ID C5I2_RHIMP Reviewed; 98 AA. AC A0A158RFT4; A0A182DWE4; DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot. DT 03-AUG-2022, sequence version 2. DT 03-AUG-2022, entry version 13. DE RecName: Full=Complement inhibitor RaCI2 {ECO:0000303|PubMed:27018802}; DE Flags: Precursor; OS Rhipicephalus microplus (Cattle tick) (Boophilus microplus). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari; OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Rhipicephalinae; OC Rhipicephalus; Boophilus. OX NCBI_TaxID=6941; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Salivary gland; RX PubMed=20298599; DOI=10.1186/1471-2164-11-186; RA Zivkovic Z., Esteves E., Almazan C., Daffre S., Nijhof A.M., Kocan K.M., RA Jongejan F., de la Fuente J.; RT "Differential expression of genes in salivary glands of male Rhipicephalus RT (Boophilus)microplus in response to infection with Anaplasma marginale."; RL BMC Genomics 11:186-186(2010). RN [2] {ECO:0000312|PDB:5HCD, ECO:0000312|PDB:5IEC} RP X-RAY CRYSTALLOGRAPHY (2.98 ANGSTROMS) OF 22-98 IN COMPLEX WITH HUMAN RP COMPLEMENT C5 AND THE TICK COMPLEMENT INHBIBITOR OMCI, STRUCTURE BY NMR OF RP 22-88, FUNCTION, DISULFIDE BONDS, AND MUTAGENESIS OF 22-GLU--VAL-31 AND RP 87-THR--GLU-98. RC TISSUE=Salivary gland; RX PubMed=27018802; DOI=10.1038/nsmb.3196; RA Jore M.M., Johnson S., Sheppard D., Barber N.M., Li Y.I., Nunn M.A., RA Elmlund H., Lea S.M.; RT "Structural basis for therapeutic inhibition of complement C5."; RL Nat. Struct. Mol. Biol. 23:378-386(2016). CC -!- FUNCTION: Complement inhibitor (PubMed:27018802). Prevents complement- CC mediated C5 activation by binding to C5 (PubMed:27018802). Binds C5 at CC a different binding site than the other tick complement inbibitors OmCI CC and CirpT1, and the drug eculizumab (By similarity). CC {ECO:0000250|UniProtKB:A0A146B485, ECO:0000269|PubMed:27018802}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:27018802}. CC -!- TISSUE SPECIFICITY: Expressed by salivary glands. CC {ECO:0000305|PubMed:27018802}. CC -!- SIMILARITY: Belongs to the RaCI family. {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; GO496246; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GO496255; -; NOT_ANNOTATED_CDS; mRNA. DR PDB; 5HCD; X-ray; 2.98 A; D=22-98. DR PDB; 5IEC; NMR; -; A=22-88. DR PDBsum; 5HCD; -. DR PDBsum; 5IEC; -. DR BMRB; A0A158RFT4; -. DR SMR; A0A158RFT4; -. PE 1: Evidence at protein level; KW 3D-structure; Complement system impairing toxin; Disulfide bond; Secreted; KW Signal; Toxin. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..98 FT /note="Complement inhibitor RaCI2" FT /id="PRO_0000456230" FT DISULFID 35..59 FT /evidence="ECO:0000269|PubMed:27018802, FT ECO:0007744|PDB:5HCD, ECO:0007744|PDB:5IEC" FT DISULFID 40..61 FT /evidence="ECO:0000269|PubMed:27018802, FT ECO:0007744|PDB:5HCD, ECO:0007744|PDB:5IEC" FT DISULFID 55..76 FT /evidence="ECO:0000269|PubMed:27018802, FT ECO:0007744|PDB:5HCD, ECO:0007744|PDB:5IEC" FT MUTAGEN 22..31 FT /note="Missing: No change in activity." FT /evidence="ECO:0000269|PubMed:27018802" FT MUTAGEN 87..98 FT /note="Missing: No change in activity." FT /evidence="ECO:0000269|PubMed:27018802" SQ SEQUENCE 98 AA; 10633 MW; 14B6E2D09FD3AACF CRC64; MNAVTVLAFT AFALIVHDCY SEEANTTPIS VKDQCANVTC RRTVDNRGKR HIDGCPPGCL CVLKGPDSKD NLDGTCYLLA TTPKSTTTST EQSFNMEE //