ID   E1142_AMBCJ             Reviewed;          97 AA.
AC   A0A023FBW4;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   11-JUN-2014, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=Evasin P1142 {ECO:0000303|PubMed:31167786};
DE   Flags: Precursor;
OS   Amblyomma cajennense (Cayenne tick) (Acarus cajennensis).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Amblyomminae; Amblyomma.
OX   NCBI_TaxID=34607;
RN   [1] {ECO:0000312|EMBL:JAC18880.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Uberlandia {ECO:0000312|EMBL:JAC18880.1};
RC   TISSUE=Salivary gland {ECO:0000312|EMBL:JAC18880.1};
RX   PubMed=25201527; DOI=10.1186/1756-3305-7-430;
RA   Garcia G.R., Gardinassi L.G., Ribeiro J.M., Anatriello E., Ferreira B.R.,
RA   Moreira H.N., Mafra C., Martins M.M., Szabo M.P., de Miranda-Santos I.K.,
RA   Maruyama S.R.;
RT   "The sialotranscriptome of Amblyomma triste, Amblyomma parvum and Amblyomma
RT   cajennense ticks, uncovered by 454-based RNA-seq.";
RL   Parasit. Vectors 7:430-430(2014).
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, CXCL7, CXCL10 and
CC       CXCL11. {ECO:0000269|PubMed:31167786}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR   EMBL; GBBK01005602; JAC18880.1; -; mRNA.
DR   AlphaFoldDB; A0A023FBW4; -.
DR   SMR; A0A023FBW4; -.
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..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..97
FT                   /note="Evasin P1142"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5001519635"
FT   CARBOHYD        55
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        78
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        46..62
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E8"
FT   DISULFID        50..64
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E8"
FT   DISULFID        58..76
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E8"
SQ   SEQUENCE   97 AA;  10328 MW;  B6182A6463E1F760 CRC64;
     MTSHGAVKIA IFAVIALHSI FECLSKPQIL QRTDHSTDSD WDPQMCPETC NPSKNISCSS
     ECLCVTLGGG DETGTCFNMS GVDWLGHAQA SDGHNDG