C5I2_RHIMP
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