ID   E1168_IXORI             Reviewed;         106 AA.
AC   A0A0K8RCU3;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   11-NOV-2015, sequence version 1.
DT   25-MAY-2022, entry version 7.
DE   RecName: Full=Evasin P1168 {ECO:0000303|PubMed:31167786};
DE   Flags: Precursor;
OS   Ixodes ricinus (Common tick) (Acarus ricinus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX   NCBI_TaxID=34613 {ECO:0000312|EMBL:JAA68901.1};
RN   [1] {ECO:0000312|EMBL:JAA68901.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Salivary gland {ECO:0000312|EMBL:JAA68901.1};
RX   PubMed=23964076; DOI=10.1096/fj.13-232140;
RA   Schwarz A., von Reumont B.M., Erhart J., Chagas A.C., Ribeiro J.M.,
RA   Kotsyfakis M.;
RT   "De novo Ixodes ricinus salivary gland transcriptome analysis using two
RT   next-generation sequencing methodologies.";
RL   FASEB J. 27:4745-4756(2013).
RN   [2] {ECO:0000305}
RP   FUNCTION.
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).
CC   -!- FUNCTION: Salivary chemokine-binding protein which binds to host
CC       chemokines CXCL1, CXCL2 and CXCL8. {ECO:0000269|PubMed:31167786}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR   EMBL; GADI01004907; JAA68901.1; -; mRNA.
DR   AlphaFoldDB; A0A0K8RCU3; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019958; F:C-X-C chemokine binding; IDA:UniProtKB.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..106
FT                   /note="Evasin P1168"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5005517493"
FT   CARBOHYD        48
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        45..67
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E8"
FT   DISULFID        49..69
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E8"
FT   DISULFID        60..80
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E8"
SQ   SEQUENCE   106 AA;  11674 MW;  505C33D10A5B9A65 CRC64;
     MEVKISTFLQ IAVLIVLGIH LIAAGQDTDG KEKSDEYELF TVEYCGTNCT QLENGSWTAC
     TGKNGTCRCF HENDKKVGLC LSTEYTDFSE YPDPNSEEIK AASPLP