ID   C5IT2_DERAN             Reviewed;         108 AA.
AC   P0DQV1;
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 CirpT2 {ECO:0000303|PubMed:31871188};
DE   Flags: Precursor;
OS   Dermacentor andersoni (Rocky mountain wood tick).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Rhipicephalinae; Dermacentor.
OX   NCBI_TaxID=34620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Salivary gland;
RX   PubMed=17175446; DOI=10.1016/j.ibmb.2006.10.002;
RA   Alarcon-Chaidez F.J., Sun J., Wikel S.K.;
RT   "Transcriptome analysis of the salivary glands of Dermacentor andersoni
RT   Stiles (Acari: Ixodidae).";
RL   Insect Biochem. Mol. Biol. 37:48-71(2007).
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}.
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DR   EMBL; EG363688; -; 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..108
FT                   /note="Complement inhibitor CirpT2"
FT                   /id="PRO_0000456233"
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   108 AA;  11747 MW;  B2C7912816D74194 CRC64;
     MRTLVASLCV FAVFSAVCCD VQERGHTYRT RNVTVEDGAC VFERNVIPDG ETKALNSPCV
     LSTCYAAARE VNSTLCPNIG VEQGCRVEWT PVGEYPNCCP KHVCPTTS