ID   C5IT1_RHIPC             Reviewed;         111 AA.
AC   L7MB58;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   03-AUG-2022, sequence version 2.
DT   03-AUG-2022, entry version 16.
DE   RecName: Full=Complement inhibitor CirpT1 {ECO:0000303|PubMed:31871188};
DE   AltName: Full=Complement inhibitor from Rhipicephalus pulchellus of the terminal pathway 1 {ECO:0000303|PubMed:31871188};
DE   Flags: Precursor;
OS   Rhipicephalus pulchellus (Yellow backed tick) (Dermacentor pulchellus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Rhipicephalinae;
OC   Rhipicephalus; Rhipicephalus.
OX   NCBI_TaxID=72859;
RN   [1] {ECO:0000312|EMBL:JAA61486.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Salivary gland;
RX   PubMed=25576852; DOI=10.1016/j.jprot.2014.12.014;
RA   Tan A.W., Francischetti I.M., Slovak M., Kini R.M., Ribeiro J.M.;
RT   "Sexual differences in the sialomes of the zebra tick, Rhipicephalus
RT   pulchellus.";
RL   J. Proteomics 117:120-144(2015).
RN   [2] {ECO:0007744|PDB:6RPT, ECO:0007744|PDB:6RQJ}
RP   X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 20-111 IN COMPLEX WITH HUMAN
RP   COMPLEMENT C5 AND THE TICK COMPLEMENT INHBIBITORS OMCI AND RACI1, STRUCTURE
RP   BY ELECTRON MICROSCOPY (3.5 ANGSTROMS) OF 24-105 IN COMPLEX WITH HUMAN
RP   COMPLEMENT C5, FUNCTION, DISULFIDE BONDS, 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       Binds C5 at a different binding site than the other tick complement
CC       inbibitors OmCI and RaCI3, and the drug eculizumab (PubMed:31871188).
CC       Inhibits the complement in human, rat and guinea pig, and also shows a
CC       reduced inhibition in rabbit and pig (PubMed:31871188).
CC       {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}.
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DR   EMBL; GACK01003548; JAA61486.1; -; mRNA.
DR   PDB; 6RPT; X-ray; 2.70 A; B/D/F=20-111.
DR   PDB; 6RQJ; EM; 3.50 A; E=24-105.
DR   PDBsum; 6RPT; -.
DR   PDBsum; 6RQJ; -.
DR   SMR; L7MB58; -.
DR   InterPro; IPR029277; SVWC_dom.
DR   Pfam; PF15430; SVWC; 1.
DR   SMART; SM01318; SVWC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250|UniProtKB:P0DQV1"
FT   CHAIN           20..111
FT                   /note="Complement inhibitor CirpT1"
FT                   /id="PRO_0000456232"
FT   DISULFID        40..64
FT                   /evidence="ECO:0000269|PubMed:31871188,
FT                   ECO:0007744|PDB:6RPT, ECO:0007744|PDB:6RQJ"
FT   DISULFID        59..98
FT                   /evidence="ECO:0000269|PubMed:31871188,
FT                   ECO:0007744|PDB:6RPT, ECO:0007744|PDB:6RQJ"
FT   DISULFID        76..99
FT                   /evidence="ECO:0000269|PubMed:31871188,
FT                   ECO:0007744|PDB:6RPT, ECO:0007744|PDB:6RQJ"
FT   DISULFID        85..104
FT                   /evidence="ECO:0000269|PubMed:31871188,
FT                   ECO:0007744|PDB:6RPT, ECO:0007744|PDB:6RQJ"
FT   UNSURE          1
FT                   /evidence="ECO:0000305"
FT   CONFLICT        20..22
FT                   /note="EVR -> DVQ (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   111 AA;  12122 MW;  5E8889E31E2A1E02 CRC64;
     MATLIAARTK RKAPRVRIFE VRERGHTYVT KNVTVEDGAC VYLRNVIPNG ETKALNNPCV
     LSTCYAADRK VNSTLCPNIG VDEGCHVEWT PDGVYPNCCP KHVCPSATAS S