ID   E1077_IXORI             Reviewed;          91 AA.
AC   A0A090XE98;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   26-NOV-2014, sequence version 1.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=Evasin P1077 {ECO:0000303|PubMed:31167786};
DE   Flags: Precursor; Fragment;
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:JAC92493.1};
RN   [1] {ECO:0000312|EMBL:JAC92493.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=25970599; DOI=10.1371/journal.pntd.0003754;
RA   Kotsyfakis M., Kopacek P., Franta Z., Pedra J.H., Ribeiro J.M.;
RT   "Deep Sequencing Analysis of the Ixodes ricinus Haemocytome.";
RL   PLoS Negl. Trop. Dis. 9:e0003754-e0003754(2015).
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, CXCL3, CXCL5, CXCL6 and CXCL11.
CC       {ECO:0000269|PubMed:31167786}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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   EMBL; GBIH01002217; JAC92493.1; -; mRNA.
DR   AlphaFoldDB; A0A090XE98; -.
DR   SMR; A0A090XE98; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019958; F:C-X-C chemokine binding; IDA:UniProtKB.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Secreted; Signal.
FT   SIGNAL          <1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..91
FT                   /note="Evasin P1077"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5001869146"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        69
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        43..62
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E8"
FT   DISULFID        47..64
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E8"
FT   DISULFID        58..75
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E8"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:JAC92493.1"
SQ   SEQUENCE   91 AA;  9653 MW;  00E87C642724C033 CRC64;
     KVKTFAFLQI VVLIALSLHL ASAGSKQLIG PQSSTNSIKA EFCDTNCTAG TNGIWNGCSG
     DCFCTHVGNS TEGRCMKITG FDEYPTSEAE E