Reviewed, UniProtKB/Swiss-Prot P0C8E7 (EVA1_RHISA)

Names and origin

Protein names	Recommended name:     Evasin-1
Organism	Rhipicephalus sanguineus (Brown dog tick)
Taxonomic identifier	34632 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Arthropoda › Chelicerata › Arachnida › Acari › Parasitiformes › Ixodida › Ixodoidea › Ixodidae › Rhipicephalinae › Rhipicephalus › Rhipicephalus

Protein attributes

Sequence length	114 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Shows chemokine neutralizing activity. Binds to chemokines CCL3, CCL4 and CCL18. Ref.1 Ref.2
Subunit structure	Monomer. Ref.1
Subcellular location	Secreted Probable.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
PTM	Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20
	Chain	21 – 114	94	Evasin-1		PRO_0000354057
Amino acid modifications
	Glycosylation	39	1	N-linked (GlcNAc...) Potential
	Glycosylation	54	1	N-linked (GlcNAc...) Potential
	Glycosylation	62	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	P0C8E7-1 [UniParc]. Last modified November 25, 2008. Version 1. Checksum: 1CDFB331167EE2CF	FASTA	114	12,593
	10 20 30 40 50 60 MTFKACIAII TALCAMQVIC EDDEDYGDLG GCPFLVAENK TGYPTIVACK QDCNGTTETA 70 80 90 100 110 PNGTRCFSIG DEGLRRMTAN LPYDCPLGQC SNGDCIPKET YEVCYRRNWR DKKN

References

[1]

"Molecular cloning and characterization of a highly selective chemokine-binding protein from the tick Rhipicephalus sanguineus." Frauenschuh A., Power C.A., Deruaz M., Ferreira B.R., Silva J.S., Teixeira M.M., Dias J.M., Martin T., Wells T.N.C., Proudfoot A.E.I. J. Biol. Chem. 282:27250-27258(2007) [PubMed: 17640866] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, SUBUNIT, FUNCTION. Tissue: Salivary gland.

[2]

"Ticks produce highly selective chemokine binding proteins with antiinflammatory activity." Deruaz M., Frauenschuh A., Alessandri A.L., Dias J.M., Coelho F.M., Russo R.C., Ferreira B.R., Graham G.J., Shaw J.P., Wells T.N.C., Teixeira M.M., Power C.A., Proudfoot A.E.I. J. Exp. Med. 205:2019-2031(2008) [PubMed: 18678732] [Abstract] Cited for: FUNCTION.

Web resources

Protein Spotlight

Hidden powers - Issue 99 of November 2008

Cross-references

3D structure databases
ModBase	Search...
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

EVA1_RHISA

Accession

Primary (citable) accession number: P0C8E7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2008
Last sequence update:	November 25, 2008
Last modified:	June 16, 2009
This is version 4 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)