E1172_IXORI
ID E1172_IXORI Reviewed; 94 AA.
AC V5I2G9;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 1.
DT 25-MAY-2022, entry version 9.
DE RecName: Full=Evasin P1172 {ECO:0000303|PubMed:31167786};
DE Flags: 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:JAB83717.1};
RN [1] {ECO:0000312|EMBL:JAB83717.1}
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, CXCL2, CXCL5 and CXCL8.
CC {ECO:0000269|PubMed:31167786}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR EMBL; GANP01000751; JAB83717.1; -; mRNA.
DR AlphaFoldDB; V5I2G9; -.
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.
FT CHAIN <1..94
FT /note="Evasin P1172"
FT /id="PRO_0000451413"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 35..54
FT /evidence="ECO:0000250|UniProtKB:P0C8E8"
FT DISULFID 39..56
FT /evidence="ECO:0000250|UniProtKB:P0C8E8"
FT DISULFID 50..67
FT /evidence="ECO:0000250|UniProtKB:P0C8E8"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:JAB83717.1"
SQ SEQUENCE 94 AA; 10434 MW; 359A4A7075C82671 CRC64;
FLLKSQLCYC LFGIELIGAG IHALHEDEIF TVDYCGTNCT KQSNGSWTTC PGNCSCYHED
GKTDGFCLST EYTDFTQFPN LTSEEMDAAT PRPE