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SLB_GLOHA
ID   SLB_GLOHA               Reviewed;         146 AA.
AC   Q9DG31; Q6V9X3;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Snaclec coagulation factor IX/factor X-binding protein subunit B;
DE            Short=IX/X-bp subunit B;
DE   AltName: Full=Halyxin subunit B;
DE   Flags: Precursor;
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   Koo B.H., Sohn Y.D., Kim D.S., Jang Y.S., Chung K.H.;
RT   "A novel coagulation factor Xa inhibitor from Korean snake (Agkistrodon
RT   halys) venom.";
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 32-146.
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: When linked to subunit A of IX/X-bp, anticoagulant protein
CC       which binds to the gamma-carboxyglutamic acid-domain regions of factors
CC       IX (F9) and factor X (F10) in the presence of calcium with a 1 to 1
CC       stoichiometry. {ECO:0000250}.
CC   -!- FUNCTION: When linked to subunit A of IX-bp, anticoagulant protein
CC       which binds to the gamma-carboxyglutamic acid-domain regions of factor
CC       IX (but not to factor X) in the presence of calcium with a 1 to 1
CC       stoichiometry. {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer with subunit A of IX/X-bp or IX-bp; disulfide-
CC       linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: Calcium is required for ligand binding. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR   EMBL; AF197915; AAG28522.1; -; mRNA.
DR   EMBL; AY346128; AAQ24216.1; -; mRNA.
DR   AlphaFoldDB; Q9DG31; -.
DR   SMR; Q9DG31; -.
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; Signal; Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..146
FT                   /note="Snaclec coagulation factor IX/factor X-binding
FT                   protein subunit B"
FT                   /id="PRO_5000057261"
FT   DOMAIN          32..143
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   BINDING         64
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         70
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   DISULFID        25..36
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        53..142
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        98
FT                   /note="Interchain (with C-102 in subunit A of IX/X-bp or
FT                   with C-71 in subunit A of IX-bp)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        119..134
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   CONFLICT        43
FT                   /note="Q -> P (in Ref. 2; AAQ24216)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        99
FT                   /note="S -> N (in Ref. 2; AAQ24216)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        104
FT                   /note="S -> N (in Ref. 2; AAQ24216)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   146 AA;  16841 MW;  C47D8A43B0A00709 CRC64;
     MGRFIFLSFG LLVVFLSLSG TGADCPSGWS SYEGHCYKPF NEQKNWADAE NFCTQQHTGG
     HLVSFHSTEE ADFVVKLAFQ NFGHGIFWMG LSNVWNQCSW QWSSAAKLKY EAWAEESYCV
     YFKSTNNKWR SRACRMEAYF VCEFQA
 
 
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