SPI2_CWPXB
ID SPI2_CWPXB Reviewed; 341 AA.
AC P07385;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Serine proteinase inhibitor 2;
DE Short=Serp-2;
DE Short=Serpin-2;
DE AltName: Full=Cytokine response modifier protein A;
DE AltName: Full=Hemorrhage-inducing 38 kDa protein;
DE AltName: Full=ICE inhibitor;
GN Name=CRMA; Synonyms=SPI-2; OrderedLocusNames=CPXV207;
OS Cowpox virus (strain Brighton Red) (CPV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX NCBI_TaxID=265872;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9785; Loxodonta africana (African elephant).
OH NCBI_TaxID=29092; Microtus agrestis (Short-tailed field vole).
OH NCBI_TaxID=10090; Mus musculus (Mouse).
OH NCBI_TaxID=447135; Myodes glareolus (Bank vole) (Clethrionomys glareolus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=White-pock variant;
RX PubMed=3532120; DOI=10.1073/pnas.83.20.7698;
RA Pickup D.J., Ink B.S., Hu W., Ray C.A., Joklik W.K.;
RT "Hemorrhage in lesions caused by cowpox virus is induced by a viral protein
RT that is related to plasma protein inhibitors of serine proteases.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:7698-7702(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Dietrich F.S., Ray C.A., Sharma D.A., Allen A., Pickup D.J.;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP CHARACTERIZATION.
RX PubMed=2773318; DOI=10.1016/0042-6822(89)90128-1;
RA Palumbo G.J., Pickup D.J., Fredrickson T.N., McIntyre L.J., Buller R.M.;
RT "Inhibition of an inflammatory response is mediated by a 38-kDa protein of
RT cowpox virus.";
RL Virology 172:262-273(1989).
RN [4]
RP FUNCTION.
RX PubMed=1339309; DOI=10.1016/0092-8674(92)90223-y;
RA Ray C.A., Black R.A., Kronheim S.R., Greenstreet T.A., Sleath P.R.,
RA Salvesen G.S., Pickup D.J.;
RT "Viral inhibition of inflammation: cowpox virus encodes an inhibitor of the
RT interleukin-1 beta converting enzyme.";
RL Cell 69:597-604(1992).
RN [5]
RP FUNCTION.
RX PubMed=8034697; DOI=10.1016/s0021-9258(17)32171-3;
RA Komiyama T., Ray C.A., Pickup D.J., Howard A.D., Thornberry N.A.,
RA Peterson E.P., Salvesen G.;
RT "Inhibition of interleukin-1 beta converting enzyme by the cowpox virus
RT serpin CrmA. An example of cross-class inhibition.";
RL J. Biol. Chem. 269:19331-19337(1994).
CC -!- FUNCTION: Specific and potent inhibitor of the interleukin-1-beta
CC converting enzyme (ICE) thereby suppressing an interleukin-1 beta
CC response to infection. The inhibition of ICE by crmA is an example of a
CC 'cross-class' interaction, in which a serpin inhibits a non-serine
CC proteinase. Also inhibits granzyme B. {ECO:0000269|PubMed:1339309,
CC ECO:0000269|PubMed:8034697}.
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; M14217; AAA42922.1; -; Genomic_DNA.
DR EMBL; AF482758; AAM13646.1; -; Genomic_DNA.
DR PIR; A26477; WMVZHI.
DR RefSeq; NP_619988.1; NC_003663.2.
DR PDB; 1C8O; X-ray; 2.90 A; A=1-300, B=301-341.
DR PDB; 1F0C; X-ray; 2.26 A; A=1-305, B=306-341.
DR PDB; 1M93; X-ray; 1.65 A; A=1-55, B=56-300, C=301-341.
DR PDBsum; 1C8O; -.
DR PDBsum; 1F0C; -.
DR PDBsum; 1M93; -.
DR SMR; P07385; -.
DR MINT; P07385; -.
DR MEROPS; I04.028; -.
DR GeneID; 1486086; -.
DR KEGG; vg:1486086; -.
DR Reactome; R-HSA-5218900; CASP8 activity is inhibited.
DR Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
DR Reactome; R-HSA-9686347; Microbial modulation of RIPK1-mediated regulated necrosis.
DR EvolutionaryTrace; P07385; -.
DR Proteomes; UP000152733; Genome.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
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; 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 Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
DR PROSITE; PS00284; SERPIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host cytoplasm; Host-virus interaction;
KW Inhibition of host caspases by virus;
KW Modulation of host cell apoptosis by virus; Protease inhibitor;
KW Thiol protease inhibitor.
FT CHAIN 1..341
FT /note="Serine proteinase inhibitor 2"
FT /id="PRO_0000094146"
FT SITE 303..304
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT HELIX 2..10
FT /evidence="ECO:0007829|PDB:1M93"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:1M93"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:1M93"
FT HELIX 20..33
FT /evidence="ECO:0007829|PDB:1M93"
FT HELIX 36..43
FT /evidence="ECO:0007829|PDB:1M93"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:1C8O"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1C8O"
FT STRAND 58..68
FT /evidence="ECO:0007829|PDB:1M93"
FT HELIX 75..81
FT /evidence="ECO:0007829|PDB:1M93"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:1F0C"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:1M93"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:1F0C"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:1M93"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:1M93"
FT STRAND 125..139
FT /evidence="ECO:0007829|PDB:1M93"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1M93"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:1M93"
FT STRAND 157..166
FT /evidence="ECO:0007829|PDB:1M93"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:1M93"
FT STRAND 183..203
FT /evidence="ECO:0007829|PDB:1M93"
FT HELIX 207..211
FT /evidence="ECO:0007829|PDB:1M93"
FT HELIX 216..224
FT /evidence="ECO:0007829|PDB:1M93"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:1M93"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:1M93"
FT STRAND 238..245
FT /evidence="ECO:0007829|PDB:1M93"
FT HELIX 246..252
FT /evidence="ECO:0007829|PDB:1M93"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:1M93"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:1M93"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:1M93"
FT STRAND 278..286
FT /evidence="ECO:0007829|PDB:1M93"
FT STRAND 288..299
FT /evidence="ECO:0007829|PDB:1M93"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:1M93"
FT STRAND 318..324
FT /evidence="ECO:0007829|PDB:1M93"
FT STRAND 329..335
FT /evidence="ECO:0007829|PDB:1M93"
SQ SEQUENCE 341 AA; 38077 MW; 25AE4E0CB123E172 CRC64;
MDIFREIASS MKGENVFISP PSISSVLTIL YYGANGSTAE QLSKYVEKEA DKNKDDISFK
SMNKVYGRYS AVFKDSFLRK IGDNFQTVDF TDCRTVDAIN KCVDIFTEGK INPLLDEPLS
PDTCLLAISA VYFKAKWLMP FEKEFTSDYP FYVSPTEMVD VSMMSMYGEA FNHASVKESF
GNFSIIELPY VGDTSMVVIL PDNIDGLESI EQNLTDTNFK KWCDSMDAMF IDVHIPKFKV
TGSYNLVDAL VKLGLTEVFG STGDYSNMCN SDVSVDAMIH KTYIDVNEEY TEAAAATCAL
VADCASTVTN EFCADHPFIY VIRHVDGKIL FVGRYCSPTT N
