ID   EVA3_RHISA              Reviewed;          86 AA.
AC   P0C8E8;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=Evasin-3 {ECO:0000303|PubMed:18678732, ECO:0000303|PubMed:31167786, ECO:0000303|PubMed:31235521};
DE            Short=EVA3 {ECO:0000303|PubMed:31167786};
DE   Flags: Precursor;
OS   Rhipicephalus sanguineus (Brown dog tick) (Ixodes sanguineus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Rhipicephalinae;
OC   Rhipicephalus; Rhipicephalus.
OX   NCBI_TaxID=34632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, SUBUNIT, AND
RP   FUNCTION.
RC   TISSUE=Salivary gland;
RX   PubMed=18678732; DOI=10.1084/jem.20072689;
RA   Deruaz M., Frauenschuh A., Alessandri A.L., Dias J.M., Coelho F.M.,
RA   Russo R.C., Ferreira B.R., Graham G.J., Shaw J.P., Wells T.N.C.,
RA   Teixeira M.M., Power C.A., Proudfoot A.E.I.;
RT   "Ticks produce highly selective chemokine binding proteins with
RT   antiinflammatory activity.";
RL   J. Exp. Med. 205:2019-2031(2008).
RN   [2] {ECO:0007744|PDB:6I31}
RP   X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 21-86, FUNCTION, AND DISULFIDE
RP   BONDS.
RX   PubMed=31167786; DOI=10.1074/jbc.ra119.008817;
RA   Lee A.W., Deruaz M., Lynch C., Davies G., Singh K., Alenazi Y.,
RA   Eaton J.R.O., Kawamura A., Shaw J., Proudfoot A.E.I., Dias J.M.,
RA   Bhattacharya S.;
RT   "A knottin scaffold directs the CXC-chemokine-binding specificity of tick
RT   evasins.";
RL   J. Biol. Chem. 294:11199-11212(2019).
RN   [3] {ECO:0007744|PDB:6QJB}
RP   STRUCTURE BY NMR OF 37-76, FUNCTION, AND DISULFIDE BONDS.
RX   PubMed=31235521; DOI=10.1074/jbc.ra119.008902;
RA   Denisov S.S., Ippel J.H., Heinzmann A.C.A., Koenen R.R., Ortega-Gomez A.,
RA   Soehnlein O., Hackeng T.M., Dijkgraaf I.;
RT   "Tick saliva protein Evasin-3 modulates chemotaxis by disrupting CXCL8
RT   interactions with glycosaminoglycans and CXCR2.";
RL   J. Biol. Chem. 294:12370-12379(2019).
CC   -!- FUNCTION: Salivary chemokine-binding protein which shows chemokine
CC       neutralizing activity and binds to host chemokines CXCL1, CXCL2, CXCL3,
CC       CXCL5, CXCL6 and CXCL8 (PubMed:18678732, PubMed:31167786,
CC       PubMed:31235521). Binds to CXCL8 with 1:1 stoichiometry
CC       (PubMed:31235521). Disrupts CXCL8 homodimer formation, disrupts the
CC       glycosaminoglycan-binding site of CXCL8 and inhibits the interaction of
CC       CXCL8 with CXCR2 (PubMed:31235521). {ECO:0000269|PubMed:18678732,
CC       ECO:0000269|PubMed:31167786, ECO:0000269|PubMed:31235521}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18678732}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Hidden powers - Issue 99 of
CC       November 2008;
CC       URL="https://web.expasy.org/spotlight/back_issues/099";
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DR   PDB; 6I31; X-ray; 1.79 A; A/B=21-86.
DR   PDB; 6QJB; NMR; -; A=37-76.
DR   PDBsum; 6I31; -.
DR   PDBsum; 6QJB; -.
DR   AlphaFoldDB; P0C8E8; -.
DR   BMRB; P0C8E8; -.
DR   SMR; P0C8E8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019958; F:C-X-C chemokine binding; IDA:UniProtKB.
DR   GO; GO:1900137; P:negative regulation of chemokine activity; IDA:UniProtKB.
DR   GO; GO:0090074; P:negative regulation of protein homodimerization activity; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:18678732"
FT   CHAIN           21..86
FT                   /note="Evasin-3"
FT                   /id="PRO_0000354058"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        76
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        42..57
FT                   /evidence="ECO:0000269|PubMed:31167786,
FT                   ECO:0000269|PubMed:31235521, ECO:0007744|PDB:6I31,
FT                   ECO:0007744|PDB:6QJB"
FT   DISULFID        46..59
FT                   /evidence="ECO:0000269|PubMed:31167786,
FT                   ECO:0000269|PubMed:31235521, ECO:0007744|PDB:6I31,
FT                   ECO:0007744|PDB:6QJB"
FT   DISULFID        53..70
FT                   /evidence="ECO:0000269|PubMed:31167786,
FT                   ECO:0000269|PubMed:31235521, ECO:0007744|PDB:6I31,
FT                   ECO:0007744|PDB:6QJB"
FT   HELIX           34..36
FT                   /evidence="ECO:0007829|PDB:6I31"
FT   STRAND          37..47
FT                   /evidence="ECO:0007829|PDB:6I31"
FT   TURN            48..50
FT                   /evidence="ECO:0007829|PDB:6QJB"
FT   STRAND          58..60
FT                   /evidence="ECO:0007829|PDB:6I31"
FT   STRAND          66..75
FT                   /evidence="ECO:0007829|PDB:6I31"
SQ   SEQUENCE   86 AA;  9145 MW;  7FD0823DD19450D4 CRC64;
     MRALLARLLL CVLVVSDSKG LVSTIESRTS GDGADNFDVV SCNKNCTSGQ NECPEGCFCG
     LLGQNKKGHC YKIIGNLSGE PPVVRR
//