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 27-MAR-2024, entry version 81.
DE RecName: Full=Cell surface-binding protein OPG105;
DE AltName: Full=Carbonic anhydrase homolog;
GN Name=OPG105; 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. {ECO:0000250|UniProtKB:P04195}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250|UniProtKB:P04195}.
CC Note=Component of the mature virion (MV) membrane.
CC {ECO:0000250|UniProtKB:P04195}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC -!- PTM: Apparently non-glycosylated. {ECO:0000250|UniProtKB:P04195}.
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:0016020; C: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; Alpha carbonic anhydrase; 1.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
DR InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR PANTHER; PTHR18952; CARBONIC ANHYDRASE; 1.
DR PANTHER; PTHR18952:SF265; CARBONIC ANHYDRASE; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; Carbonic anhydrase; 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 OPG105"
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
//
