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 27-MAR-2024, entry version 70.
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; Mannose-Binding Protein A, subunit A; 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 PANTHER; PTHR22803:SF124; C-TYPE LECTIN DOMAIN FAMILY 19 MEMBER A-RELATED; 1.
DR PANTHER; PTHR22803; MANNOSE, PHOSPHOLIPASE, LECTIN RECEPTOR RELATED; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR PRINTS; PR01504; PNCREATITSAP.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 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
//
