ID   SPI2_VARV               Reviewed;         344 AA.
AC   P0DSW4; P33830;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 1.
DT   29-SEP-2021, entry version 12.
DE   RecName: Full=Serine proteinase inhibitor 2;
DE            Short=Serp-2;
DE            Short=Serpin-2;
GN   Name=SPI-2; ORFNames=B12R, B13R, B14R;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Somalia-1977;
RA   Massung R.F., Loparev V.N., Knight J.C., Chizhikov V.E., Parsons J.M.,
RA   Totmenin A.V., Shchelkunov S.N., Esposito J.J.;
RL   Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in the regulation of the complement cascade.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the serpin family. Poxviruses subfamily.
CC       {ECO:0000305}.
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DR   EMBL; L22579; AAA60921.1; -; Genomic_DNA.
DR   EMBL; U18341; AAA69453.1; -; Genomic_DNA.
DR   PIR; T28611; T28611.
DR   RefSeq; NP_042225.1; NC_001611.1.
DR   SMR; P0DSW4; -.
DR   GeneID; 1486543; -.
DR   KEGG; vg:1486543; -.
DR   Proteomes; UP000119805; Genome.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0039650; P:suppression by virus of host cysteine-type endopeptidase activity involved in apoptotic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.39.10; -; 1.
DR   Gene3D; 3.30.497.10; -; 1.
DR   InterPro; IPR015557; Serpin_B1.
DR   InterPro; IPR023795; Serpin_CS.
DR   InterPro; IPR023796; Serpin_dom.
DR   InterPro; IPR000215; Serpin_fam.
DR   InterPro; IPR036186; Serpin_sf.
DR   InterPro; IPR042178; Serpin_sf_1.
DR   InterPro; IPR042185; Serpin_sf_2.
DR   PANTHER; PTHR11461; PTHR11461; 1.
DR   PANTHER; PTHR11461:SF180; PTHR11461:SF180; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; SSF56574; 1.
DR   PROSITE; PS00284; SERPIN; 1.
PE   3: Inferred from homology;
KW   Host cytoplasm; Host-virus interaction;
KW   Inhibition of host caspases by virus;
KW   Modulation of host cell apoptosis by virus; Protease inhibitor;
KW   Serine protease inhibitor.
FT   CHAIN           1..344
FT                   /note="Serine proteinase inhibitor 2"
FT                   /id="PRO_0000448126"
FT   SITE            306..307
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   344 AA;  38435 MW;  4EAF2AEDD394D063 CRC64;
     MDIFREIASS TKGENVFISP ATISSVLTIL YYGANGSTAE QLSKYVEKEE TMDKVSAQNI
     SFKSMNKVYG RYSAVFKNSF LGKIGDNFQT VDFTDCRTID AINKCVDVFT EGKINPLLTE
     QLSPNTCLLA ISAVYFKAKW LIPFKKEFTS DYPFYVSPTE MVDVSMMSMY GESFNYASVK
     ESFGNFSIIE LPYVGNTSMM VILPDKIDGL ESIKQNLTDT NFKKWCNSLE ATFIDVHIPK
     FKVTGSYNLV DTLVKLGLTD VFYSTGDYSN MCNSDVSVDA MIHKTYIDVN EEYTEAAAAT
     SVLVADCAST VTNEFCADHP FIYVIRHVDG KILFVGRYCS PTTN