CAHH_VARV
ID CAHH_VARV Reviewed; 304 AA.
AC P0DSY2; P33065;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 1.
DT 29-SEP-2021, entry version 11.
DE RecName: Full=Cell surface-binding protein;
DE AltName: Full=Carbonic anhydrase homolog;
GN ORFNames=D8L;
OS Variola virus.
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX NCBI_TaxID=10255;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Bangladesh-1975;
RX PubMed=8264798; DOI=10.1038/366748a0;
RA Massung R.F., Esposito J.J., Liu L.I., Qi J., Utterback T.R., Knight J.C.,
RA Aubin L., Yuran T.E., Parsons J.M., Loparev V.N., Selivanov N.A.,
RA Cavallaro K.F., Kerlavage A.R., Mahy B.W.J., Venter J.C.;
RT "Potential virulence determinants in terminal regions of variola smallpox
RT virus genome.";
RL Nature 366:748-751(1993).
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; L22579; AAA60846.1; -; Genomic_DNA.
DR PIR; H72162; H72162.
DR PIR; T28536; T28536.
DR RefSeq; NP_042142.1; NC_001611.1.
DR SMR; P0DSY2; -.
DR GeneID; 1486424; -.
DR KEGG; vg:1486424; -.
DR Proteomes; UP000119805; 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_0000077452"
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; 35401 MW; D7210C50F75E1625 CRC64;
MSQQLSPINI ETKKAISNAR LKPLNIHYNE SKPTTIQNTG KLVRINFKGG YLSGGFLPNE
YVLSSLHIYW GKEDDYGSNH LIDVYKYSGE INLVHWNKKK YSSYEEAKKH DDGLIIISIF
LQVSDHKNVY FQKIVNQLDS IRTANTSAPF DSVFYLDNLL PSKLDYFKYL GTTINHSADA
VWIIFPTPIN IHSDQLSKFR TLLSLSNHEG KPHYITENYR NPYKLNDDTE VYYSGEIIRA
ATTSPARENY FMRWLSDLRE TCFSYYQKYI EGNKTFAIIA IVFVYILTAI LFLMSRRYSR
EKQN