EV991_AMBCJ
ID EV991_AMBCJ Reviewed; 136 AA.
AC A0A023FFD0;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 11-JUN-2014, sequence version 1.
DT 25-MAY-2022, entry version 9.
DE RecName: Full=Evasin P991 {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:JAC19654.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Uberlandia {ECO:0000312|EMBL:JAC19654.1};
RC TISSUE=Salivary gland {ECO:0000312|EMBL:JAC19654.1};
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 has chemokine-
CC neutralizing activity and binds to host chemokines CCL2, CCL3, CCL3L1,
CC CCL4, CCL4L1, CCL5, CCL6, CCL7, CCL8, CCL9, CCL11, CCL12, CCL13, CCL14,
CC CCL16, CCL17, CCL18, CCL19, CCL22, CCL23, CCL24 and CCL27.
CC {ECO:0000269|PubMed:28655871}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR EMBL; GBBK01004828; JAC19654.1; -; mRNA.
DR AlphaFoldDB; A0A023FFD0; -.
DR SMR; A0A023FFD0; -.
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; IDA:UniProtKB.
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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..136
FT /note="Evasin P991"
FT /evidence="ECO:0000255"
FT /id="PRO_5001520871"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 64
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 CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 55..77
FT /evidence="ECO:0000250|UniProtKB:P0C8E7"
FT DISULFID 73..114
FT /evidence="ECO:0000250|UniProtKB:P0C8E7"
FT DISULFID 90..119
FT /evidence="ECO:0000250|UniProtKB:P0C8E7"
FT DISULFID 109..128
FT /evidence="ECO:0000250|UniProtKB:P0C8E7"
SQ SEQUENCE 136 AA; 14781 MW; E5C91899C25CBA11 CRC64;
MHSTIVYACL LALAVFVALH GTPLAALAEN GEGTTQPDYD NSTDYYNYED FKCTCPAPHL
NNTNGTVMKP IGCYYTCNVT RCTAPDTYPC YNLTEHQAKN LTTSPTTLCA VGNCDHGICV
PNGTKELCFK APNLEE
