E1156_IXORI
ID E1156_IXORI Reviewed; 108 AA.
AC V5HBW0;
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 P1156 {ECO:0000303|PubMed:29679010};
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:JAB72437.1};
RN [1] {ECO:0000312|EMBL:JAB72437.1}
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=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 CXCL1, CXCL2, CXCL3,
CC CXCL5, CXCL6 and CXCL8. {ECO:0000269|PubMed:29679010}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR EMBL; GANP01012031; JAB72437.1; -; mRNA.
DR AlphaFoldDB; V5HBW0; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0019956; F:chemokine binding; IDA:UniProtKB.
DR GO; GO:1900137; P:negative regulation of chemokine activity; IDA:UniProtKB.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..108
FT /note="Evasin P1156"
FT /evidence="ECO:0000255"
FT /id="PRO_5004735646"
FT REGION 89..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 41..63
FT /evidence="ECO:0000250|UniProtKB:P0C8E8"
FT DISULFID 45..65
FT /evidence="ECO:0000250|UniProtKB:P0C8E8"
FT DISULFID 56..76
FT /evidence="ECO:0000250|UniProtKB:P0C8E8"
SQ SEQUENCE 108 AA; 11969 MW; 1941C7C73D78ECD4 CRC64;
MEVKTYAFLQ IAVFIFLGMQ IFASLTDAAD DDNELFTVQY CGMNCTKDEG GTWTGCTGKK
EGCKCYHESG KNYGLCLSTE YTDFSQYGNP SDSEIEAAKP KRSDTLSH