C5IT3_RHISA
ID C5IT3_RHISA Reviewed; 111 AA.
AC P0DQV2;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 1.
DT 03-AUG-2022, entry version 1.
DE RecName: Full=Complement inhibitor CirpT3 {ECO:0000303|PubMed:31871188};
DE Flags: Precursor;
OS Rhipicephalus sanguineus (Brown dog tick) (Ixodes sanguineus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Rhipicephalinae;
OC Rhipicephalus; Rhipicephalus.
OX NCBI_TaxID=34632;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Salivary gland;
RX PubMed=20650005; DOI=10.1186/1471-2164-11-450;
RA Anatriello E., Ribeiro J.M., de Miranda-Santos I.K., Brandao L.G.,
RA Anderson J.M., Valenzuela J.G., Maruyama S.R., Silva J.S., Ferreira B.R.;
RT "An insight into the sialotranscriptome of the brown dog tick,
RT Rhipicephalus sanguineus.";
RL BMC Genomics 11:450-450(2010).
RN [2]
RP FUNCTION, AND RECOMBINANT EXPRESSION.
RC TISSUE=Salivary gland;
RX PubMed=31871188; DOI=10.1073/pnas.1909973116;
RA Reichhardt M.P., Johnson S., Tang T., Morgan T., Tebeka N., Popitsch N.,
RA Deme J.C., Jore M.M., Lea S.M.;
RT "An inhibitor of complement C5 provides structural insights into
RT activation.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:362-370(2020).
CC -!- FUNCTION: Complement inhibitor (PubMed:31871188). Prevents complement-
CC mediated activation of C5 by sterically preventing direct binding of C5
CC to its convertase (binding with domains MG4 and MG5) (PubMed:31871188)
CC (By similarity). Binds C5 at a different binding site than the other
CC tick complement inbibitors OmCI and RaCI3, and the drug eculizumab (By
CC similarity). Inhibits the complement in human, rat and guinea pig, and
CC also shows a reduced inhibition in rabbit and pig (By similarity).
CC {ECO:0000250|UniProtKB:L7MB58, ECO:0000269|PubMed:31871188}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:31871188}.
CC -!- TISSUE SPECIFICITY: Expressed by the salivary glands.
CC {ECO:0000305|PubMed:31871188}.
CC -!- SIMILARITY: Belongs to the CirpT 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; GT031647; -; NOT_ANNOTATED_CDS; mRNA.
PE 3: Inferred from homology;
KW Disulfide bond; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..111
FT /note="Complement inhibitor CirpT3"
FT /id="PRO_0000456234"
FT DISULFID 40..64
FT /evidence="ECO:0000250|UniProtKB:L7MB58"
FT DISULFID 59..98
FT /evidence="ECO:0000250|UniProtKB:L7MB58"
FT DISULFID 76..99
FT /evidence="ECO:0000250|UniProtKB:L7MB58"
FT DISULFID 85..104
FT /evidence="ECO:0000250|UniProtKB:L7MB58"
SQ SEQUENCE 111 AA; 11896 MW; C7D6BCF726909AED CRC64;
MRTLGVSLFV LVGISAVYCD VQERGHTYVT KNVTVENGAC VFERNVIPDG ETKALNSPCV
LSTCYAADRK VNSTLCPNFG VAEGCHVEWT PDGEYPNCCP KHVCPAAPAT S