VMI2_HHV8P
ID VMI2_HHV8P Reviewed; 94 AA.
AC Q98157; D0UZM1; Q2HRC3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Viral macrophage inflammatory protein 2;
DE AltName: Full=Viral macrophage inflammatory protein II;
DE Short=vMIP-II;
DE AltName: Full=vMIP-1B;
DE Flags: Precursor;
GN Name=ORF K4;
OS Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's
OS sarcoma-associated herpesvirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=868565;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Nicholas J., Ruvolo V.R., Burns W.H., Sandford G., Wan X., Ciufo D.,
RA Hendrickson S., Guo H.G., Hayward G.S., Reitz M.S.;
RT "Kaposi's sarcoma-associated human herpesvirus-8 encodes homologs of
RT macrophage inflammatory protein-1 and interleukin-6.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8939871; DOI=10.1126/science.274.5293.1739;
RA Moore P.S., Bashoff C., Weiss R.A., Chang Y.;
RT "Molecular mimicry of human cytokine and cytokine response pathway genes by
RT KSHV.";
RL Science 274:1739-1744(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8962146; DOI=10.1073/pnas.93.25.14862;
RA Russo J.J., Bohenzky R.A., Chien M.-C., Chen J., Yan M., Maddalena D.,
RA Parry J.P., Peruzzi D., Edelman I.S., Chang Y., Moore P.S.;
RT "Nucleotide sequence of the Kaposi sarcoma-associated herpesvirus (HHV8).";
RL Proc. Natl. Acad. Sci. U.S.A. 93:14862-14867(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Sun R., Lin S.-F., Miller G.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16760382; DOI=10.1099/vir.0.81919-0;
RA Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
RT "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview.";
RL J. Gen. Virol. 87:1781-1804(2006).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=11041848; DOI=10.1021/bi001166f;
RA Fernandez E.J., Wilken J., Thompson D.A., Peiper S.C., Lolis E.;
RT "Comparison of the structure of vMIP-II with eotaxin-1, RANTES, and MCP-3
RT suggests a unique mechanism for CCR3 activation.";
RL Biochemistry 39:12837-12844(2000).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=10595530; DOI=10.1110/ps.8.11.2270;
RA Liwang A.C., Wang Z.-X., Sun Y., Peiper S.C., Liwang P.J.;
RT "The solution structure of the anti-HIV chemokine vMIP-II.";
RL Protein Sci. 8:2270-2280(1999).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 24-94 IN COMPLEX WITH HUMAN
RP CXCR4, AND INTERACTION WITH HOST CXCR4.
RX PubMed=25612609; DOI=10.1126/science.1261064;
RA Qin L., Kufareva I., Holden L.G., Wang C., Zheng Y., Zhao C., Fenalti G.,
RA Wu H., Han G.W., Cherezov V., Abagyan R., Stevens R.C., Handel T.M.;
RT "Structural biology. Crystal structure of the chemokine receptor CXCR4 in
RT complex with a viral chemokine.";
RL Science 347:1117-1122(2015).
CC -!- FUNCTION: Blocks infection by several different human immunodeficiency
CC virus type 1 (HIV-1) strains. This occurs because vMIP-II binds to a
CC wide range of chemokine receptors. May form part of the response to
CC host defenses contributing to virus-induced neoplasia and may have
CC relevance to KSHV and HIV-I interactions.
CC -!- SUBUNIT: Monomer. Interacts with human chemokine receptor CXCR4
CC (PubMed:25612609). {ECO:0000269|PubMed:25612609}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U67775; AAB61702.1; -; Genomic_DNA.
DR EMBL; U75698; AAC57093.1; -; Genomic_DNA.
DR EMBL; U93872; AAB62642.1; -; Genomic_DNA.
DR EMBL; U71365; AAC34941.1; -; Genomic_DNA.
DR EMBL; AF148805; ABD28861.1; -; Genomic_DNA.
DR RefSeq; YP_001129362.1; NC_009333.1.
DR PDB; 1CM9; X-ray; 2.10 A; A/B=21-94.
DR PDB; 1HFF; NMR; -; A=24-33.
DR PDB; 1HFG; NMR; -; A=24-94.
DR PDB; 1HFN; NMR; -; A=24-94.
DR PDB; 1HHV; NMR; -; A=21-94.
DR PDB; 1VMP; NMR; -; A=24-94.
DR PDB; 2FHT; X-ray; 1.70 A; A=24-94.
DR PDB; 2FJ2; X-ray; 2.30 A; A/B/C/D=24-94.
DR PDB; 4RWS; X-ray; 3.10 A; C=24-94.
DR PDBsum; 1CM9; -.
DR PDBsum; 1HFF; -.
DR PDBsum; 1HFG; -.
DR PDBsum; 1HFN; -.
DR PDBsum; 1HHV; -.
DR PDBsum; 1VMP; -.
DR PDBsum; 2FHT; -.
DR PDBsum; 2FJ2; -.
DR PDBsum; 4RWS; -.
DR BMRB; Q98157; -.
DR SMR; Q98157; -.
DR BioGRID; 1777017; 5.
DR DNASU; 4961514; -.
DR GeneID; 4961514; -.
DR KEGG; vg:4961514; -.
DR EvolutionaryTrace; Q98157; -.
DR Proteomes; UP000000942; Genome.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0008009; F:chemokine activity; IEA:InterPro.
DR GO; GO:0045236; F:CXCR chemokine receptor binding; IPI:CAFA.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR InterPro; IPR039809; Chemokine_b/g/d.
DR InterPro; IPR000827; Chemokine_CC_CS.
DR InterPro; IPR001811; Chemokine_IL8-like_dom.
DR InterPro; IPR036048; Interleukin_8-like_sf.
DR PANTHER; PTHR12015; PTHR12015; 1.
DR Pfam; PF00048; IL8; 1.
DR SMART; SM00199; SCY; 1.
DR SUPFAM; SSF54117; SSF54117; 1.
DR PROSITE; PS00472; SMALL_CYTOKINES_CC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytokine; Disulfide bond; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..20
FT CHAIN 21..94
FT /note="Viral macrophage inflammatory protein 2"
FT /id="PRO_0000005245"
FT DISULFID 34..58
FT DISULFID 35..74
FT TURN 25..29
FT /evidence="ECO:0007829|PDB:4RWS"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1CM9"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:2FHT"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:2FHT"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:2FHT"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:2FHT"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1HFG"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:2FHT"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:2FHT"
SQ SEQUENCE 94 AA; 10486 MW; 44F749BED18DD128 CRC64;
MDTKGILLVA VLTALLCLQS GDTLGASWHR PDKCCLGYQK RPLPQVLLSS WYPTSQLCSK
PGVIFLTKRG RQVCADKSKD WVKKLMQQLP VTAR