ID   TAP_ORNMO               Reviewed;          60 AA.
AC   P17726;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Tick anticoagulant peptide;
DE            Short=TAP;
OS   Ornithodoros moubata (Soft tick) (Argasid tick).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Argasidae; Ornithodoros.
OX   NCBI_TaxID=6938;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=2333510; DOI=10.1126/science.2333510;
RA   Waxman L., Smith D.E., Arcuri K.E., Vlasuk G.P.;
RT   "Tick anticoagulant peptide (TAP) is a novel inhibitor of blood coagulation
RT   factor Xa.";
RL   Science 248:593-596(1990).
RN   [2]
RP   DISULFIDE BONDS.
RX   PubMed=1856193; DOI=10.1016/s0021-9258(18)92735-3;
RA   Sardana M., Sardana V., Rodkey J., Wood T., Ng A., Vlasuk G.P., Waxman L.;
RT   "Determination of disulfide bond pairs and stability in recombinant tick
RT   anticoagulant peptide.";
RL   J. Biol. Chem. 266:13560-13563(1991).
RN   [3]
RP   STRUCTURE BY NMR.
RX   PubMed=7925983; DOI=10.1016/0014-5793(94)00941-4;
RA   Antuch W., Guntert P., Billeter M., Hawthorne T., Grossenbacher H.,
RA   Wuethrich K.;
RT   "NMR solution structure of the recombinant tick anticoagulant protein
RT   (rTAP), a factor Xa inhibitor from the tick Ornithodoros moubata.";
RL   FEBS Lett. 352:251-257(1994).
RN   [4]
RP   STRUCTURE BY NMR.
RX   PubMed=7538849; DOI=10.1002/pro.5560040205;
RA   Lim-Wilby M.S.L., Hallenga K., de Maeyer M., Lasters I., Vlasuk G.P.,
RA   Brunck T.K.;
RT   "NMR structure determination of tick anticoagulant peptide (TAP).";
RL   Protein Sci. 4:178-186(1995).
CC   -!- FUNCTION: TAP is a slow, tight-binding inhibitor of blood coagulation,
CC       specific for factor Xa.
CC   -!- MISCELLANEOUS: The inhibition of factor Xa seems to be reversible and
CC       stoichiometric.
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DR   PIR; A41212; A41212.
DR   PDB; 1D0D; X-ray; 1.62 A; A=1-60.
DR   PDB; 1KIG; X-ray; 3.00 A; I=1-60.
DR   PDB; 1TAP; NMR; -; A=1-60.
DR   PDB; 1TCP; NMR; -; A=1-60.
DR   PDBsum; 1D0D; -.
DR   PDBsum; 1KIG; -.
DR   PDBsum; 1TAP; -.
DR   PDBsum; 1TCP; -.
DR   AlphaFoldDB; P17726; -.
DR   SMR; P17726; -.
DR   MINT; P17726; -.
DR   MEROPS; I52.001; -.
DR   EvolutionaryTrace; P17726; -.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.410.10; -; 1.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   SUPFAM; SSF57362; SSF57362; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Protease inhibitor; Serine protease inhibitor.
FT   CHAIN           1..60
FT                   /note="Tick anticoagulant peptide"
FT                   /id="PRO_0000155457"
FT   DOMAIN          5..59
FT                   /note="BPTI/Kunitz inhibitor"
FT   DISULFID        5..59
FT                   /evidence="ECO:0000269|PubMed:1856193"
FT   DISULFID        15..39
FT                   /evidence="ECO:0000269|PubMed:1856193"
FT   DISULFID        33..55
FT                   /evidence="ECO:0000269|PubMed:1856193"
FT   HELIX           3..5
FT                   /evidence="ECO:0007829|PDB:1D0D"
FT   TURN            11..14
FT                   /evidence="ECO:0007829|PDB:1TAP"
FT   HELIX           17..19
FT                   /evidence="ECO:0007829|PDB:1D0D"
FT   STRAND          22..27
FT                   /evidence="ECO:0007829|PDB:1D0D"
FT   STRAND          29..38
FT                   /evidence="ECO:0007829|PDB:1D0D"
FT   TURN            40..42
FT                   /evidence="ECO:0007829|PDB:1D0D"
FT   HELIX           52..59
FT                   /evidence="ECO:0007829|PDB:1D0D"
SQ   SEQUENCE   60 AA;  6985 MW;  700D3D1245E83099 CRC64;
     YNRLCIKPRD WIDECDSNEG GERAYFRNGK GGCDSFWICP EDHTGADYYS SYRDCFNACI