ID   SPI3_VACCW              Reviewed;         369 AA.
AC   P18384; Q76ZX8;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   23-FEB-2022, entry version 86.
DE   RecName: Full=Protein K2;
DE   AltName: Full=Serine proteinase inhibitor 3;
DE   Flags: Precursor;
GN   Name=SPI-3; OrderedLocusNames=VACWR033; ORFNames=K2L;
OS   Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS   WR)).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10254;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3264331; DOI=10.1099/0022-1317-69-12-2995;
RA   Boursnell M.E.G., Foulds I.J., Campbell J.I., Binns M.M.;
RT   "Non-essential genes in the vaccinia virus HindIII K fragment: a gene
RT   related to serine protease inhibitors and a gene related to the 37K
RT   vaccinia virus major envelope antigen.";
RL   J. Gen. Virol. 69:2995-3003(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2719552; DOI=10.1007/bf01311113;
RA   Altenburger W., Suter C.P., Altenburger J.;
RT   "Partial deletion of the human host range gene in the attenuated vaccinia
RT   virus MVA.";
RL   Arch. Virol. 105:15-27(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA   Wohlhueter R.;
RT   "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT   redundancy and an error rate of 0.16/10kb.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   INTERACTION WITH A56, AND SUBCELLULAR LOCATION.
RX   PubMed=21715594; DOI=10.1099/vir.0.030460-0;
RA   Dehaven B.C., Gupta K., Isaacs S.N.;
RT   "The vaccinia virus A56 protein: a multifunctional transmembrane
RT   glycoprotein that anchors two secreted viral proteins.";
RL   J. Gen. Virol. 92:1971-1980(2011).
CC   -!- FUNCTION: Prevents cell to cell fusion via its interaction with A56
CC       protein. The A56-K2 complex associates with components of the entry
CC       fusion complex (EFC) presumably to avoid superinfection and syncytium
CC       formation.
CC   -!- SUBUNIT: Interacts with A56 protein. {ECO:0000269|PubMed:21715594}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305|PubMed:21715594};
CC       Peripheral membrane protein {ECO:0000305|PubMed:21715594}. Host cell
CC       membrane {ECO:0000305|PubMed:21715594}; Peripheral membrane protein
CC       {ECO:0000305|PubMed:21715594}; Extracellular side
CC       {ECO:0000305|PubMed:21715594}. Note=Component of extracellular
CC       enveloped virus (EEV) but not intracellular mature virus (IMV).
CC       Anchored to the surface of the outermost membrane of EEV via its
CC       interaction with A56 protein.
CC   -!- SIMILARITY: Belongs to the serpin family. Poxviruses subfamily.
CC       {ECO:0000305}.
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DR   EMBL; D00382; BAA00287.1; -; Genomic_DNA.
DR   EMBL; M27648; AAA69632.1; -; Genomic_DNA.
DR   EMBL; AY243312; AAO89312.1; -; Genomic_DNA.
DR   PIR; JS0211; WMVZS3.
DR   RefSeq; YP_232915.1; NC_006998.1.
DR   SMR; P18384; -.
DR   IntAct; P18384; 1.
DR   MINT; P18384; -.
DR   MEROPS; I04.047; -.
DR   DNASU; 3707648; -.
DR   GeneID; 3707648; -.
DR   KEGG; vg:3707648; -.
DR   Proteomes; UP000000344; Genome.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; 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; 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.
PE   1: Evidence at protein level;
KW   Host cell membrane; Host membrane; Membrane; Protease inhibitor;
KW   Reference proteome; Serine protease inhibitor; Signal; Virion.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..369
FT                   /note="Protein K2"
FT                   /id="PRO_0000094152"
SQ   SEQUENCE   369 AA;  42286 MW;  64E1C2378158ED05 CRC64;
     MIALLILSLT CSVSTYRLQG FTNAGIVAYK NIQDDNIVFS PFGYSFSMFM SLLPASGNTR
     IELLKTMDLR KRDLGPAFTE LISGLAKLKT SKYTYTDLTY QSFVDNTVCI KPSYYQQYHR
     FGLYRLNFRR DAVNKINSIV ERRSGMSNVV DSNMLDNNTL WAIINTIYFK GIWQYPFDIT
     KTRNASFTNK YGTKTVPMMN VVTKLQGNTI TIDDEEYDMV RLPYKDANIS MYLAIGDNMT
     HFTDSITAAK LDYWSFQLGN KVYNLKLPKF SIENKRDIKS IAEMMAPSMF NPDNASFKHM
     TRDPLYIYKM FQNAKIDVDE QGTVAEASTI MVATARSSPE KLEFNTPFVF IIRHDITGFI
     LFMGKVESP