ID   CAHH_MONPZ              Reviewed;         304 AA.
AC   Q8V4Y0;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   10-FEB-2021, entry version 79.
DE   RecName: Full=Cell surface-binding protein;
DE   AltName: Full=Carbonic anhydrase homolog;
GN   ORFNames=E8L;
OS   Monkeypox virus (strain Zaire-96-I-16) (MPX).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=619591;
OH   NCBI_TaxID=45479; Cynomys gunnisoni (Gunnison's prairie dog).
OH   NCBI_TaxID=99825; Cynomys leucurus (White-tailed prairie dog).
OH   NCBI_TaxID=45480; Cynomys ludovicianus (Black-tailed prairie dog).
OH   NCBI_TaxID=99826; Cynomys mexicanus (Mexican prairie dog).
OH   NCBI_TaxID=99827; Cynomys parvidens (Utah prairie dog).
OH   NCBI_TaxID=30650; Gliridae (dormice).
OH   NCBI_TaxID=226685; Heliosciurus ruwenzorii (Ruwenzori sun squirrel).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zaire-96-I-16;
RX   PubMed=11734207; DOI=10.1016/s0014-5793(01)03144-1;
RA   Shchelkunov S.N., Totmenin A.V., Babkin I.V., Safronov P.F.,
RA   Ryazankina O.I., Petrov N.A., Gutorov V.V., Uvarova E.A., Mikheev M.V.,
RA   Sisler J.R., Esposito J.J., Jahrling P.B., Moss B., Sandakhchiev L.S.;
RT   "Human monkeypox and smallpox viruses: genomic comparison.";
RL   FEBS Lett. 509:66-70(2001).
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; AF380138; AAL40563.1; -; Genomic_DNA.
DR   RefSeq; NP_536532.1; NC_003310.1.
DR   SMR; Q8V4Y0; -.
DR   GeneID; 929017; -.
DR   KEGG; vg:929017; -.
DR   Proteomes; UP000101269; Genome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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   InterPro; IPR018441; Carbonic_anhydrase_CA3.
DR   PANTHER; PTHR18952; PTHR18952; 1.
DR   PANTHER; PTHR18952:SF127; PTHR18952:SF127; 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_0000077446"
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;  35278 MW;  8A3E0886BDA8FBFB CRC64;
     MPQQLSPINI ETKKAISDTR LKTLDIHYNE SKPTTIQNTG KLVRINFKGG YISGGFLPNE
     YVLSTIHIYW GKEDDYGSNH LIDVYKYSGE INLVHWNKKK YSSYEEAKKH DDGIIIIAIF
     LQVSDHKNVY FQKIVNQLDS IRSANMSAPF DSVFYLDNLL PSTLDYFTYL GTTINHSADA
     AWIIFPTPIN IHSDQLSKFR TLLSSSNHEG KPHYITENYR NPYKLNDDTQ VYYSGEIIRA
     ATTSPVRENY FMKWLSDLRE ACFSYYQKYI EGNKTFAIIA IVFVFILTAI LFLMSQRYSR
     EKQN