EV675_IXORI
ID EV675_IXORI Reviewed; 92 AA.
AC A0A0K8R374;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 1.
DT 25-MAY-2022, entry version 8.
DE RecName: Full=Evasin P675 {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:JAA65288.1};
RN [1] {ECO:0000312|EMBL:JAA65288.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Salivary gland {ECO:0000312|EMBL:JAA65288.1};
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, CXCL3, CXCL4, CXCL5, CXCL6, CXCL10, CXCL11 and
CC CXCL13. {ECO:0000269|PubMed:31167786}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR EMBL; GADI01008520; JAA65288.1; -; mRNA.
DR AlphaFoldDB; A0A0K8R374; -.
DR SMR; A0A0K8R374; -.
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..92
FT /note="Evasin P675"
FT /evidence="ECO:0000255"
FT /id="PRO_5005515753"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 44..63
FT /evidence="ECO:0000250|UniProtKB:P0C8E8"
FT DISULFID 48..65
FT /evidence="ECO:0000250|UniProtKB:P0C8E8"
FT DISULFID 59..76
FT /evidence="ECO:0000250|UniProtKB:P0C8E8"
SQ SEQUENCE 92 AA; 9576 MW; F6DA9066C8B0AEA5 CRC64;
MEVKTFAFLQ IAVIIALGLH LAPAGSNQLS GPQSSANSND AVFCDTNCTQ GTDGAWSGCR
GDCFCVHVGN STEGRCIELI GDFDYSTPGA ED