TCI1_RHIBU
ID TCI1_RHIBU Reviewed; 97 AA.
AC Q5EPH2;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=Carboxypeptidase inhibitor;
DE AltName: Full=TCI;
DE Flags: Precursor;
OS Rhipicephalus bursa (Tick).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Rhipicephalinae;
OC Rhipicephalus; Rhipicephalus.
OX NCBI_TaxID=67831;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAW72225.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-52, FUNCTION, AND MASS
RP SPECTROMETRY.
RX PubMed=15561703; DOI=10.1074/jbc.m411086200;
RA Arolas J.L., Lorenzo J., Rovira A., Castella J., Aviles F.X.,
RA Sommerhoff C.P.;
RT "A carboxypeptidase inhibitor from the tick Rhipicephalus bursa. Isolation,
RT cDNA cloning, recombinant expression, and characterization.";
RL J. Biol. Chem. 280:3441-3448(2005).
CC -!- FUNCTION: Potent competitive inhibitor of metallo-carboxypeptidases
CC CPA1, CPA2, CPB, CPN and TAF1a. Accelerates fibrinolysis in vitro and
CC may contribute to the maintenance of host blood liquidity during
CC feeding. {ECO:0000269|PubMed:15561703}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- MASS SPECTROMETRY: Mass=7798; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15561703};
CC -!- SIMILARITY: Belongs to the protease inhibitor I68 family.
CC {ECO:0000305}.
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DR EMBL; AY794405; AAW72225.1; -; mRNA.
DR PDB; 1ZLH; X-ray; 1.70 A; B=23-97.
DR PDB; 1ZLI; X-ray; 2.09 A; B=23-97.
DR PDB; 2JTO; NMR; -; A=23-97.
DR PDB; 2K2X; NMR; -; A=23-97.
DR PDB; 2K2Y; NMR; -; A=23-61.
DR PDB; 2K2Z; NMR; -; A=59-97.
DR PDB; 3D4U; X-ray; 1.70 A; B=23-96.
DR PDB; 3LMS; X-ray; 2.50 A; B=23-96.
DR PDB; 3OSL; X-ray; 6.00 A; B/D=23-96.
DR PDBsum; 1ZLH; -.
DR PDBsum; 1ZLI; -.
DR PDBsum; 2JTO; -.
DR PDBsum; 2K2X; -.
DR PDBsum; 2K2Y; -.
DR PDBsum; 2K2Z; -.
DR PDBsum; 3D4U; -.
DR PDBsum; 3LMS; -.
DR PDBsum; 3OSL; -.
DR AlphaFoldDB; Q5EPH2; -.
DR BMRB; Q5EPH2; -.
DR SMR; Q5EPH2; -.
DR MEROPS; I68.001; -.
DR EvolutionaryTrace; Q5EPH2; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:UniProtKB.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0044002; P:acquisition of nutrients from host; IDA:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.20.20.10; -; 1.
DR InterPro; IPR019509; Carboxypeptidase_inhibitor_I68.
DR InterPro; IPR023355; Myo_ane_neurotoxin_sf.
DR Pfam; PF10468; Inhibitor_I68; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Blood coagulation; Direct protein sequencing; Fibrinolysis;
KW Hemostasis; Metalloenzyme inhibitor; Metalloprotease inhibitor;
KW Protease inhibitor; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:15561703"
FT CHAIN 23..97
FT /note="Carboxypeptidase inhibitor"
FT /evidence="ECO:0000269|PubMed:15561703"
FT /id="PRO_0000227529"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:1ZLH"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:1ZLH"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:1ZLH"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:1ZLH"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1ZLH"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1ZLH"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1ZLH"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:1ZLH"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:3LMS"
FT HELIX 80..86
FT /evidence="ECO:0007829|PDB:1ZLH"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:1ZLH"
SQ SEQUENCE 97 AA; 10189 MW; 22A8B710821B0C0E CRC64;
MAATLPVFAV VFFAMVLASS QANECVSKGF GCLPQSDCPQ EARLSYGGCS TVCCDLSKLT
GCKGKGGECN PLDRQCKELQ AESASCGKGQ KCCVWLH
