THBI_RHOPR
ID THBI_RHOPR Reviewed; 103 AA.
AC Q06684;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Thrombin inhibitor rhodniin {ECO:0000303|PubMed:8344906};
OS Rhodnius prolixus (Triatomid bug).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC Cimicomorpha; Reduviidae; Triatominae; Rhodnius.
OX NCBI_TaxID=13249;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-25, FUNCTION, AND
RP 3D-STRUCTURE MODELING.
RX PubMed=8344906; DOI=10.1016/s0021-9258(19)85408-x;
RA Friedrich T., Kroeger B., Bialojan S., Lemaire H.G., Hoeffken H.W.,
RA Reuschenbach P., Otte M., Dodt J.;
RT "A Kazal-type inhibitor with thrombin specificity from Rhodnius prolixus.";
RL J. Biol. Chem. 268:16216-16222(1993).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=7489704;
RA van de Locht A., Lamba D., Bauer M., Huber R., Friedrich T., Kroeger B.,
RA Hoeffken H.W., Bode W.;
RT "Two heads are better than one: crystal structure of the insect derived
RT double domain Kazal inhibitor rhodniin in complex with thrombin.";
RL EMBO J. 14:5149-5157(1995).
CC -!- FUNCTION: Thrombin-specific inhibitor. Appears to form 1:1 complexes
CC with thrombin. Prevents blood clotting to allow the insect to feed on
CC blood.
CC -!- SUBCELLULAR LOCATION: Secreted.
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DR EMBL; Z22559; CAA80281.1; -; mRNA.
DR PIR; A47337; A47337.
DR PDB; 1TBQ; X-ray; 3.10 A; R/S=1-103.
DR PDB; 1TBR; X-ray; 2.60 A; R/S=1-103.
DR PDBsum; 1TBQ; -.
DR PDBsum; 1TBR; -.
DR AlphaFoldDB; Q06684; -.
DR SMR; Q06684; -.
DR MEROPS; I01.019; -.
DR MEROPS; I01.031; -.
DR EvolutionaryTrace; Q06684; -.
DR Proteomes; UP000015103; Unassembled WGS sequence.
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 InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR039932; Spink4-like.
DR PANTHER; PTHR21179; PTHR21179; 2.
DR Pfam; PF00050; Kazal_1; 1.
DR Pfam; PF07648; Kazal_2; 1.
DR SMART; SM00280; KAZAL; 2.
DR SUPFAM; SSF100895; SSF100895; 2.
DR PROSITE; PS00282; KAZAL_1; 1.
DR PROSITE; PS51465; KAZAL_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Blood coagulation; Direct protein sequencing; Disulfide bond;
KW Hemostasis; Protease inhibitor; Reference proteome; Repeat; Secreted;
KW Serine protease inhibitor.
FT CHAIN 1..103
FT /note="Thrombin inhibitor rhodniin"
FT /evidence="ECO:0000305|PubMed:8344906"
FT /id="PRO_0000073198"
FT DOMAIN 1..50
FT /note="Kazal-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 51..103
FT /note="Kazal-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 10..11
FT /note="Reactive bond"
FT DISULFID 6..31
FT /evidence="ECO:0000269|PubMed:7489704,
FT ECO:0007744|PDB:1TBQ, ECO:0007744|PDB:1TBR"
FT DISULFID 8..27
FT /evidence="ECO:0000269|PubMed:7489704,
FT ECO:0007744|PDB:1TBQ, ECO:0007744|PDB:1TBR"
FT DISULFID 16..48
FT /evidence="ECO:0000269|PubMed:7489704,
FT ECO:0007744|PDB:1TBQ, ECO:0007744|PDB:1TBR"
FT DISULFID 57..84
FT /evidence="ECO:0000269|PubMed:7489704,
FT ECO:0007744|PDB:1TBQ, ECO:0007744|PDB:1TBR"
FT DISULFID 60..80
FT /evidence="ECO:0000269|PubMed:7489704,
FT ECO:0007744|PDB:1TBQ, ECO:0007744|PDB:1TBR"
FT DISULFID 69..101
FT /evidence="ECO:0000269|PubMed:7489704,
FT ECO:0007744|PDB:1TBQ, ECO:0007744|PDB:1TBR"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:1TBR"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:1TBR"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:1TBR"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:1TBR"
FT HELIX 26..33
FT /evidence="ECO:0007829|PDB:1TBR"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:1TBR"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:1TBR"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:1TBR"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1TBR"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:1TBR"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:1TBR"
FT HELIX 79..85
FT /evidence="ECO:0007829|PDB:1TBR"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:1TBR"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:1TBR"
SQ SEQUENCE 103 AA; 11079 MW; F9588330458836B3 CRC64;
EGGEPCACPH ALHRVCGSDG ETYSNPCTLN CAKFNGKPEL VKVHDGPCEP DEDEDVCQEC
DGDEYKPVCG SDDITYDNNC RLECASISSS PGVELKHEGP CRT
