TRIA_MECPA
ID TRIA_MECPA Reviewed; 160 AA.
AC Q27049; Q27046; Q27047; Q27048;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Triabin {ECO:0000303|PubMed:7499380, ECO:0000303|PubMed:9342325};
DE AltName: Full=Thrombin inhibitor {ECO:0000303|PubMed:7499380, ECO:0000303|PubMed:9342325};
DE Flags: Precursor;
OS Meccus pallidipennis (Triatomine bug) (Triatoma pallidipennis).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC Cimicomorpha; Reduviidae; Triatominae; Meccus.
OX NCBI_TaxID=30077;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RC TISSUE=Salivary gland;
RX PubMed=7499380; DOI=10.1074/jbc.270.48.28629;
RA Noeske-Jungblut C., Haendler B., Donner P., Alagon A., Possani L.D.,
RA Schleuning W.-D.;
RT "Triabin, a highly potent exosite inhibitor of thrombin.";
RL J. Biol. Chem. 270:28629-28634(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH THROMBIN, AND
RP DISULFIDE BONDS.
RX PubMed=9342325; DOI=10.1073/pnas.94.22.11845;
RA Fuentes-Prior P., Noeske-Jungblut C., Donner P., Schleuning W.-D.,
RA Huber R., Bode W.;
RT "Structure of the thrombin complex with triabin, a lipocalin-like exosite-
RT binding inhibitor derived from a triatomine bug.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:11845-11850(1997).
CC -!- FUNCTION: Thrombin inhibitor, forms a non-covalent complex with
CC thrombin at a molar ratio of 1:1, inhibits thrombin-induced platelet
CC aggregation, and prolongs thrombin clotting time and activated partial
CC thromboplastin time. It only minimally suppresses the amidolytic
CC activity of thrombin. {ECO:0000269|PubMed:7499380}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:7499380}.
CC -!- TISSUE SPECIFICITY: Expressed in salivary glands.
CC {ECO:0000305|PubMed:7499380}.
CC -!- MISCELLANEOUS: The sequence shown is that of clone TR5.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Triabin family.
CC {ECO:0000305}.
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DR EMBL; X80246; CAA56540.1; -; mRNA.
DR EMBL; X80247; CAA56541.1; -; mRNA.
DR EMBL; X80248; CAA56542.1; -; mRNA.
DR EMBL; X80249; CAA56543.1; -; mRNA.
DR PDB; 1AVG; X-ray; 2.60 A; I=19-160.
DR PDBsum; 1AVG; -.
DR AlphaFoldDB; Q27049; -.
DR SMR; Q27049; -.
DR DIP; DIP-6100N; -.
DR IntAct; Q27049; 1.
DR MEROPS; I59.001; -.
DR EvolutionaryTrace; Q27049; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0030682; P:mitigation of host defenses by symbiont; IEA:InterPro.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR005657; Triabi/Procalin.
DR Pfam; PF03973; Triabin; 1.
DR SUPFAM; SSF50814; SSF50814; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Blood coagulation cascade inhibiting toxin;
KW Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW Protease inhibitor; Secreted; Serine protease inhibitor; Signal; Toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000305|PubMed:7499380"
FT CHAIN 19..160
FT /note="Triabin"
FT /evidence="ECO:0000305|PubMed:7499380"
FT /id="PRO_0000017994"
FT DISULFID 24..128
FT /evidence="ECO:0000269|PubMed:9342325,
FT ECO:0007744|PDB:1AVG"
FT DISULFID 57..160
FT /evidence="ECO:0000269|PubMed:9342325,
FT ECO:0007744|PDB:1AVG"
FT DISULFID 87..102
FT /evidence="ECO:0000269|PubMed:9342325,
FT ECO:0007744|PDB:1AVG"
FT VARIANT 26
FT /note="I -> L (in clones TR12, TR28 and TR45)"
FT VARIANT 50
FT /note="G -> D (in clones TR28 and TR45)"
FT VARIANT 90..95
FT /note="VDNKNG -> ADKKND (in clone TR45)"
FT VARIANT 95
FT /note="G -> D (in clones TR12 and TR28)"
FT VARIANT 104
FT /note="S -> G (in clones TR12, TR28 and TR45)"
FT VARIANT 132
FT /note="T -> I (in clones TR12 and TR28)"
FT VARIANT 145
FT /note="L -> F (in clones TR12, TR28 and TR45)"
FT VARIANT 157
FT /note="K -> N (in clones TR12, TR28 and TR45)"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:1AVG"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:1AVG"
FT STRAND 39..50
FT /evidence="ECO:0007829|PDB:1AVG"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:1AVG"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1AVG"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:1AVG"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:1AVG"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:1AVG"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:1AVG"
FT STRAND 110..119
FT /evidence="ECO:0007829|PDB:1AVG"
FT STRAND 123..136
FT /evidence="ECO:0007829|PDB:1AVG"
FT STRAND 140..148
FT /evidence="ECO:0007829|PDB:1AVG"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:1AVG"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:1AVG"
SQ SEQUENCE 160 AA; 17860 MW; 7DB62819F7C4406A CRC64;
MKTIIAVTIF GILTCAYAAE GDDCSIEKAM GDFKPEEFFN GTWYLAHGPG VTSPAVCQKF
TTSGSKGFTQ IVEIGYNKFE SNVKFQCNQV DNKNGEQYSF KCKSSDNTEF EADFTFISVS
YDNFALVCRS ITFTSQPKED DYLVLERTKS DTDPDAKEIC
