ID   SLA_GLOHA               Reviewed;         121 AA.
AC   Q7SZV0;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Snaclec coagulation factor IX-binding protein subunit A;
DE            Short=IX-bp subunit A;
DE   Flags: Fragment;
OS   Gloydius halys (Chinese water mocassin) (Agkistrodon halys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX   NCBI_TaxID=8714;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Zang J., Teng M., Niu L.;
RT   "Crystal structure of AHP IX-bp at pH 6.5 and 7.5 and implications for the
RT   pH-dependent mechanism of AHP IX-bp binding to coagulation factor IX.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Anticoagulant protein which binds to the gamma-
CC       carboxyglutamic acid-domain regions of factor IX (F9) (but not factor
CC       X) in the presence of calcium with a 1 to 1 stoichiometry.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of subunits A and B; disulfide-linked.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR   EMBL; AY356354; AAQ18640.1; -; mRNA.
DR   EMBL; AY346127; AAQ24215.1; -; mRNA.
DR   AlphaFoldDB; Q7SZV0; -.
DR   SMR; Q7SZV0; -.
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   2: Evidence at transcript level;
KW   Blood coagulation cascade inhibiting toxin; Calcium; Disulfide bond;
KW   Hemostasis impairing toxin; Metal-binding; Secreted; Toxin.
FT   CHAIN           <1..121
FT                   /note="Snaclec coagulation factor IX-binding protein
FT                   subunit A"
FT                   /id="PRO_0000355237"
FT   DOMAIN          1..120
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   BINDING         33
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         35
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         39
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   DISULFID        22..119
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        71
FT                   /note="Interchain (with C-98 in subunit B)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        94..111
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   NON_TER         1
SQ   SEQUENCE   121 AA;  13883 MW;  FF7C84DD6A4E4765 CRC64;
     YEGHCYQTFK LFKTWADAES FCTEQAKGGH LVSIESDGEA DFVAQLVAEN IQKTEIYVWV
     GLRVQGKEQQ CSSEWSDGSS VSYQNWIEAE SKTCLGLQKE TEFRKWFNIY CGERNPFVCE
     A