ID   EV974_AMBCJ             Reviewed;         118 AA.
AC   A0A023FDY8;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   11-JUN-2014, sequence version 1.
DT   03-AUG-2022, entry version 11.
DE   RecName: Full=Evasin P974 {ECO:0000303|PubMed:28655871};
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:JAC18993.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Uberlandia {ECO:0000312|EMBL:JAC18993.1};
RC   TISSUE=Salivary gland {ECO:0000312|EMBL:JAC18993.1};
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=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 CCL1, CCL3, CCL4, CCL8, CCL17, CCL18 and CCL22.
CC       {ECO:0000269|PubMed:28655871}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR   EMBL; GBBK01005489; JAC18993.1; -; mRNA.
DR   PDB; 7S4N; X-ray; 1.65 A; A/C=30-114.
DR   PDB; 7S58; X-ray; 1.82 A; A/B/C/D=30-114.
DR   PDB; 7S59; X-ray; 2.39 A; 1/3=30-114.
DR   PDB; 7SO0; X-ray; 1.74 A; A=30-114.
DR   PDBsum; 7S4N; -.
DR   PDBsum; 7S58; -.
DR   PDBsum; 7S59; -.
DR   PDBsum; 7SO0; -.
DR   AlphaFoldDB; A0A023FDY8; -.
DR   SMR; A0A023FDY8; -.
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   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Glycoprotein; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..118
FT                   /note="Evasin P974"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5001514896"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        38..59
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E7"
FT   DISULFID        55..96
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E7"
FT   DISULFID        72..101
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E7"
FT   DISULFID        91..110
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E7"
SQ   SEQUENCE   118 AA;  13277 MW;  2FA18D2563BD53D4 CRC64;
     MKVLLCIAAS CLMLLALNVS AENTQQEEQD YDYGTDTCPF PVLANKTNKA KFVGCHQKCN
     GGDQKLTDGT ACYVVERKVW DRMTPMLWYE CPLGECKNGV CEDLRKKEDC RKGNGEEK