ID   SL9A_ECHCA              Reviewed;         131 AA.
AC   Q9PSM9;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Snaclec coagulation factor IX/factor X-binding protein subunit A;
DE            Short=IX/X-BP subunit A;
DE   AltName: Full=ECLV IX/X-BP subunit A;
OS   Echis carinatus (Saw-scaled viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Echis.
OX   NCBI_TaxID=40353;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, DISULFIDE BONDS, SUBUNIT, SUBCELLULAR LOCATION,
RP   AND TISSUE SPECIFICITY.
RC   TISSUE=Venom;
RX   PubMed=8611513; DOI=10.1021/bi952520q;
RA   Chen Y.L., Tsai I.H.;
RT   "Functional and sequence characterization of coagulation factor IX/factor
RT   X-binding protein from the venom of Echis carinatus leucogaster.";
RL   Biochemistry 35:5264-5271(1996).
CC   -!- FUNCTION: Anticoagulant protein which binds to coagulation factor IX
CC       (F9) and coagulation factor X (F10) in the presence of calcium. It may
CC       bind the gamma-carboxyglutamic acid-domain regions of factors with a 1
CC       to 1 stoichiometry. The dissociation constant (K(d)) are 6.6 nM for
CC       factor IX (F9) and 125 nM for factor X (F10). Does not bind
CC       carbohydrates. {ECO:0000269|PubMed:8611513}.
CC   -!- SUBUNIT: Heterodimer of subunits A and B; disulfide-linked.
CC       {ECO:0000269|PubMed:8611513}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8611513}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:8611513}.
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR   AlphaFoldDB; Q9PSM9; -.
DR   SMR; Q9PSM9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   1: Evidence at protein level;
KW   Blood coagulation cascade inhibiting toxin; Calcium;
KW   Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW   Metal-binding; Secreted; Toxin.
FT   CHAIN           1..131
FT                   /note="Snaclec coagulation factor IX/factor X-binding
FT                   protein subunit A"
FT                   /id="PRO_0000415605"
FT   DOMAIN          1..131
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   BINDING         41
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         43
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         47
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   DISULFID        2..13
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:8611513"
FT   DISULFID        30..129
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:8611513"
FT   DISULFID        81
FT                   /note="Interchain (with C-75 in subunit B)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:8611513"
FT   DISULFID        104..121
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:8611513"
SQ   SEQUENCE   131 AA;  15439 MW;  B85E6C5CBF317E24 CRC64;
     DCLPGWSSHE GHCYKVFNEY KTWKDAEKFC KKQGKSGHLV SVESSEEGDF VAKLISENLE
     KSHSIDFVWT GLTYKGRWKQ CSSEWSDGSK IKYQKWGKQQ PRKCLGLEKQ TEFRKWVNLY
     CEEPQRFTCE I