SPI1_CWPXB
ID SPI1_CWPXB Reviewed; 355 AA.
AC P42927; Q8QMN1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 29-SEP-2021, entry version 95.
DE RecName: Full=Serine proteinase inhibitor 1;
DE Short=Serp-1;
DE Short=Serpin-1;
GN Name=SPI-1; OrderedLocusNames=CPXV217;
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.
RX PubMed=8009842; DOI=10.1006/viro.1994.1347;
RA Ali A.N., Turner P.C., Brooks M.A., Moyer R.W.;
RT "The SPI-1 gene of rabbitpox virus determines host range and is required
RT for hemorrhagic pock formation.";
RL Virology 202:305-314(1994).
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.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA19160.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAM13655.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U07767; AAA19160.1; ALT_INIT; Unassigned_DNA.
DR EMBL; AF482758; AAM13655.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_619997.1; NC_003663.2.
DR SMR; P42927; -.
DR MEROPS; I04.028; -.
DR GeneID; 1486096; -.
DR KEGG; vg:1486096; -.
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: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; 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 3: Inferred from homology;
KW Host cytoplasm; Protease inhibitor; Serine protease inhibitor.
FT CHAIN 1..355
FT /note="Serine proteinase inhibitor 1"
FT /id="PRO_0000094138"
FT SITE 320..321
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
SQ SEQUENCE 355 AA; 40870 MW; FA7625AA9330F47C CRC64;
MDIFKELILK HTDENVLISP VSILSTLSIL NHGAAGSTAE QLSKYIENKN TPKDDKDDNN
DMDVDIPYCA TLATANKIYC SDSIEFHASF LQKIKDDFQT VNFNNANQTK ELINEWVKTM
TNGKINSLLT TPLPINTRMT VVSAVHFKAM WKYPFSKHLT YTDKFYISKN IVTSVDMMVS
TKNDLQYVHI NELFGGFSII DIPYEGNSSM VIILPDDIEG LYNIEKHITD ENFKKWCSKL
STKSIDLYMP KFKVEMTEPY NLVPILENLG LTNIFGYYSD FSKMCNETIT VEKFLHKTFI
DVNEEYTEAS AITGVFMTNF SMVYRTKVYI NHPFMYMIKD NTGRILFIGK YCYPQ