ID   A38_VACCW               Reviewed;         277 AA.
AC   P24763; Q80HU2;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Protein A38;
GN   OrderedLocusNames=VACWR162; ORFNames=A38L;
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=2045793; DOI=10.1099/0022-1317-72-6-1349;
RA   Smith G.L., Chan Y.S., Howard S.T.;
RT   "Nucleotide sequence of 42 kbp of vaccinia virus strain WR from near the
RT   right inverted terminal repeat.";
RL   J. Gen. Virol. 72:1349-1376(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1856205; DOI=10.1016/s0021-9258(18)92757-2;
RA   Amegadzie B.Y., Ahn B.-Y., Moss B.;
RT   "Identification, sequence, and expression of the gene encoding a Mr 35,000
RT   subunit of the vaccinia virus DNA-dependent RNA polymerase.";
RL   J. Biol. Chem. 266:13712-13718(1991).
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   SUBCELLULAR LOCATION.
RX   PubMed=8525613; DOI=10.1006/viro.1995.9942;
RA   Parkinson J.E., Sanderson C.M., Smith G.L.;
RT   "The vaccinia virus A38L gene product is a 33-kDa integral membrane
RT   glycoprotein.";
RL   Virology 214:177-188(1995).
RN   [5]
RP   FUNCTION.
RX   PubMed=8551630; DOI=10.1128/jvi.70.2.905-914.1996;
RA   Sanderson C.M., Parkinson J.E., Hollinshead M., Smith G.L.;
RT   "Overexpression of the vaccinia virus A38L integral membrane protein
RT   promotes Ca2+ influx into infected cells.";
RL   J. Virol. 70:905-914(1996).
CC   -!- FUNCTION: Promotes, when overexpressed, the influx of extracellular
CC       Ca2+, leading to membrane permeability and host cell necrosis.
CC       {ECO:0000269|PubMed:8551630}.
CC   -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305|PubMed:8525613};
CC       Multi-pass membrane protein {ECO:0000305|PubMed:8525613}.
CC   -!- SIMILARITY: Belongs to the chordopoxvirinae A38 protein family.
CC       {ECO:0000305}.
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DR   EMBL; D11079; BAA01810.1; -; Genomic_DNA.
DR   EMBL; M61187; AAA48334.1; -; Genomic_DNA.
DR   EMBL; X57318; CAA40588.1; -; Genomic_DNA.
DR   EMBL; AY243312; AAO89441.1; -; Genomic_DNA.
DR   PIR; S29922; S29922.
DR   SMR; P24763; -.
DR   Proteomes; UP000000344; Genome.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0070053; F:thrombospondin receptor activity; IEA:InterPro.
DR   GO; GO:0022409; P:positive regulation of cell-cell adhesion; IEA:InterPro.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; IEA:InterPro.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR006704; CD47.
DR   InterPro; IPR013147; CD47-like_TM.
DR   InterPro; IPR013270; CD47_Vset.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR10613; PTHR10613; 1.
DR   Pfam; PF04549; CD47; 1.
DR   Pfam; PF08204; V-set_CD47; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Host membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..277
FT                   /note="Protein A38"
FT                   /id="PRO_0000099325"
FT   TRANSMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        114
FT                   /note="R -> L (in Ref. 3; AAO89441)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   277 AA;  31612 MW;  96B2EB9E9E897837 CRC64;
     MSRVRISLIY LCTFMIITST KTIEYTACNN TIIIPCTIDN PTKYIRWKLD NHDILTYNKT
     SKTTILSKWH TSARLHSLSD SDVSLIIEYK DILPGTYTCE DNTGIKSTVK LVQRHTNWFN
     DYQTMLMFIF TGITLFLLFL EITYTSISVV FSTNLGILQV FGCVIAMIEL CGAFLFYPSM
     FTLRHIIGLL MMTLPSIFLI ITKVFSFWLL CKLSCAVHLI IYYQLAGYIL TVLGLGLSLK
     ECVDGTLLLS GLGTIMVSEH FSLLFLVCFP STQRDYY