ID   E1174_IXORI             Reviewed;         104 AA.
AC   V5I3C5;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   22-JAN-2014, sequence version 1.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=Evasin P1174 {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:JAB82333.1};
RN   [1] {ECO:0000312|EMBL:JAB82333.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=25765539; DOI=10.1038/srep09103;
RA   Kotsyfakis M., Schwarz A., Erhart J., Ribeiro J.M.;
RT   "Tissue- and time-dependent transcription in Ixodes ricinus salivary glands
RT   and midguts when blood feeding on the vertebrate host.";
RL   Sci. Rep. 5:9103-9103(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 and CXCL8. {ECO:0000269|PubMed:31167786}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR   EMBL; GANP01002135; JAB82333.1; -; mRNA.
DR   AlphaFoldDB; V5I3C5; -.
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..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..104
FT                   /note="Evasin P1174"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5004736597"
FT   REGION          85..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        43
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        49
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        40..59
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E8"
FT   DISULFID        44..61
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E8"
FT   DISULFID        55..72
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E8"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:JAB82333.1"
SQ   SEQUENCE   104 AA;  11646 MW;  E9DF14334106C6BD CRC64;
     LKTFCLFLQI AVFIALGIQI FLCGTDALNN ENELFSVEYC GANCTQQDNG SWTKCKGNCT
     CYHEDGKRYG LCLSTEYTDF TQFPKPTSEE IADASPRPKE TNSH