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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}.
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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
 
 
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