ID   EV672_RHIPC             Reviewed;         125 AA.
AC   L7MC74;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2013, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=Evasin P672 {ECO:0000303|PubMed:29487134};
DE   Flags: Precursor;
OS   Rhipicephalus pulchellus (Yellow backed tick) (Dermacentor pulchellus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Rhipicephalinae;
OC   Rhipicephalus; Rhipicephalus.
OX   NCBI_TaxID=72859;
RN   [1] {ECO:0000312|EMBL:JAA60789.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Salivary gland {ECO:0000312|EMBL:JAA60789.1};
RX   PubMed=25576852; DOI=10.1016/j.jprot.2014.12.014;
RA   Tan A.W., Francischetti I.M., Slovak M., Kini R.M., Ribeiro J.M.;
RT   "Sexual differences in the sialomes of the zebra tick, Rhipicephalus
RT   pulchellus.";
RL   J. Proteomics 117:120-144(2015).
RN   [2] {ECO:0000305}
RP   FUNCTION, DOMAIN, AND GLYCOSYLATION AT ASN-35; ASN-55; ASN-65; ASN-104;
RP   ASN-112 AND ASN-118.
RX   PubMed=29487134; DOI=10.1074/jbc.ra117.000487;
RA   Eaton J.R.O., Alenazi Y., Singh K., Davies G., Geis-Asteggiante L.,
RA   Kessler B., Robinson C.V., Kawamura A., Bhattacharya S.;
RT   "The N-terminal domain of a tick evasin is critical for chemokine binding
RT   and neutralization and confers specific binding activity to other
RT   evasins.";
RL   J. Biol. Chem. 293:6134-6146(2018).
CC   -!- FUNCTION: Salivary chemokine-binding protein which has chemokine-
CC       neutralizing activity and binds to host chemokines CCL1, CCL2, CCL3,
CC       CCL3L1, CCL7, CCL8, CCL11, CCL12, CCL13, CCL14, CCL15, CCL16, CCL18 and
CC       CCL23 (PubMed:29487134). Binds to CCL8 with 1:1 stoichiometry and
CC       disrupts CCL8 homodimer formation (PubMed:29487134).
CC       {ECO:0000269|PubMed:29487134}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- DOMAIN: The N-terminal region is required for binding to CCL8.
CC       {ECO:0000269|PubMed:29487134}.
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DR   EMBL; GACK01004245; JAA60789.1; -; mRNA.
DR   AlphaFoldDB; L7MC74; -.
DR   SMR; L7MC74; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019957; F:C-C chemokine binding; IEA:InterPro.
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   Disulfide bond; Glycoprotein; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..125
FT                   /note="Evasin P672"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5003981242"
FT   CARBOHYD        35
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:29487134"
FT   CARBOHYD        55
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:29487134"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:29487134"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        78
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:29487134"
FT   CARBOHYD        112
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:29487134"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:29487134"
FT   DISULFID        70..110
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E7"
FT   DISULFID        87..115
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E7"
FT   DISULFID        105..124
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E7"
SQ   SEQUENCE   125 AA;  13925 MW;  FB7C0B3FD768FB0A CRC64;
     MAHKIAIGLV CVLYALHIMS AVCEVSEQEG VGEDNATEDE DYEDFFKPVT CYFANSTVGP
     LRPPNCTVVC TNNTAWWNDT KSDGGHCYSE YRPEKRTHSR EIYNCTIGVC GNGTCIANHT
     YADCW