ID   A38_VARV                Reviewed;         277 AA.
AC   P0DST6; P33853;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 1.
DT   03-AUG-2022, entry version 11.
DE   RecName: Full=Protein A38;
GN   ORFNames=A38L, A41L;
OS   Variola virus.
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=10255;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Harvey;
RX   PubMed=1331292; DOI=10.1099/0022-1317-73-11-2887;
RA   Aguado B., Selmes I.P., Smith G.L.;
RT   "Nucleotide sequence of 21.8 kbp of variola major virus strain Harvey and
RT   comparison with vaccinia virus.";
RL   J. Gen. Virol. 73:2887-2902(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Bangladesh-1975;
RX   PubMed=8264798; DOI=10.1038/366748a0;
RA   Massung R.F., Esposito J.J., Liu L.I., Qi J., Utterback T.R., Knight J.C.,
RA   Aubin L., Yuran T.E., Parsons J.M., Loparev V.N., Selivanov N.A.,
RA   Cavallaro K.F., Kerlavage A.R., Mahy B.W.J., Venter J.C.;
RT   "Potential virulence determinants in terminal regions of variola smallpox
RT   virus genome.";
RL   Nature 366:748-751(1993).
CC   -!- FUNCTION: Promotes, when overexpressed, the influx of extracellular
CC       Ca2+, leading to membrane permeability and host cell necrosis.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the chordopoxvirinae A38 protein family.
CC       {ECO:0000305}.
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DR   EMBL; L22579; AAA60893.1; -; Genomic_DNA.
DR   PIR; A72169; A72169.
DR   PIR; T28583; T28583.
DR   RefSeq; NP_042191.1; NC_001611.1.
DR   SMR; P0DST6; -.
DR   GeneID; 1486522; -.
DR   KEGG; vg:1486522; -.
DR   Proteomes; UP000119805; 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; Transmembrane; Transmembrane helix.
FT   CHAIN           1..277
FT                   /note="Protein A38"
FT                   /id="PRO_0000448165"
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"
SQ   SEQUENCE   277 AA;  31595 MW;  16A7AC95E215D57E CRC64;
     MLRVRILLIY LCTFVVITST KTIEYTACND TIIIPCTIDN PTKYIRWKLD NHNILTYNKT
     SKTIILSKWH TSAKLHSLSD NDVSLIIKYK DILPGTYTCE DNTGIKSTVK LVQRHTNWFN
     DHHTMLMFIF TGITLFLLFL EIAYTSISVV FSTNLGILQV FGCIIAMIEL CGAFLFYPSM
     FTLRHIIGLL MMTLPSIFLI ITKVFSFWLL CKLSCAVHLI IYYQLAGYIL TVLGLGLSLK
     ECVDGTLLLS GLGTIMVSEH FSLLFLVCFP STQRDYY