ID   E1182_AMBMU             Reviewed;         115 AA.
AC   G3MJ83;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   02-DEC-2020, sequence version 2.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Evasin P1182 {ECO:0000303|PubMed:28655871};
DE   Flags: Precursor;
OS   Amblyomma maculatum (Gulf Coast tick).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Amblyomminae; Amblyomma.
OX   NCBI_TaxID=34609;
RN   [1] {ECO:0000312|EMBL:AEO33551.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Salivary gland {ECO:0000312|EMBL:AEO33551.1};
RX   PubMed=22216098; DOI=10.1371/journal.pone.0028525;
RA   Karim S., Singh P., Ribeiro J.M.;
RT   "A deep insight into the sialotranscriptome of the gulf coast tick,
RT   Amblyomma maculatum.";
RL   PLoS ONE 6:E28525-E28525(2011).
RN   [2] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=28655871; DOI=10.1038/s41598-017-04378-1;
RA   Singh K., Davies G., Alenazi Y., Eaton J.R.O., Kawamura A.,
RA   Bhattacharya S.;
RT   "Yeast surface display identifies a family of evasins from ticks with novel
RT   polyvalent CC chemokine-binding activities.";
RL   Sci. Rep. 7:4267-4267(2017).
CC   -!- FUNCTION: Salivary chemokine-binding protein which binds to host
CC       chemokines CCL2, CCL3, CCL4, CCL8 and CCL18.
CC       {ECO:0000269|PubMed:28655871}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AEO33551.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; JO841934; AEO33551.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; G3MJ83; -.
DR   SMR; G3MJ83; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019957; F:C-C chemokine binding; IDA:UniProtKB.
DR   GO; GO:1900137; P:negative regulation of chemokine activity; IEA:InterPro.
DR   InterPro; IPR045797; EVA_Class_A.
DR   Pfam; PF19429; EVA_Class_A; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..115
FT                   /note="Evasin P1182"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000451308"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        38..58
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E7"
FT   DISULFID        54..94
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E7"
FT   DISULFID        70..99
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E7"
FT   DISULFID        89..108
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E7"
SQ   SEQUENCE   115 AA;  12702 MW;  2E42161DB8F8BC72 CRC64;
     MALNWSFRVI FVSTMWCALL KFATLGEPKD DNDYGGGCPF VVLGNGTHAK PAGCSHLCNG
     APETLDNIEC YNVTEEVAKR MTPGIPYACW LGWCNKGECK RGNRTEVCYR GSEEE