A38_VACCC
ID A38_VACCC Reviewed; 277 AA.
AC P21061;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Protein A38;
GN ORFNames=A38L;
OS Vaccinia virus (strain Copenhagen) (VACV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10249;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2;
RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA Paoletti E.;
RT "The complete DNA sequence of vaccinia virus.";
RL Virology 179:247-266(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA Paoletti E.;
RT "Appendix to 'The complete DNA sequence of vaccinia virus'.";
RL Virology 179:517-563(1990).
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; M35027; AAA48168.1; -; Genomic_DNA.
DR PIR; D42521; D42521.
DR SMR; P21061; -.
DR Proteomes; UP000008269; 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_0000099324"
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; 31563 MW; 1B0903BE1D351E3C CRC64;
MSRVRISLIY LYTLVVITTT KTIEYTACND TIIIPCTIDN PTKYIRWKLD NHDILTYNKT
SKTTILSKWH TSARLHSLSD SDVSLIIEYK DILPGTYTCE DNTGIKSTVK LVQLHTNWFN
DYQTMLMFIF TGITLFLLFL EITYTSISVV FSTNLGILQV FGCVIAMIEL CGAFLFYPSM
FTLRHIIGLL MMTLPSIFLI ITKVFSFWLL CKLSCAVHLI IYYQLAGYIL TVLGLGLSLK
ECVDGTLLLS GLGTIMVSEH FSLLFLVCFP STQRDYY