EV985_AMBPA
ID EV985_AMBPA Reviewed; 132 AA.
AC A0A023FT45;
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 P985 {ECO:0000303|PubMed:28655871};
DE Flags: Precursor;
OS Amblyomma parvum (South American tick).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Amblyomminae; Amblyomma.
OX NCBI_TaxID=251391;
RN [1] {ECO:0000312|EMBL:JAC24842.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Araguapaz {ECO:0000312|EMBL:JAC24842.1};
RC TISSUE=Salivary gland {ECO:0000312|EMBL:JAC24842.1};
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 chemokine CCL5. {ECO:0000269|PubMed:28655871}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR EMBL; GBBL01002478; JAC24842.1; -; mRNA.
DR AlphaFoldDB; A0A023FT45; -.
DR SMR; A0A023FT45; -.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..132
FT /note="Evasin P985"
FT /evidence="ECO:0000255"
FT /id="PRO_5001520201"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 74
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 CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 48..70
FT /evidence="ECO:0000250|UniProtKB:P0C8E7"
FT DISULFID 66..109
FT /evidence="ECO:0000250|UniProtKB:P0C8E7"
FT DISULFID 83..114
FT /evidence="ECO:0000250|UniProtKB:P0C8E7"
FT DISULFID 104..123
FT /evidence="ECO:0000250|UniProtKB:P0C8E7"
SQ SEQUENCE 132 AA; 14165 MW; 859A0BEDEB5A9B0B CRC64;
MHSTIAYVSL LPLALFVAMH GASTDEESEE LGASTDVDYE ELDANCTCPA PALTSTRNNK
HYPLGCIYNC SSYNCTIPDG TPCYVLTLGE VKEHLQIGST VPNCTCGLCR NGTCVSNGTV
EECFAVEEIE ET