ID   SPI1_VARV               Reviewed;         372 AA.
AC   P0DOT4; P33829;
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 1;
DE            Short=Serp-1;
DE            Short=Serpin-1;
GN   Name=SPI-1; ORFNames=B25R, C12L;
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: This viral protein may be involved in the regulation of the
CC       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; AAA60930.1; -; Genomic_DNA.
DR   EMBL; U18341; AAA69464.1; -; Genomic_DNA.
DR   PIR; T28620; T28620.
DR   RefSeq; NP_042237.1; NC_001611.1.
DR   SMR; P0DOT4; -.
DR   GeneID; 1486556; -.
DR   KEGG; vg:1486556; -.
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   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   Early protein; Host cytoplasm; Protease inhibitor;
KW   Serine protease inhibitor.
FT   CHAIN           1..372
FT                   /note="Serine proteinase inhibitor 1"
FT                   /id="PRO_0000448125"
FT   SITE            337..338
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   372 AA;  43136 MW;  785225988BD66374 CRC64;
     MIYIIYRYRY CLVYTMDIFK ELILKYPDEN VLISPVSILS TLSILNHGAA GSTAEQLSKY
     IENVNENTPD DKKDDNNDMD VDVPYCATLA IANKIYCSDS IEFHASFLQK IKDDFQTVNF
     NNANQTKELI NEWVKTMTNG KINSLLTSPL PINTRMTVVS AVHFKAMWKY PFSKHLTYTD
     KFYISKNIVT SVDMMVSTEN DLQYVHINEL FGGFSIIDIP YEGNSSMVII LPDDIEGLYN
     IEKHITEENF KKWCGKLYTK SIDLYMPKFK LKMTESYNLV PILENLGLTN IFGYYADFSK
     MCNETITVEK FLHKTFIDVN EEYTEASAIT GVFMTNFSMV YRTKVYINHP FIYMIKDNTG
     RILFIGKYCY PQ