IL10H_EBVB9
ID IL10H_EBVB9 Reviewed; 170 AA.
AC P03180; Q777H2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Viral interleukin-10 homolog;
DE Short=vIL-10;
DE AltName: Full=20 kDa protein;
DE AltName: Full=Protein BCRF1;
DE Flags: Precursor;
GN ORFNames=BCRF1;
OS Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=10377;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6087149; DOI=10.1038/310207a0;
RA Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J.,
RA Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C.,
RA Tuffnell P.S., Barrell B.G.;
RT "DNA sequence and expression of the B95-8 Epstein-Barr virus genome.";
RL Nature 310:207-211(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2998073; DOI=10.1016/0042-6822(85)90229-6;
RA Hudson G.S., Bankier A.T., Satchwell S.C., Barrell B.G.;
RT "The short unique region of the B95-8 Epstein-Barr virus genome.";
RL Virology 147:81-98(1985).
RN [3]
RP FUNCTION.
RX PubMed=2161559; DOI=10.1126/science.2161559;
RA Moore K.W., Vieira P., Fiorentino D.F., Trounstine M.L., Khan T.A.,
RA Mosmann T.R.;
RT "Homology of cytokine synthesis inhibitory factor (IL-10) to the Epstein-
RT Barr virus gene BCRFI.";
RL Science 248:1230-1234(1990).
RN [4]
RP FUNCTION.
RX PubMed=9310490;
RA Zeidler R., Eissner G., Meissner P., Uebel S., Tampe R., Lazis S.,
RA Hammerschmidt W.;
RT "Downregulation of TAP1 in B lymphocytes by cellular and Epstein-Barr
RT virus-encoded interleukin-10.";
RL Blood 90:2390-2397(1997).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=9159483; DOI=10.1006/jmbi.1997.0990;
RA Zdanov A., Schalk-Hihi C., Menon S., Moore K.W., Wlodawer A.;
RT "Crystal structure of Epstein-Barr virus protein BCRF1, a homolog of
RT cellular interleukin-10.";
RL J. Mol. Biol. 268:460-467(1997).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 26-170 IN COMPLEX WITH HUMAN
RP IL10R1.
RX PubMed=15837194; DOI=10.1016/j.str.2005.01.016;
RA Yoon S.I., Jones B.C., Logsdon N.J., Walter M.R.;
RT "Same structure, different function crystal structure of the Epstein-Barr
RT virus IL-10 bound to the soluble IL-10R1 chain.";
RL Structure 13:551-564(2005).
CC -!- FUNCTION: Plays a role in masking infected cells for immune recognition
CC by cytotoxic T-lymphocytes. Down-regulates the expression of the host
CC TAP1 gene (transporter associated with antigen processing), thereby
CC affecting the transport of peptides into the endoplasmic reticulum and
CC subsequent peptide loading by MHC class I molecules. Inhibits IFN-gamma
CC synthesis. {ECO:0000269|PubMed:2161559, ECO:0000269|PubMed:9310490}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15837194}.
CC -!- INTERACTION:
CC P03180; Q13651: IL10RA; Xeno; NbExp=4; IntAct=EBI-1042167, EBI-1031656;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the IL-10 family. {ECO:0000305}.
CC -!- CAUTION: Be careful of the possible confusion between BCRF1 with BcRF1.
CC {ECO:0000305}.
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DR EMBL; V01555; CAA24863.1; -; Genomic_DNA.
DR EMBL; M11924; AAA45900.1; -; Genomic_DNA.
DR EMBL; AJ507799; CAD53385.1; -; Genomic_DNA.
DR PIR; A03741; QQBE2.
DR RefSeq; YP_401634.1; NC_007605.1.
DR PDB; 1VLK; X-ray; 1.90 A; A=26-170.
DR PDB; 1Y6M; X-ray; 2.80 A; L=26-170.
DR PDB; 1Y6N; X-ray; 2.70 A; L=26-170.
DR PDBsum; 1VLK; -.
DR PDBsum; 1Y6M; -.
DR PDBsum; 1Y6N; -.
DR SMR; P03180; -.
DR DIP; DIP-35519N; -.
DR IntAct; P03180; 1.
DR PRIDE; P03180; -.
DR DNASU; 3783689; -.
DR GeneID; 3783689; -.
DR KEGG; vg:3783689; -.
DR EvolutionaryTrace; P03180; -.
DR Proteomes; UP000153037; Genome.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0001817; P:regulation of cytokine production; IEA:UniProt.
DR Gene3D; 1.20.1250.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR000098; IL-10.
DR InterPro; IPR020443; IL-10/19/20/22/24/26_fam.
DR InterPro; IPR020423; IL-10_CS.
DR Pfam; PF00726; IL10; 1.
DR PRINTS; PR01294; INTRLEUKIN10.
DR SMART; SM00188; IL10; 1.
DR SUPFAM; SSF47266; SSF47266; 1.
DR PROSITE; PS00520; INTERLEUKIN_10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytokine; Disulfide bond;
KW Evasion of host immunity by viral interleukin-like protein; Glycoprotein;
KW Host-virus interaction; Reference proteome; Secreted; Signal;
KW Viral immunoevasion.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..170
FT /note="Viral interleukin-10 homolog"
FT /id="PRO_0000015375"
FT COILED 97..145
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 27..119
FT DISULFID 73..125
FT TURN 30..33
FT /evidence="ECO:0007829|PDB:1VLK"
FT HELIX 34..45
FT /evidence="ECO:0007829|PDB:1VLK"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:1VLK"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:1Y6N"
FT HELIX 61..68
FT /evidence="ECO:0007829|PDB:1VLK"
FT HELIX 72..85
FT /evidence="ECO:0007829|PDB:1VLK"
FT HELIX 87..94
FT /evidence="ECO:0007829|PDB:1VLK"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:1VLK"
FT HELIX 99..118
FT /evidence="ECO:0007829|PDB:1VLK"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:1VLK"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:1VLK"
FT HELIX 130..141
FT /evidence="ECO:0007829|PDB:1VLK"
FT HELIX 143..152
FT /evidence="ECO:0007829|PDB:1VLK"
FT HELIX 154..166
FT /evidence="ECO:0007829|PDB:1VLK"
SQ SEQUENCE 170 AA; 19914 MW; AE20AE65D358F0CE CRC64;
MERRLVVTLQ CLVLLYLAPE CGGTDQCDNF PQMLRDLRDA FSRVKTFFQT KDEVDNLLLK
ESLLEDFKGY LGCQALSEMI QFYLEEVMPQ AENQDPEAKD HVNSLGENLK TLRLRLRRCH
RFLPCENKSK AVEQIKNAFN KLQEKGIYKA MSEFDIFINY IEAYMTIKAR
