EVA1_RHISA
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 25-MAY-2022, entry version 26.
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";
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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 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 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
