ID   E1243_AMBAM             Reviewed;         123 AA.
AC   A0A0C9S461;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2015, sequence version 1.
DT   25-MAY-2022, entry version 8.
DE   RecName: Full=Evasin P1243 {ECO:0000303|PubMed:29679010};
DE   Flags: Precursor;
OS   Amblyomma americanum (Lone star tick).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Amblyomminae; Amblyomma.
OX   NCBI_TaxID=6943 {ECO:0000312|EMBL:JAG91989.1};
RN   [1] {ECO:0000312|EMBL:JAG91989.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Salivary gland {ECO:0000312|EMBL:JAG91989.1};
RX   PubMed=26131772; DOI=10.1371/journal.pone.0131292;
RA   Karim S., Ribeiro J.M.;
RT   "An Insight into the Sialome of the Lone Star Tick, Amblyomma americanum,
RT   with a Glimpse on Its Time Dependent Gene Expression.";
RL   PLoS ONE 10:e0131292-e0131292(2015).
RN   [2] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=29679010; DOI=10.1038/s41598-018-24568-9;
RA   Alenazi Y., Singh K., Davies G., Eaton J.R.O., Elders P., Kawamura A.,
RA   Bhattacharya S.;
RT   "Genetically engineered two-warhead evasins provide a method to achieve
RT   precision targeting of disease-relevant chemokine subsets.";
RL   Sci. Rep. 8:6333-6333(2018).
CC   -!- FUNCTION: Salivary chemokine-binding protein which has chemokine-
CC       neutralizing activity and binds to host chemokines CCL1, CCL3, CCL3L1,
CC       CCL4, CCL4L1, CCL5, CCL7, CCL8, CCL13, CCL14, CCL15, CCL16, CCL17,
CC       CCL18, CCL19, CCL20, CCL21, CCL22, CCL23, CCL24, CCL27, XCL1, CX3CL1,
CC       CXCL1, CXCL2, CXCL4, CXCL5, CXCL6, CXCL7, CXCL9, CXCL12 and CXCL14.
CC       {ECO:0000269|PubMed:29679010}.
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; GBZX01000751; JAG91989.1; -; mRNA.
DR   AlphaFoldDB; A0A0C9S461; -.
DR   SMR; A0A0C9S461; -.
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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..123
FT                   /note="Evasin P1243"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5002219583"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        32
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        55
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   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        46..68
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E7"
FT   DISULFID        64..105
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E7"
FT   DISULFID        81..110
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E7"
FT   DISULFID        100..119
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E7"
SQ   SEQUENCE   123 AA;  13436 MW;  A5940F39A4AAFE71 CRC64;
     MHSTIAYVFV SALALFAALH GSTSARNHTE DNSTEYYDYE EARCACPARH LNNTNGTVLK
     LLGCHYFCNG TLCTAPDGYP CYNLTAQQVR TLTTYPNTSC AVGVCMKGTC VKNGTMEQCF
     KTP