ID EVA1_RHISA Reviewed; 114 AA. AC P0C8E7; DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 1. DT 22-FEB-2023, entry version 27. DE RecName: Full=Evasin-1 {ECO:0000303|PubMed:17640866, ECO:0000303|PubMed:18678732, ECO:0000303|PubMed:25266725}; DE Short=EVA1 {ECO:0000250|UniProtKB:P0C8E8, ECO:0000305}; 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=17640866; DOI=10.1074/jbc.m704706200; RA Frauenschuh A., Power C.A., Deruaz M., Ferreira B.R., Silva J.S., RA Teixeira M.M., Dias J.M., Martin T., Wells T.N.C., Proudfoot A.E.I.; RT "Molecular cloning and characterization of a highly selective chemokine- RT binding protein from the tick Rhipicephalus sanguineus."; RL J. Biol. Chem. 282:27250-27258(2007). RN [2] RP FUNCTION. 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 [3] RP FUNCTION, AND MUTAGENESIS OF ASP-23; GLU-24; ASP-25; TYR-26; ASP-28; RP PHE-34; GLU-58; ASN-108; TRP-109 AND ARG-110. RX PubMed=25266725; DOI=10.1074/jbc.m114.599233; RA Bonvin P., Dunn S.M., Rousseau F., Dyer D.P., Shaw J., Power C.A., RA Handel T.M., Proudfoot A.E.; RT "Identification of the pharmacophore of the CC chemokine-binding proteins RT Evasin-1 and -4 using phage display."; RL J. Biol. Chem. 289:31846-31855(2014). RN [4] {ECO:0007744|PDB:3FPR, ECO:0007744|PDB:3FPT, ECO:0007744|PDB:3FPU} RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 21-114 IN COMPLEX WITH HUMAN RP CCL3, FUNCTION, DOMAIN, GLYCOSYLATION AT ASN-39 AND ASN-62, AND DISULFIDE RP BONDS. RX PubMed=20041127; DOI=10.1371/journal.pone.0008514; RA Dias J.M., Losberger C., Deruaz M., Power C.A., Proudfoot A.E., Shaw J.P.; RT "Structural basis of chemokine sequestration by a tick chemokine binding RT protein: the crystal structure of the complex between Evasin-1 and CCL3."; RL PLoS ONE 4:e8514-e8514(2009). CC -!- FUNCTION: Salivary chemokine-binding protein which shows chemokine CC neutralizing activity and binds to host chemokines CCL3, CCL4 and CCL18 CC (PubMed:17640866, PubMed:18678732, PubMed:25266725, PubMed:20041127). CC Binds to CCL3 with 1:1 stoichiometry (PubMed:20041127). CC {ECO:0000269|PubMed:17640866, ECO:0000269|PubMed:18678732, CC ECO:0000269|PubMed:20041127, ECO:0000269|PubMed:25266725}. CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17640866}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. CC -!- DOMAIN: Both the N- and C-termini are required for chemokine-binding. CC {ECO:0000269|PubMed:20041127}. CC -!- SIMILARITY: Belongs to the evasin C8 family. {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"; 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 PDB; 3FPR; X-ray; 1.63 A; A/D=21-114. DR PDB; 3FPT; X-ray; 2.70 A; A/B/C=21-114. DR PDB; 3FPU; X-ray; 1.76 A; A=21-114. DR PDBsum; 3FPR; -. DR PDBsum; 3FPT; -. DR PDBsum; 3FPU; -. DR AlphaFoldDB; P0C8E7; -. DR SMR; P0C8E7; -. DR iPTMnet; P0C8E7; -. DR EvolutionaryTrace; P0C8E7; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0019957; F:C-C chemokine binding; IDA:UniProtKB. DR GO; GO:0019956; F:chemokine binding; IDA:UniProtKB. DR GO; GO:1900137; P:negative regulation of chemokine activity; IDA:UniProtKB. DR Gene3D; 2.30.130.100; -; 1. DR InterPro; IPR045797; EVA_Class_A. DR Pfam; PF19429; EVA_Class_A; 1. 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:17640866" FT CHAIN 21..114 FT /note="Evasin-1" FT /id="PRO_0000354057" FT CARBOHYD 39 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:20041127, FT ECO:0007744|PDB:3FPT" FT CARBOHYD 54 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 62 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:20041127, FT ECO:0007744|PDB:3FPT" FT DISULFID 32..53 FT /evidence="ECO:0000269|PubMed:20041127, FT ECO:0007744|PDB:3FPR, ECO:0007744|PDB:3FPT, FT ECO:0007744|PDB:3FPU" FT DISULFID 49..90 FT /evidence="ECO:0000269|PubMed:20041127, FT ECO:0007744|PDB:3FPR, ECO:0007744|PDB:3FPT, FT ECO:0007744|PDB:3FPU" FT DISULFID 66..95 FT /evidence="ECO:0000269|PubMed:20041127, FT ECO:0007744|PDB:3FPR, ECO:0007744|PDB:3FPT, FT ECO:0007744|PDB:3FPU" FT DISULFID 85..104 FT /evidence="ECO:0000269|PubMed:20041127, FT ECO:0007744|PDB:3FPR, ECO:0007744|PDB:3FPT, FT ECO:0007744|PDB:3FPU" FT MUTAGEN 23 FT /note="D->A: No effect on binding to CCL3." FT /evidence="ECO:0000269|PubMed:25266725" FT MUTAGEN 24 FT /note="E->A: No effect on binding to CCL3." FT /evidence="ECO:0000269|PubMed:25266725" FT MUTAGEN 25 FT /note="D->A: No effect on binding to CCL3." FT /evidence="ECO:0000269|PubMed:25266725" FT MUTAGEN 26 FT /note="Y->A: No effect on binding to CCL3." FT /evidence="ECO:0000269|PubMed:25266725" FT MUTAGEN 28 FT /note="D->A: No effect on binding to CCL3." FT /evidence="ECO:0000269|PubMed:25266725" FT MUTAGEN 34 FT /note="F->A: Significantly reduced binding to CCL3." FT /evidence="ECO:0000269|PubMed:25266725" FT MUTAGEN 58 FT /note="E->A: No effect on binding to CCL3." FT /evidence="ECO:0000269|PubMed:25266725" FT MUTAGEN 108 FT /note="N->A: Significantly reduced binding to CCL3 and FT significantly reduced inhibition of chemokine activity." FT /evidence="ECO:0000269|PubMed:25266725" FT MUTAGEN 109 FT /note="W->A: Significantly reduced binding to CCL3 and FT significantly reduced inhibition of chemokine activity." FT /evidence="ECO:0000269|PubMed:25266725" FT MUTAGEN 110 FT /note="R->A: No effect on binding to CCL3." FT /evidence="ECO:0000269|PubMed:25266725" FT STRAND 25..27 FT /evidence="ECO:0007829|PDB:3FPU" FT STRAND 34..38 FT /evidence="ECO:0007829|PDB:3FPR" FT STRAND 44..47 FT /evidence="ECO:0007829|PDB:3FPR" FT STRAND 49..53 FT /evidence="ECO:0007829|PDB:3FPR" FT STRAND 56..59 FT /evidence="ECO:0007829|PDB:3FPR" FT STRAND 65..67 FT /evidence="ECO:0007829|PDB:3FPR" FT HELIX 70..76 FT /evidence="ECO:0007829|PDB:3FPR" FT STRAND 83..91 FT /evidence="ECO:0007829|PDB:3FPR" FT STRAND 94..105 FT /evidence="ECO:0007829|PDB:3FPR" FT HELIX 109..112 FT /evidence="ECO:0007829|PDB:3FPU" SQ SEQUENCE 114 AA; 12593 MW; 1CDFB331167EE2CF CRC64; MTFKACIAII TALCAMQVIC EDDEDYGDLG GCPFLVAENK TGYPTIVACK QDCNGTTETA PNGTRCFSIG DEGLRRMTAN LPYDCPLGQC SNGDCIPKET YEVCYRRNWR DKKN //