ID   3SO1_HEMHA              Reviewed;          65 AA.
AC   C0HJT5;
DT   24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT   24-JUN-2015, sequence version 1.
DT   25-MAY-2022, entry version 18.
DE   RecName: Full=Ringhalexin {ECO:0000303|PubMed:27173146};
OS   Hemachatus haemachatus (Rinkhals) (Sepedon haemachatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Hemachatus.
OX   NCBI_TaxID=8626;
RN   [1] {ECO:0007744|PDB:4ZQY}
RP   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, SUBCELLULAR LOCATION,
RP   DISULFIDE BONDS, AND X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS).
RC   TISSUE=Venom;
RX   PubMed=27173146; DOI=10.1038/srep25935;
RA   Barnwal B., Jobichen C., Girish V.M., Foo C.S., Sivaraman J., Kini R.M.;
RT   "Ringhalexin from Hemachatus haemachatus: A novel inhibitor of extrinsic
RT   tenase complex.";
RL   Sci. Rep. 6:25935-25935(2016).
CC   -!- FUNCTION: Has anticoagulant activity, since it is able to inhibit the
CC       activation of coagulation factor X (F10) by coagulation factor VIIa
CC       (F7) (IC(50)=123.8 nM) (PubMed:27173146). Also shows weak irreversible
CC       neurotoxicity (PubMed:27173146). {ECO:0000269|PubMed:27173146}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27173146}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:27173146}.
CC   -!- MASS SPECTROMETRY: Mass=7437; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:27173146};
CC   -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC       subfamily. Orphan group I sub-subfamily. {ECO:0000305}.
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DR   PDB; 4ZQY; X-ray; 2.95 A; A/B/C=1-65.
DR   PDBsum; 4ZQY; -.
DR   AlphaFoldDB; C0HJT5; -.
DR   SMR; C0HJT5; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0044470; P:envenomation resulting in negative regulation of blood coagulation in another organism; IDA:UniProtKB.
DR   CDD; cd00206; snake_toxin; 1.
DR   Gene3D; 2.10.60.10; -; 1.
DR   InterPro; IPR003571; Snake_3FTx.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   InterPro; IPR018354; Snake_toxin_con_site.
DR   InterPro; IPR035076; Toxin/TOLIP.
DR   Pfam; PF00087; Toxin_TOLIP; 1.
DR   SUPFAM; SSF57302; SSF57302; 1.
DR   PROSITE; PS00272; SNAKE_TOXIN; 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   Neurotoxin; Secreted; Toxin.
FT   CHAIN           1..65
FT                   /note="Ringhalexin"
FT                   /evidence="ECO:0000269|PubMed:27173146"
FT                   /id="PRO_0000433406"
FT   DISULFID        3..24
FT                   /evidence="ECO:0000269|PubMed:27173146,
FT                   ECO:0007744|PDB:4ZQY"
FT   DISULFID        17..42
FT                   /evidence="ECO:0000269|PubMed:27173146,
FT                   ECO:0007744|PDB:4ZQY"
FT   DISULFID        46..57
FT                   /evidence="ECO:0000269|PubMed:27173146,
FT                   ECO:0007744|PDB:4ZQY"
FT   DISULFID        58..63
FT                   /evidence="ECO:0000269|PubMed:27173146,
FT                   ECO:0007744|PDB:4ZQY"
FT   STRAND          2..7
FT                   /evidence="ECO:0007829|PDB:4ZQY"
FT   STRAND          12..16
FT                   /evidence="ECO:0007829|PDB:4ZQY"
FT   STRAND          23..31
FT                   /evidence="ECO:0007829|PDB:4ZQY"
FT   STRAND          39..45
FT                   /evidence="ECO:0007829|PDB:4ZQY"
FT   STRAND          53..58
FT                   /evidence="ECO:0007829|PDB:4ZQY"
SQ   SEQUENCE   65 AA;  7446 MW;  4ECBBE1C032825C3 CRC64;
     RLCLSDYSIF SETIEICPEG HNYCFKKFPK GITRLPWVIR GCAATCPKPE AQVYVDCCAR
     DKCNR