ID   EV467_RHIPC             Reviewed;         127 AA.
AC   L7M8Z8;
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 P467 {ECO:0000303|PubMed:28655871};
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:JAA60786.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Salivary gland {ECO:0000312|EMBL:JAA60786.1};
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.
RX   PubMed=28655871; DOI=10.1038/s41598-017-04378-1;
RA   Singh K., Davies G., Alenazi Y., Eaton J.R.O., Kawamura A.,
RA   Bhattacharya S.;
RT   "Yeast surface display identifies a family of evasins from ticks with novel
RT   polyvalent CC chemokine-binding activities.";
RL   Sci. Rep. 7:4267-4267(2017).
CC   -!- FUNCTION: Salivary chemokine-binding protein which binds to host
CC       chemokines CCL1, CCL2, CCL3 and CCL5. {ECO:0000269|PubMed:28655871}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR   EMBL; GACK01004248; JAA60786.1; -; mRNA.
DR   AlphaFoldDB; L7M8Z8; -.
DR   SMR; L7M8Z8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019957; F:C-C chemokine binding; IDA:UniProtKB.
DR   GO; GO:1900137; P:negative regulation of chemokine activity; IEA:InterPro.
DR   InterPro; IPR045797; EVA_Class_A.
DR   Pfam; PF19429; EVA_Class_A; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..127
FT                   /note="Evasin P467"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5003981916"
FT   CARBOHYD        49
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        42..63
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E7"
FT   DISULFID        59..100
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E7"
FT   DISULFID        76..105
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E7"
FT   DISULFID        95..114
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E7"
SQ   SEQUENCE   127 AA;  13691 MW;  BF0972A4BEBB6B53 CRC64;
     MALKACITVI AVVYVVQVVR GAEKSLDSDS SGEDYELWTQ GCPFLVAENR TGFGTTVSCQ
     HNCNGAIEKV PEGEPCYTIG EDGLGRMKLN LPYNCSLGEC SGGVCVPNGR SDVCFKRTWE
     ENNKAMA