C., Schmidt M., Lukassen S., Linke B., Krause L.,
RA   Konietzny S., Goesmann A., Howley P., Chaplin P., Suter M., Hausmann J.;
RT   "Genomic sequence of chorioallantois vaccinia virus Ankara, the ancestor of
RT   modified vaccinia virus Ankara.";
RL   J. Gen. Virol. 88:3249-3259(2007).
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; U94848; AAB96450.1; -; Genomic_DNA.
DR   EMBL; AY603355; AAT10503.1; -; Genomic_DNA.
DR   EMBL; AM501482; CAM58283.1; -; Genomic_DNA.
DR   PIR; T37381; T37381.
DR   SMR; O57211; -.
DR   Proteomes; UP000136916; Genome.
DR   Proteomes; UP000159908; Genome.
DR   Proteomes; UP000172909; 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_0000077448"
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        67
FT                   /note="R -> H (in Ref. 3; CAM58283)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        144
FT                   /note="T -> A (in Ref. 3; CAM58283)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        230
FT                   /note="Q -> E (in Ref. 3; CAM58283)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        272
FT                   /note="G -> E (in Ref. 3; CAM58283)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        293
FT                   /note="F -> L (in Ref. 3; CAM58283)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        296
FT                   /note="Q -> R (in Ref. 3; CAM58283)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   304 AA;  35369 MW;  978CBD0DE2F361DD CRC64;
     MPQQLSPINI ETKKAISNAR LKPLDIHYNE SKPTTIQNTG KLVRINFKGG YISGGFLPNE
     YVLSSLRIYW GKEDDYGSNH LIDVYKYSGE INLVHWNKKK YSSYEEAKKH DDGLIIISIF
     LQVSDHKNVY FQKIVNQLDS IRSTNTSAPF DSVFYLDNLL PSKLDYFTYL GTTINHSADA
     VWIIFPTPIN IHSDQLSKFR TLLSSSNHDG KPHYITENYR NPYKLNDDTQ VYYSGEIIRA
     ATTSPARENY FMRWLSDLRE TCFSYYQKYI EGNKTFAIIA IVFVFILTAI LFFMSQRYSR
     EKQN