ID   SPI3_VACCA              Reviewed;         369 AA.
AC   Q85339;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   23-FEB-2022, entry version 73.
DE   RecName: Full=Protein K2;
DE   AltName: Full=Serine proteinase inhibitor 3;
DE   Flags: Precursor;
GN   Name=SPI-3; OrderedLocusNames=MVA023L, ACAM3000_MVA_023;
OS   Vaccinia virus (strain Ankara) (VACV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=126794;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9601507; DOI=10.1006/viro.1998.9123;
RA   Antoine G., Scheiflinger F., Dorner F., Falkner F.G.;
RT   "The complete genomic sequence of the modified vaccinia Ankara strain:
RT   comparison with other orthopoxviruses.";
RL   Virology 244:365-396(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate Acambis 3000;
RA   Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S., Osborne J.,
RA   Khristova M., Wohlhueter R.M.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with A56 protein. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Extracellular side
CC       {ECO:0000250}. Note=Component of extracellular enveloped virus (EEV)
CC       but not intracellular mature virus (IMV). Anchored to the surface of
CC       the outermost membrane of EEV via its interaction with A56 protein (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the serpin family. Poxviruses subfamily.
CC       {ECO:0000305}.
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DR   EMBL; M27650; AAA69614.1; -; Genomic_DNA.
DR   EMBL; U94848; AAB96409.1; -; Genomic_DNA.
DR   EMBL; AY603355; AAT10421.1; -; Genomic_DNA.
DR   PIR; T30775; T30775.
DR   SMR; Q85339; -.
DR   MEROPS; I04.047; -.
DR   Proteomes; UP000159908; Genome.
DR   Proteomes; UP000172909; 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   3: Inferred from homology;
KW   Host cell membrane; Host membrane; Membrane; Protease inhibitor;
KW   Serine protease inhibitor; Signal; Virion.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..369
FT                   /note="Protein K2"
FT                   /id="PRO_0000094150"
SQ   SEQUENCE   369 AA;  42257 MW;  6BFE4BA1C7B14321 CRC64;
     MIALLILSLT CSASTYRLQG FTNAGIVAYK NIQDDNIVFS PFGYSFSMFM SLLPASGNTR
     IELLKTMDLR KRDLGPAFTE LISGLAKLKT SKYTYTDLTY QSFVDNTVCI KPSYYQQYHR
     FGLYRLNFRR DAVNKINSIV ERRSGMSNVV DSNMLDNNTL WAIINTIYFK GIWQYPFDIT
     KTRNASFTNK YGTKTVPMMN VVTKLQGNTI TIDDKEYDMV RLPYKDANIS MYLAIGDNMT
     HFTDSITAAK LDYWSFQLGN KVYNLKLPKF SIENKRDIKS IAEMMAPSMF NPDNASFKHM
     TRDPLYIYKM FQNAKIDVDE QGTVAEASTI MVATARSSPE KLEFNTPFVF IIRHDITGFI
     LFMGKVESP